Journal articles: 'PIAS'

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Kotaja, Noora, Saara Aittomäki, Olli Silvennoinen, Jorma J. Palvimo, and Olli A. Jänne. "ARIP3 (Androgen Receptor-Interacting Protein 3) and Other PIAS (Protein Inhibitor of Activated STAT) Proteins Differ in Their Ability to Modulate Steroid Receptor-Dependent Transcriptional Activation." Molecular Endocrinology 14, no. 12 (December 1, 2000): 1986–2000. http://dx.doi.org/10.1210/mend.14.12.0569.

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Abstract Steroid receptors mediate their actions by using various coregulatory proteins. We have recently characterized ARIP3/PIASxα as an androgen receptor (AR)-interacting protein (ARIP) that belongs to the PIAS [protein inhibitor of activated STAT (signal transducer and activator of transcription)] protein family implicated in the inhibition of cytokine signaling. We have analyzed herein the roles that four different PIAS proteins (ARIP3/PIASxα, Miz1/PIASxβ, GBP/PIAS1, and PIAS3) play in the regulation of steroid receptor- or STAT-mediated transcriptional activation. All PIAS proteins are able to coactivate steroid receptor-dependent transcription but to a differential degree, depending on the receptor, the promoter, and the cell type. Miz1 and PIAS1 are more potent than ARIP3 in activating AR function on minimal promoters. With the natural probasin promoter, PIAS proteins influence AR function more divergently, in that ARIP3 represses, but Miz1 and PIAS1 activate it. Miz1 and PIAS1 possess inherent transcription activating function, whereas ARIP3 and PIAS3 are devoid of this feature. ARIP3 enhances glucocorticoid receptor-dependent transcription more efficiently than Miz1 or PIAS1, and all PIAS proteins also activate estrogen receptor- and progesterone receptor-dependent transcription but to a dissimilar degree. The same amounts of PIAS proteins that modulate steroid receptor-dependent transcription influence only marginally transactivation mediated by various STAT proteins. It remains to be established whether the PIAS proteins play a more significant physiological role in steroid receptor than in cytokine signaling.

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Tirard, M., J. Jasbinsek, OF Almeida, and TM Michaelidis. "The manifold actions of the protein inhibitor of activated STAT proteins on the transcriptional activity of mineralocorticoid and glucocorticoid receptors in neural cells." Journal of Molecular Endocrinology 32, no. 3 (June 1, 2004): 825–41. http://dx.doi.org/10.1677/jme.0.0320825.

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Corticosteroid actions in the brain are exerted via the mineralocorticoid receptor (MR) and glucocorticoid receptor (GR). These receptors share several structural and functional similarities but their activation in the brain triggers distinct biological actions, for instance on neuronal survival or the regulation of the hypothalamo-pituitary-adrenal axis. Like other hormone-activated receptors, the transcriptional properties of the MR and GR depend on their ability to recruit a variety of co-regulators, which modulate their activity on target promoters, in a specific manner. The N-terminal regions of the MR and GR share the smallest degree of sequence conservation, whereas they display opposite effects on the transactivation properties of these receptors; thus, they may provide surfaces suitable for receptorspecific interactions with co-regulatory proteins. Here, we employed a yeast two-hybrid system to identify molecules interacting with the N-terminal part of the MR (amino acids 170-433). This approach resulted in the isolation of representative cDNAs from all members of the protein inhibitor of activated STAT (PIAS) family of proteins as potential MR-interacting partners. In neural cells, PIAS3 exhibited a strong and specific interaction with MR, but not GR, as indicated by mammalian two-hybrid assays and co-immunoprecipitation experiments in vivo. The interaction with MR was enhanced in the presence of aldosterone, an MR agonist, and was found to occur through a conserved, serine- and acidic amino acid residue-rich domain of PIAS3. To compare the modulatory properties of PIAS proteins on MR and GR transcriptional activity in a neural environment, MMTV reporter gene assays were performed in the human neuroblastoma cell line SK-N-MC. This analysis revealed that PIAS3 can inhibit MR, but not GR, transactivation in response to their corresponding ligands. Further, it showed that PIAS1 and PIASxbeta, but not PIASy, could also inhibit MR-mediated transcription despite the lack of detected physical interaction with MR. Interestingly, PIASxbeta and PIASy dose-dependently co-activated GR, whereas PIAS1 impaired GR-induced transcription. Taken together the results reveal differential modulatory roles of the PIAS proteins on the transcriptional properties of MR and GR, thus providing new insights into the bifurcating actions of these two receptors in neural cells where they are frequently co-localized.

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Wong, Kelly A., Rachel Kim, Heather Christofk, Jing Gao, Gregory Lawson, and Hong Wu. "Protein Inhibitor of Activated STAT Y (PIASy) and a Splice Variant Lacking Exon 6 Enhance Sumoylation but Are Not Essential for Embryogenesis and Adult Life." Molecular and Cellular Biology 24, no. 12 (June 15, 2004): 5577–86. http://dx.doi.org/10.1128/mcb.24.12.5577-5586.2004.

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ABSTRACT Protein inhibitor of activated STAT Y (PIASy) is the shortest member of the PIAS family and has been reported to modulate the transcriptional activities of STAT1, lymphoid enhancer factor 1 (LEF-1), and the androgen receptor. PIAS proteins have also been identified as E3 ligases for the small ubiquitin-like modifier (SUMO) proteins. PIASy in particular has been reported to mediate SUMO-2/3 modification of LEF-1, sequestering it into nuclear bodies, and SUMO-1 ligation to c-Myb, modulating its transcriptional activation properties. We have cloned murine Piasy and a splice variant which omits exon 6, containing the nuclear retention PINIT motif. Cell culture studies indicate that both the full length and the splice variant are localized in the nucleus but differentially enhance SUMO ligation. To further understand the functions of PIASy, we have generated PIASy-deficient mice. Surprisingly, Piasy−/− mice appear phenotypically normal. Activation of STAT1 is not significantly perturbed in Piasy−/− cells, and sumoylation patterns for SUMO-1 or SUMO-3 modification are similar when comparing tissues and embryonic fibroblasts from wild-type and knockout mice. Our study demonstrates that at steady state, PIASy is either dispensable or compensated for by other PIAS family members or by other mechanisms when deleted.

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Brayman, Melissa Jo, Neeraja Dharmaraj, Errin Lagow, and Daniel D. Carson. "MUC1 Expression Is Repressed by Protein Inhibitor of Activated Signal Transducer and Activator of Transcription-y." Molecular Endocrinology 21, no. 11 (November 1, 2007): 2725–37. http://dx.doi.org/10.1210/me.2006-0539.

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Abstract Mucin 1 (MUC1) is a transmembrane glycoprotein that modulates the interaction between the embryo and the uterine epithelial cell surface. MUC1 also is a tumor marker and has been implicated in the protection of cancer cells from immune cell attack as well as in cell signaling in some tumors. We and others have shown that MUC1 expression is activated by progesterone (P), TNF-α, and interferon-γ (IFN-γ). Here we demonstrate that MUC1 expression is down-regulated by overexpression of members of the protein inhibitor of activated signal transducer and activator of transcription (PIAS) family, PIAS1, PIAS3, PIASxα, PIASxβ, and PIASy, in human uterine epithelial cell lines HES and HEC-1A and in a breast cancer cell line, T47D. Treatments with P, TNF-α, and IFN-γ were unable to overcome the repression by PIASy. PIASy repression of basal, P-, and TNF-α-stimulated MUC1 promoter activity was not dependent on the PIASy sumoylation domain. In contrast, PIASy suppression of IFN-γ-activated MUC1 promoter activity was dependent on the PIASy sumoylation domain. PIASy and P receptor B were localized to the nucleus upon P treatment, and small interfering RNA knockdown of PIASy resulted in an increase in P-mediated stimulation of MUC1 protein expression. Overexpression of PIASy did not affect P receptor B binding to the MUC1 promoter but surprisingly led to a loss of nuclear receptor corepressor (NCoR), which was recruited to the promoter in response to P. Collectively, these data indicate that PIASy may be a useful target for down-regulation of MUC1 expression in various contexts.

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Tan, Joseph-Anthony T., Jing Song, Yuan Chen, and Linda K. Durrin. "Phosphorylation-Dependent Interaction of SATB1 and PIAS1 Directs SUMO-Regulated Caspase Cleavage of SATB1." Molecular and Cellular Biology 30, no. 11 (March 29, 2010): 2823–36. http://dx.doi.org/10.1128/mcb.01603-09.

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ABSTRACT Special AT-rich sequence-binding protein 1 (SATB1) is a tissue-restricted genome organizer that provides a key link between DNA loop organization, chromatin modification/remodeling, and transcription factor association at matrix attachment regions (MARs). The SUMO E3 ligase PIAS1 enhances SUMO conjugation to SATB1 lysine-744, and this modification regulates caspase-6 mediated cleavage of SATB1 at promyelocytic leukemia nuclear bodies (PML NBs). Since this regulated caspase cleavage occurs on only a subset of SATB1, and the products are relatively stable, proteolysis likely mediates cellular processes other than programmed cell death. However, the mechanism for the spatial and temporal regulation of SATB1 sumoylation and caspase cleavage is not known. Here we report that these processes are controlled by SATB1 phosphorylation; specifically, PIAS1 interaction with SATB1 is inhibited by phosphorylation. Mutagenesis studies identified interaction of the PIAS SAP (scaffold attachment factor-A/B/acinus/PIAS) motif with SATB1 N-terminal sequences. Notably, phosphorylation of SATB1 at threonine-188 regulates its interaction with PIAS1. Sequences near this phosphorylation site, LXXLL (residues 193 to 197), appear to be conserved among a subset of SUMO substrate proteins. Thus, this motif may be commonly involved in interaction with the PIAS SAP, and phosphorylation may similarly inhibit some of these substrates by preventing their interaction with the ligase.

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Santti, H., L. Mikkonen, A. Anand, S. Hirvonen-Santti, J. Toppari, M. Panhuysen, F. Vauti, et al. "Disruption of the murine PIASx gene results in reduced testis weight." Journal of Molecular Endocrinology 34, no. 3 (June 2005): 645–54. http://dx.doi.org/10.1677/jme.1.01666.

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PIASx belongs to the PIAS protein family, the members of which modulate activities of several transcription factors and act as E3 ligases in the sumoylation pathway. The PIASx gene is highly expressed in testis, suggesting a role in spermatogenesis. To investigate the function of PIASx in vivo, we have disrupted the PIASx gene in mice. Interestingly, the knockout mice were viable and fertile. Despite the normal fertility, the testis weight of the mutant animals was reduced and their number of apoptotic testicular cells was increased. Also, the sperm count of mutant mice tended to be reduced, but the quality of their sperm cells was normal. No significant changes were observed in the serum levels of LH and FSH or in the intratesticular testosterone concentration between the knockout animals and their wild-type littermates. Compensatory increases in other PIAS protein mRNAs were not observed in the knockout mice. These results imply that PIASx is required quantitatively rather than qualitatively for normal spermatogenesis.

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Conn, Kristen L., Peter Wasson, Steven McFarlane, Lily Tong, James R. Brown, Kyle G. Grant, Patricia Domingues, and Chris Boutell. "Novel Role for Protein Inhibitor of Activated STAT 4 (PIAS4) in the Restriction of Herpes Simplex Virus 1 by the Cellular Intrinsic Antiviral Immune Response." Journal of Virology 90, no. 9 (March 2, 2016): 4807–26. http://dx.doi.org/10.1128/jvi.03055-15.

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ABSTRACTSmallubiquitin-likemodifier (SUMO) is used by the intrinsic antiviral immune response to restrict viral pathogens, such as herpes simplex virus 1 (HSV-1). Despite characterization of the host factors that rely on SUMOylation to exert their antiviral effects, the enzymes that mediate these SUMOylation events remain to be defined. We show that unconjugated SUMO levels are largely maintained throughout infection regardless of the presence of ICP0, the HSV-1 SUMO-targeted ubiquitin ligase. Moreover, in the absence of ICP0, high-molecular-weight SUMO-conjugated proteins do not accumulate if HSV-1 DNA does not replicate. These data highlight the continued importance for SUMO signaling throughout infection. We show that the SUMO ligase protein inhibitor of activated STAT 4 (PIAS4) is upregulated during HSV-1 infection and localizes to nuclear domains that contain viral DNA. PIAS4 is recruited to sites associated with HSV-1 genome entry through SUMO interaction motif (SIM)-dependent mechanisms that are destabilized by ICP0. In contrast, PIAS4 accumulates in replication compartments through SIM-independent mechanisms irrespective of ICP0 expression. Depletion of PIAS4 enhances the replication of ICP0-null mutant HSV-1, which is susceptible to restriction by the intrinsic antiviral immune response. The mechanisms of PIAS4-mediated restriction are synergistic with the restriction mechanisms of a characterized intrinsic antiviral factor, promyelocytic leukemia protein, and are antagonized by ICP0. We provide the first evidence that PIAS4 is an intrinsic antiviral factor. This novel role for PIAS4 in intrinsic antiviral immunity contrasts with the known roles of PIAS proteins as suppressors of innate immunity.IMPORTANCEPosttranslational modifications withsmallubiquitin-likemodifier (SUMO) proteins regulate multiple aspects of host immunity and viral replication. Theproteininhibitor ofactivatedSTAT (PIAS) family of SUMO ligases is predominantly associated with the suppression of innate immune signaling. We now identify a unique and contrasting role for PIAS proteins as positive regulators of the intrinsic antiviral immune response to herpes simplex virus 1 (HSV-1) infection. We show that PIAS4 relocalizes to nuclear domains that contain viral DNA throughout infection. Depletion of PIAS4, either alone or in combination with the intrinsic antiviral factor promyelocytic leukemia protein, significantly impairs the intrinsic antiviral immune response to HSV-1 infection. Our data reveal a novel and dynamic role for PIAS4 in the cellular-mediated restriction of herpesviruses and establish a new functional role for the PIAS family of SUMO ligases in the intrinsic antiviral immune response to DNA virus infection.

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West, Peter W. "PIAs adorer." Manufacturing Engineer 68, no. 5 (1989): 16. http://dx.doi.org/10.1049/me:19890016.

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Ungureanu, Daniela, Sari Vanhatupa, Noora Kotaja, Jie Yang, Saara Aittomäki, Olli A. Jänne, Jorma J. Palvimo, and Olli Silvennoinen. "PIAS proteins promote SUMO-1 conjugation to STAT1." Blood 102, no. 9 (November 1, 2003): 3311–13. http://dx.doi.org/10.1182/blood-2002-12-3816.

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AbstractSignal transducer and activator of transcription 1 (STAT1) is a critical mediator of interferon-γ (IFN-γ)–induced transcription that is regulated through posttranslational modifications and through transacting proteins such as protein inhibitor of activated STAT1 (PIAS1). PIAS proteins have been shown to function as E3-type small ubiquitin-like modifier (SUMO) ligases, and sumoylation has been identified as a modulatory mechanism for several transcription factors. Here we show that STAT1 is subject to SUMO-1 modification, and sumoylation occurs in vivo and in vitro at a single, evolutionary conserved amino acid residue Lys703. Members of the PIAS family of proteins were found to strongly stimulate sumoylation of STAT1. Furthermore, activation of STAT1 by IFN-γ or pervanadate induced SUMO-1 conjugation. Mutation of Lys703 in STAT1 resulted in increased IFN-γ–mediated transactivation, suggesting a negative regulatory function for sumoylation. These results indicate that STAT1 is covalently modified by SUMO-1 in cytokine signaling and that PIAS proteins promote SUMO-1 conjugation to STAT1.

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Munarriz, Eliana, Daniela Barcaroli, Anastasis Stephanou, Paul A. Townsend, Carine Maisse, Alessandro Terrinoni, Michael H. Neale, et al. "PIAS-1 Is a Checkpoint Regulator Which Affects Exit from G1 and G2 by Sumoylation of p73." Molecular and Cellular Biology 24, no. 24 (December 15, 2004): 10593–610. http://dx.doi.org/10.1128/mcb.24.24.10593-10610.2004.

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ABSTRACT p73 is a recently described member of the p53 family, and, like p53, it undergoes a number of posttranslational modifications. Here we show, by yeast two-hybrid screening, pull-down assays, and coimmunoprecipitation, that p73α, -β, and -γ bind to the protein inhibitor of activated STAT-1 (PIAS-1) and that this binding stabilizes p73. PIAS-1 also sumoylates p73α, although not the C-terminally truncated isoforms p73β and -γ, and this requires the RING finger domain of PIAS-1. The ΔNp73α isoform can also bind, and be sumoylated by, PIAS-1. PIAS-1-mediated sumoylation decreases p73 transcriptional activity on several target promoters, such as Bax. p73 is colocalized in the nucleus with PIAS-1, and sumoylated p73 is located exclusively in the nuclear matrix. PIAS-1 is expressed predominantly during S phase, and PIAS-1 overexpression reduces p73-mediated transcription of p21, with a reduction of cells in G1 and cell cycle reentry. Inhibition of endogenous PIAS-1 by RNA interference reduces the proportion of cells in S phase and induces G2 arrest. These data suggest that PIAS-1, acting partly through binding and sumoylation of p73, is an important component of the cell cycle machinery.

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Kotaja, Noora, Ulla Karvonen, Olli A. Jänne, and Jorma J. Palvimo. "PIAS Proteins Modulate Transcription Factors by Functioning as SUMO-1 Ligases." Molecular and Cellular Biology 22, no. 14 (July 15, 2002): 5222–34. http://dx.doi.org/10.1128/mcb.22.14.5222-5234.2002.

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ABSTRACT PIAS (protein inhibitor of activated STAT) proteins interact with and modulate the activities of various transcription factors. In this work, we demonstrate that PIAS proteins xα, xβ, 1, and 3 interact with the small ubiquitin-related modifier SUMO-1 and its E2 conjugase, Ubc9, and that PIAS proteins themselves are covalently modified by SUMO-1 (sumoylated). PIAS proteins also tether other sumoylated proteins in a noncovalent fashion. Furthermore, recombinant PIASxα enhances Ubc9-mediated sumoylation of the androgen receptor and c-Jun in vitro. Importantly, PIAS proteins differ in their abilities to promote sumoylation in intact cells. The ability to stimulate protein sumoylation and the interaction with sumoylated proteins are dependent on the conserved PIAS RING finger-like domain. These functions are linked to the activity of PIASxα on androgen receptor-dependent transcription. Collectively, our results imply that PIAS proteins function as SUMO-1-tethering proteins and zinc finger-dependent E3 SUMO protein ligases, and these properties are likely to explain their ability to modulate the activities of various transcription factors.

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Hsieh, Hsiang-Tsan, Chih-Hung Wang, Mei-Ling Wu, Feng-Ming Yang, Yu-Chen Tai, and Meng-Chun Hu. "PIASy inhibits LRH-1-dependent CYP11A1 expression by competing for SRC-1 binding." Biochemical Journal 419, no. 1 (March 13, 2009): 201–9. http://dx.doi.org/10.1042/bj20081402.

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The orphan nuclear receptor LRH-1 (liver receptor homologue-1; NR5A2) plays a critical role in development, bile acid synthesis and cholesterol metabolism. LRH-1 is also expressed in the ovary where it is implicated in the regulation of steroidogenic genes for steroid hormone synthesis. In the present study, we investigated the molecular mechanisms of the transcriptional regulation of CYP11A1 by LRH-1 and found that LRH-1-mediated transactivation was markedly repressed by PIASy [protein inhibitor of activated STAT (signal transducer and activator of transcription) y], the shortest member of the PIAS family. The suppression of LRH-1 activity requires the N-terminal repression domain. Although PIAS proteins also function as E3 SUMO (small ubiquitin-related modifier) ligases and enhance SUMO conjugation, PIASy-mediated repression was independent of LRH-1 SUMOylation status. In addition, histone deacetylase activity was not involved in the inhibition of LRH-1 by PIASy. Immunoprecipitation and mammalian two-hybrid analyses indicated that PIASy interacted with LRH-1 through the C-terminal region, including the AF-2 (activation function-2) motif, which was also involved in the interaction between LRH-1 and the co-activator SRC-1 (steroid receptor co-activator-1). PIASy inhibited the binding of SRC-1 to LRH-1, although overexpression of SRC-1 partially overcame the PIASy inhibition of LRH-1 induction of the CYP11A1 promoter. The results of the present study suggest that competition with co-activators may be an important mechanism underlying the PIASy repression of LRH-1-mediated transactivation.

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O'Shea, John J., and Wendy Watford. "A peek at PIAS." Nature Immunology 5, no. 9 (September 2004): 875–76. http://dx.doi.org/10.1038/ni0904-875.

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Lonsdale, Tom. "AVA, ACAC and PIAS." Australian Veterinary Journal 78, no. 10 (October 2000): 673. http://dx.doi.org/10.1111/j.1751-0813.2000.tb10395.x.

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Palvimo, J. J. "PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription." Biochemical Society Transactions 35, no. 6 (November 23, 2007): 1405–8. http://dx.doi.org/10.1042/bst0351405.

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Transcriptional activity of signal-dependent transcription factors, including nuclear receptors, relies on interacting co-regulator proteins, many of which possess protein-modifying activity. SUMOs (small ubiquitin-related modifiers) and their conjugation pathway components act as co-regulator proteins for numerous transcription factors that also are often targets for SUMO modification. PIAS [protein inhibitor of activated STAT (signal transducer and activator of transcription)] proteins promote SUMOylation in a manner that resembles the action of RING-type ubiquitin E3 ligases. PIAS proteins were initially named for their ability to interact with STAT proteins and inhibit their activity, but their interactions and functions are not restricted to the STATs. Moreover, PIAS proteins do not operate merely as SUMO E3s, since their co-regulator effects are often independent of their RING finger but dependent on their SIM (SUMO-interacting motif) or SAP (scaffold attachment factor-A/B/acinus/PIAS) domain capable of interacting with DNA. The modulator activity imparted by the PIAS/SUMO system involves altered subnuclear targeting and/or assembly of transcription complexes. PIAS proteins may act as platforms that facilitate both removal and recruitment of other regulatory proteins in the transcription complexes.

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Depaux, A., F. Regnier-Ricard, A. Germani, and N. Varin-Blank. "A crosstalk between hSiah2 and Pias E3-ligases modulates Pias-dependent activation." Oncogene 26, no. 46 (May 28, 2007): 6665–76. http://dx.doi.org/10.1038/sj.onc.1210486.

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Iwata, Makoto, Kyohei Kanoh, Takuya Imaoka, and Kazuo Nagasawa. "Total synthesis of (+)-cylindradine A." Chem. Commun. 50, no. 53 (2014): 6991–94. http://dx.doi.org/10.1039/c4cc00137k.

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Yakass, Michael B., David Franco, and Osbourne Quaye. "Yellow Fever Virus Down-Regulates mRNA Expression of SOCS1 in the Initial Phase of Infection in Human Cell Lines." Viruses 12, no. 8 (July 25, 2020): 802. http://dx.doi.org/10.3390/v12080802.

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Flaviviruses are constantly evolving diverse immune evasion strategies, and the exploitation of the functions of suppressors of cytokine signalling (SOCS) and protein inhibitors of activated STATs (PIAS) to favour virus replication has been described for Dengue and Japanese encephalitis viruses but not for yellow fever virus (YFV), which is still of global importance despite the existence of an effective vaccine. Some mechanisms that YFV employs to evade host immune defence has been reported, but the expression patterns of SOCS and PIAS in infected cells is yet to be determined. Here, we show that SOCS1 is down-regulated early in YFV-infected HeLa and HEK 293T cells, while SOCS3 and SOCS5 are not significantly altered, and PIAS mRNA expression appears to follow a rise-dip pattern akin to circadian-controlled genes. We also demonstrate that YFV evades interferon-β application to produce comparable viral titres. This report provides initial insight into the in vitro expression dynamics of SOCS and PIAS upon YFV infection and a basis for further investigation into SOCS/PIAS expression and how these modulate the immune response in animal models.

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Wattimena, Jessica D., and Mansye Ronal Ayal. "Analisis Perubahan Garis Pantai Desa Rutong Kota Ambon." Jurnal Teknik Sipil 14, no. 2 (July 15, 2019): 115–36. http://dx.doi.org/10.28932/jts.v14i2.1796.

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Ambon sebagai ibukota Provinsi Maluku merupakan Daerah Kepulauan yang mana sebagian besardesanya berada pada Daerah pesisir pantai. Hal ini membuat timbulnya berbagai permasalahanpantai. Pantai Desa Rutong Kecamatan Leitmur Selatan Kota Ambon merupakan salah satu daerahyang sering mendapat serangan gelombang dan mengakibatkan kerusakan yang cukup parah.Berdasarkan informasi dan tinjauan yang dilakukan, jenis pantai pada Desa Rutong ialah pantaipasir (Sandy Beach). Kondisi ini menyebabkan sejumlah besar material (Pasir) terbawa akibatgelombang angin dan pasang tertinggi sehingga terjadi erosi yang mengakibatkan adanyaperubahan posisi garis pantai. Penelitian ini dilakukan dengan observasi dan pengamatan selama15 hari di pantai Desa Rutong Kota Ambon. Melalui penelitian ini diperoleh besarnya perubahangaris pantai dengan menggunakan metode perhitungan CERC (Coastal Engineering ResearchCenter) yaitu dengan membagi panjang garis pantai menjadi 50 pias untuk memprediksiperubahan garis pantai untuk 5 tahun dan 10 tahun ke depan. Dari analisis data tersebut diperolehhasil bahwa Desa Rutong mengalami kemunduran garis pantai pada 5 tahun sebesar -6,63 m dimana erosi terjadi pada pias 12 dan pada 10 tahun sebesar 16,04 m di mana erosi terjadi pada pias0.

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Imaoka, Takuya, Makoto Iwata, Takafumi Akimoto, and Kazuo Nagasawa. "Synthetic Approaches to Tetracyclic Pyrrole Imidazole Marine Alkaloids." Natural Product Communications 8, no. 7 (July 2013): 1934578X1300800. http://dx.doi.org/10.1177/1934578x1300800722.

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Oroidin derived pyrrole imidazole marine alkaloids (PIAs) are attractive targets for synthetic organic chemists because of their structural complexity and diversity as well as their interesting biological activities. A number of efforts have been carried out to develop strategies for the synthesis of these natural products. Members of PIAs ( eg., 2-7) which contain tetracyclic ring systems possessing characteristic cyclic guanidine or urea moieties show significant biological activities including anticancer activity and agonistic activity against the adrenoceptor. In this review investigations of the total synthesis of the representative tetracyclic PIAs dibromophakellin (2) and dibromophakellstatin (3) are described.

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Живковић, Валентина. "ПОМЕНИ ГРОБНОГ МЕСТА У ТЕСТАМЕНТИМА КОТОРАНА (1326–1337) REFERENCES TO BURIAL PLACES IN THE TESTAMENTS OF KOTOR CITIZENS (1326–1337)." Историјски часопис, no. 66/2017 (December 31, 2017): 129–47. http://dx.doi.org/10.34298/ic1766129z.

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Апстракт: У раду ce разматрају помени гробног места у оквиру сачуваног корпуса тестамената Которана из времена од 1326. до 1337. године. Основни задатак рада јесте утврђивање заступљености ове врсте завештања у оквиру формалне и садржајне структуре легата ad pias causas, а потом и анализа избора гробног места са становишта ширег контекста фунерарне праксе у касносредњовековном Котору. Кључне речи: тестаменти, касносредњовековни Котор, гробно местo, легати ad pias causas, катедрала Светог Трипуна, фрањевачки манастир, prandium pro anima. Abstract: The paper examines references to burial places within the preserved corpus of testaments of Kotor citizens from 1326 to 1337. The main purpose of the paper is to determine the presence of this type of testaments within the formal and content structure of ad pias causas bequests, and to analyse the choice of burial places in a wider context of funerary practice in late medieval Kotor. Keywords: testaments, late medieval Kotor, burial place, ad pias causas bequests, Cathedral of Saint Tryphon, Franciscan convent, prandium pro anima.

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Beliakoff, Jason, and Zijie Sun. "Zimp7 and Zimp10, two novel PIAS-like proteins, function as androgen receptor coregulators." Nuclear Receptor Signaling 4, no. 1 (January 2006): nrs.04017. http://dx.doi.org/10.1621/nrs.04017.

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The androgen receptor (AR) plays a critical role in male sexual development and in normal and malignant prostate cell growth and survival. It has been shown that AR transcriptional activation is regulated through interactions with a variety of transcriptional co-regulators. The Protein Inhibitors of Activated STATs (PIAS) are transcriptional co-regulators, and have been shown to modulate AR-mediated transcription. In this brief, we summarize our recent studies on two novel PIAS-like proteins, Zimp7 and Zimp10. Particularly, we address the functional interactions between the AR and these two proteins, and potential mechanisms by which they regulate AR mediated transcription. In addition, we explore potential roles of Zimp10 in transcriptional regulation in vivo using a recent Zimp10 knockout mouse model. Taken together, our findings thus far suggest that Zimp7 and Zimp10 are functionally non-redundant and share unique characteristics that have not been described for the PIAS family. Further investigation into the functional roles of these two PIAS-like proteins may help to better understand prostate cancer progression, and yield possible new targets for therapeutic intervention.

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Miyauchi, Yasuhiro, Satomi Yogosawa, Reiko Honda, Tamotsu Nishida, and Hideyo Yasuda. "Sumoylation of Mdm2 by Protein Inhibitor of Activated STAT (PIAS) and RanBP2 Enzymes." Journal of Biological Chemistry 277, no. 51 (October 18, 2002): 50131–36. http://dx.doi.org/10.1074/jbc.m208319200.

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Mdm2, a ubiquitin ligase that acts on p53, is regulated by sumoylation. In the current study, we identify the enzymes responsible for the sumoylation of Mdm2. When mammalian cells are co-transfected with cDNAs encoding Mdm2 and PIAS1 or PIASxβ (proteininhibitor ofactivatedSTAT) as sumoylation enzymes, Mdm2 is highly sumoylated. Mdm2 is also sumoylated in anin vitrosystem containing PIASxβ, PIAS1, and RanBP2. When several lysine residues of Mdm2 were sequentially mutated to arginine, the K182R mutant was not sumoylated in intact cells; however, in thein vitrosystem this mutant was sumoylated by PIAS1, PIASxβ, and RanBP2 as efficiently as the wild-type Mdm2 protein. Lysine residues 182 and 185 map within the nuclear localization signal of Mdm2. A K185R mutant of Mdm2 is sumoylated in intact cells, whereas a K182R protein is not. Only a Mdm2 protein bearing the K182R mutation is localized exclusively in the cytoplasm. Because RanBP2 is a nuclear pore protein and PIAS proteins are localized within the nucleus, our data suggest that Mdm2 is sumoylated during nuclear translocation by RanBP2 and then further sumoylated once in the nucleus by PIASxβ and PIAS1.

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Haryanto, Yanuar, Iman Satyarno, and Djoko Sulistyo. "ANALISIS DAYA DUKUNG BEBAN BALOK BETON BERTULANG TAMPANG T DENGAN PERKUATAN WIRE ROPE PADA DAERAH MOMEN NEGATIF MENGGUNAKAN PROGRAM RESPONSE-2000 DAN METODE PIAS." Jurnal Teknik Sipil 13, no. 3 (January 23, 2017): 173. http://dx.doi.org/10.24002/jts.v13i3.873.

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Abstrak: Response-2000 adalah suatu program yang dapat digunakan untuk menganalisis elemen beton bertulang akibat beban aksial, momen, geser, maupun kombinasi ketiganya sehingga respon beban-lendutan dapat diprediksi dan kekuatannya dapat diketahui. Makalah ini membahas perbandingan kapasitas daya dukung beban hasil pengujian balok bertulang tampang T yang diperkuat wire rope pada daerah momen negatif dengan analisis menggunakan Response-2000 dan metode pias. Metode pias dilakukan dengan cara membagi penampang menjadi sejumlah pias dengan ketebalan tertentu, kemudian menganalisis gaya-gaya yang bekerja sampai tercapai keseimbangan sehingga dapat ditentukan kapasitasnya. Analisis dilakukan terhadap 3 model balok tampang T, masing-masing 1 balok tanpa perkuatan, 1 balok diperkuat dengan 2 wire rope, dan 1 balok dipekuat dengan 4 wire rope. Jenis wire rope yang digunakan adalah Independent Wire Rope Core (IWRC) dengan diameter 10 mm. Hasil analisis menunjukkan bahwa kurva hubungan beban-lendutan untuk semua balok berdasarkan analisis Response-2000 memiliki pola yang mendekati kurva hubungan beban-lendutan hasil pengujian. Namun demikian terdapat perbedaan pada kemiringan kurva di mana hal tersebut dapat disebabkan oleh adanya anggapan lekatan sempurna (perfect bond) pada program Response-2000. Hal yang sama juga berlaku pada analisis metode pias. Daya dukung beban hasil Response-2000 menunjukkan rasio sebesar 1,05; 0,95; dan 0,89 terhadap hasil pengujian, masing-masing untuk balok tanpa perkuatan, balok diperkuat dengan 2 wire rope, dan balok dipekuat dengan 4 wire rope. Sedangkan kapasitas daya dukung beban hasil analisis metode pias menunjukkan rasio sebesar 1,05; 0,85; dan 0,76 terhadap hasil pengujian.

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Kawata, Takefumi, Tatsunori Hirano, Shun Ogasawara, Ryota Aoshima, and Ayako Yachi. "Evidence for a functional link between Dd-STATa and Dd-PIAS, a Dictyostelium PIAS homologue." Development, Growth & Differentiation 53, no. 7 (September 2011): 897–909. http://dx.doi.org/10.1111/j.1440-169x.2011.01296.x.

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Brown, James R., Kristen L. Conn, Peter Wasson, Matthew Charman, Lily Tong, Kyle Grant, Steven McFarlane, and Chris Boutell. "SUMO Ligase Protein Inhibitor of Activated STAT1 (PIAS1) Is a Constituent Promyelocytic Leukemia Nuclear Body Protein That Contributes to the Intrinsic Antiviral Immune Response to Herpes Simplex Virus 1." Journal of Virology 90, no. 13 (April 20, 2016): 5939–52. http://dx.doi.org/10.1128/jvi.00426-16.

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ABSTRACTAspects of intrinsic antiviral immunity are mediated bypromyelocyticleukemianuclearbody (PML-NB) constituent proteins. During herpesvirus infection, these antiviral proteins are independently recruited to nuclear domains that contain infecting viral genomes to cooperatively promote viral genome silencing. Central to the execution of this particular antiviral response is thesmallubiquitin-likemodifier (SUMO) signaling pathway. However, the participating SUMOylation enzymes are not fully characterized. We identify the SUMO ligaseproteininhibitor ofactivatedSTAT1 (PIAS1) as a constituent PML-NB protein. We show that PIAS1 localizes at PML-NBs in aSUMOinteractionmotif (SIM)-dependent manner that requires SUMOylated or SUMOylation-competent PML. Following infection with herpes simplex virus 1 (HSV-1), PIAS1 is recruited to nuclear sites associated with viral genome entry in a SIM-dependent manner, consistent with the SIM-dependent recruitment mechanisms of other well-characterized PML-NB proteins. In contrast to that of Daxx and Sp100, however, the recruitment of PIAS1 is enhanced by PML. PIAS1 promotes the stable accumulation of SUMO1 at nuclear sites associated with HSV-1 genome entry, whereas the accumulation of other evaluated PML-NB proteins occurs independently of PIAS1. We show that PIAS1 cooperatively contributes to HSV-1 restriction through mechanisms that are additive to those of PML and cooperative with those of PIAS4. The antiviral mechanisms of PIAS1 are counteracted by ICP0, the HSV-1 SUMO-targeted ubiquitin ligase, which disrupts the recruitment of PIAS1 to nuclear domains that contain infecting HSV-1 genomes through mechanisms that do not directly result in PIAS1 degradation.IMPORTANCEAdaptive, innate, and intrinsic immunity cooperatively and efficiently restrict the propagation of viral pathogens. Intrinsic immunity mediated by constitutively expressed cellular proteins represents the first line of intracellular defense against infection. PML-NB constituent proteins mediate aspects of intrinsic immunity to restrict herpes simplex virus 1 (HSV-1) as well as other viruses. These proteins repress viral replication through mechanisms that rely on SUMO signaling. However, the participating SUMOylation enzymes are not known. We identify the SUMO ligase PIAS1 as a constituent PML-NB antiviral protein. This finding distinguishes a SUMO ligase that may mediate signaling events important in PML-NB-mediated intrinsic immunity. Moreover, this research complements the recent identification of PIAS4 as an intrinsic antiviral factor, supporting a role for PIAS proteins as both positive and negative regulators of host immunity to virus infection.

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Pujiastuti, Asih. "Segmentasi Citra Kartu Pias Tipe SO-40U (1400-40S) Pada Perhitungan Lama Penyinaran Matahari." Angkasa: Jurnal Ilmiah Bidang Teknologi 9, no. 2 (December 14, 2017): 9. http://dx.doi.org/10.28989/angkasa.v9i2.174.

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The measurement of the duration of solar irradiation at the climatology station can be done using campbell stokes and pias cards. The aim of this research is to assist the climatology station operator to determine the burn object on the SO-40U (1400-40S) type of pias cards, making it easier to calculate the duration of solar irradiation. This app is designed and built to successfully segmentation the burn on the card automatically. In this research, the data was collected at a climatology station located in Barongan, Sumberagung Jetis, Bantul. Based on the test conducted segmentation generated in this study is good and produce RMSE number of object result of segmentation equal to 2,6485 to sum object in original image. The difference in object calculation results from a segmentation error caused by a small burning object of the pias card and or a thin but translucent object, so that the object is partially lost or forms an object's separation area.

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PUTRI, LINDA MATARINA KARTIKA. "Peningkatan Keterampilan Membaca Nyaring Melalui Media Pias-Pias Kata pada Siswa Kelas I SDN 1 Mojorejo Ponorogo." Trapsila: Jurnal Pendidikan Dasar 1, no. 01 (July 21, 2019): 81. http://dx.doi.org/10.30742/tpd.v1i01.726.

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This classroom action research was conducted on grade 1 students of SD Negeri 1 Mojorejo Ponorogo 2014/2015 Academic Year, due to the existence of problems, namely the learning outcomes of Indonesian language subjects especially reading aloud were still low. Through word-of-mouth media this problem is tried to be improved and improved. The design of this study was to use classroom action research (PTK) methods which aimed to improve or improve the quality of continuous learning practices. The study was conducted at SD Negeri 1 Mojorejo Ponorogo and the students studied were grade 1 students totaling 20 students. The implementation of classroom action research was carried out in two cycles. In one cycle consists of four steps, namely (1) planning (2), 2) actions or actions (acting), (3) observations (observing), (4) reflection (reflecting). Instruments used in learning are implementation plans learning (RPP), and research instruments namely observation sheets and activity sheets. Data collection is done by observation and performance testing techniques. Data analysis uses the mean. The results of this study can be seen by the increase in reading skills of students with the following values: in the pre-cycle the average value was 57.50 (35%), in the first cycle the average score was 70.00 (60%), and in cycle II the average value rose again to 81.75 (95%). Based on the data mentioned above, it can be said that through the word pias media it is very effective to improve the ability to read aloud to grade 1 students of SD Negeri 1 Mojorejo Ponorogo in 2014/2015 Academic Year.

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Martin, Nadine, Klaus Schwamborn, Henning Urlaub, Boyi Gan, Jun-Lin Guan, and Anne Dejean. "Spatial Interplay between PIASy and FIP200 in the Regulation of Signal Transduction and Transcriptional Activity." Molecular and Cellular Biology 28, no. 8 (February 19, 2008): 2771–81. http://dx.doi.org/10.1128/mcb.01210-07.

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ABSTRACT The members of the protein inhibitor of activated STAT (PIAS) family of proteins are implicated in fundamental cellular processes, including transcriptional regulation, either through action as E3 SUMO ligases or through SUMO-independent effects. We report here the identification of FIP200 (focal adhesion kinase family-interacting protein of 200 kDa) as a new PIASy-interacting protein. We show that the interaction depends on the integrity of the RING finger of PIASy and the carboxy terminus of FIP200. Both in vitro and in vivo sumoylation assays failed to reveal any sumoylation of FIP200, suggesting that FIP200 is not a bona fide SUMO substrate. Immunofluorescence microscopy and subcellular fractionation, either upon forced PIASy expression or in the absence of PIASy, revealed that interaction with PIASy redistributes FIP200 from the cytoplasm to the nucleus, correlating with abrogation of FIP200 regulation of TSC/S6K signaling. Conversely, FIP200 enhances the transcriptional activation of the p21 promoter by PIASy whereas PIASy transcription activity is severely reduced upon FIP200 depletion by RNA interference. Chromatin immunoprecipitation analysis demonstrates that endogenous PIASy and FIP200 are corecruited to the p21 promoter. Altogether, these results provide the first evidence for the existence of a close—spatially controlled—mode of regulation of FIP200 and PIASy nucleocytoplasmic functions.

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Fredrikzon, Johan. "Cybernetics: The Macy Conferences." Sensorium Journal 3 (March 26, 2021): 56–59. http://dx.doi.org/10.3384/sens.2002-3030.2021.3.56-59.

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Sturm, Sabine, Manuel Koch, and Fletcher A. White. "Cloning and Analysis of a Murine PIAS Family Member, PIASγ, in Developing Skin and Neurons." Journal of Molecular Neuroscience 14, no. 1-2 (2000): 107–22. http://dx.doi.org/10.1385/jmn:14:1-2:107.

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Deng, Zhiyong, Meimei Wan, and Guangchao Sui. "PIASy-Mediated Sumoylation of Yin Yang 1 Depends on Their Interaction but Not the RING Finger." Molecular and Cellular Biology 27, no. 10 (March 12, 2007): 3780–92. http://dx.doi.org/10.1128/mcb.01761-06.

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ABSTRACT As a multifunctional protein, Yin Yang 1 (YY1) has been demonstrated to regulate both gene expression and protein posttranslational modifications. However, gaps still exist in our knowledge of how YY1 can be modified and what the consequences of its modifications are. Here we report that YY1 protein can be sumoylated both in vivo and in vitro. We have identified lysine 288 as the major sumoylation site of YY1. We also discovered that PIASy, a SUMO E3 ligase, is a novel YY1-interacting protein and can stimulate the sumoylation of YY1 both in vitro and in vivo. Importantly, the effects of PIASy mutants on in vivo YY1 sumoylation correlate with the YY1-PIASy interaction but do not depend on the RING finger domain of PIASy. This regulation is unique to YY1 sumoylation because PIASy-mediated p53 sumoylation still relies on the integrity of PIASy, which is also true of all of the previously identified substrates of PIASy. In addition, PIASy colocalizes with YY1 in the nucleus, stabilizes YY1 in vivo, and differentially regulates YY1 transcriptional activity on different target promoters. This study demonstrates that YY1 is a target of SUMOs and reveals a novel feature of a SUMO E3 ligase in the PIAS family that selectively stimulates protein sumoylation independent of the RING finger domain.

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Liu, Yang, Ya-Dong Zhang, Liang Guo, Hai-Yan Huang, Hao Zhu, Jia-Xin Huang, Yuan Liu, et al. "Protein Inhibitor of Activated STAT 1 (PIAS1) Is Identified as the SUMO E3 Ligase of CCAAT/Enhancer-Binding Protein β (C/EBPβ) during Adipogenesis." Molecular and Cellular Biology 33, no. 22 (September 23, 2013): 4606–17. http://dx.doi.org/10.1128/mcb.00723-13.

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It is well recognized that PIAS1, a SUMO (small ubiquitin-like modifier) E3 ligase, modulates such cellular processes as cell proliferation, DNA damage responses, and inflammation responses. Recent studies have shown that PIAS1 also plays a part in cell differentiation. However, the role of PIAS1 in adipocyte differentiation remains unknown. CCAAT/enhancer-binding protein β (C/EBPβ), a major regulator of adipogenesis, is a target of SUMOylation, but the E3 ligase responsible for the SUMOylation of C/EBPβ has not been identified. The present study showed that PIAS1 functions as a SUMO E3 ligase of C/EBPβ to regulate adipogenesis. PIAS1 expression was significantly and transiently induced on day 4 of 3T3-L1 adipocyte differentiation, when C/EBPβ began to decline. PIAS1 was found to interact with C/EBPβ through the SAP (scaffold attachment factor A/B/acinus/PIAS) domain and SUMOylate it, leading to increased ubiquitination and degradation of C/EBPβ. C/EBPβ became more stable when PIAS1 was silenced by RNA interference (RNAi). Moreover, adipogenesis was inhibited by overexpression of wild-type PIAS1 and promoted by knockdown of PIAS1. The mutational study indicated that the catalytic activity of SUMO E3 ligase was required for PIAS1 to restrain adipogenesis. Importantly, the inhibitory effect of PIAS1 overexpression on adipogenesis was rescued by overexpressed C/EBPβ. Thus, PIAS1 could play a dynamic role in adipogenesis by promoting the SUMOylation of C/EBPβ.

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Betz, A., N. Lampen, S. Martinek, M. W. Young, and J. E. Darnell. "A Drosophila PIAS homologue negatively regulates stat92E." Proceedings of the National Academy of Sciences 98, no. 17 (August 14, 2001): 9563–68. http://dx.doi.org/10.1073/pnas.171302098.

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Pechan, P. "PIAS - The Prague Institute of Advanced Studies." TATuP - Zeitschrift für Technikfolgenabschätzung in Theorie und Praxis 5, no. 4 (December 1, 1996): 50–51. http://dx.doi.org/10.14512/tatup.5.4.50.

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Ghaffari, Saghi. "PIAS adds methyl-bias to HSC-differentiation." EMBO Journal 33, no. 2 (January 2014): 93–95. http://dx.doi.org/10.1002/embj.201387332.

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Schmidt, D., and S. M�ller. "PIAS/SUMO: new partners in transcriptional regulation." Cellular and Molecular Life Sciences (CMLS) 60, no. 12 (December 1, 2003): 2561–74. http://dx.doi.org/10.1007/s00018-003-3129-1.

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Škoda, Jan. "The Prague Institute of Advanced Studies (PIAS)." Biochemical Education 19, no. 4 (October 1991): 203–4. http://dx.doi.org/10.1016/0307-4412(91)90102-e.

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Tolkunova, Elena, Anna Malashicheva, Vladimir N. Parfenov, Claudio Sustmann, Rudolf Grosschedl, and Alexey Tomilin. "PIAS Proteins as Repressors of Oct4 Function." Journal of Molecular Biology 374, no. 5 (December 2007): 1200–1212. http://dx.doi.org/10.1016/j.jmb.2007.09.081.

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Rytinki, Miia M., Sanna Kaikkonen, Petri Pehkonen, Tiina Jääskeläinen, and Jorma J. Palvimo. "PIAS proteins: pleiotropic interactors associated with SUMO." Cellular and Molecular Life Sciences 66, no. 18 (June 13, 2009): 3029–41. http://dx.doi.org/10.1007/s00018-009-0061-z.

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von Cranach, M., and J. Valdes-Stauber. "Struktur und Entwicklung einer Institutsambulanz." Nervenheilkunde 24, no. 08 (2005): 686–95. http://dx.doi.org/10.1055/s-0038-1630007.

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ZusammenfassungIn Folge der Psychiatrie-Enquete wurden bundesweit psychiatrische Institutsambulanzen (PIAs) installiert. Diese bemühen sich um multiprofessionelle, nachgehend aufsuchende Behandlung und Rehabilitation schwer psychisch Kranker orientiert nach Komplexleistungsprogrammen, um somit das Leistungsspektrum der niedergelassenen Psychiater im Sinne der Enquete zu ergänzen, nicht zuletzt mit Notfallbehandlung und Konsiliardienst. Die Institutsambulanz am Bezirkskrankenhaus Kaufbeuren entwickelte sich allmählich seit deren Gründung 1981 in diesem Sinne, ähnlich wie die meisten bundesweit arbeitenden PIAs. Aktuell verfügt sie über eine zentral-dezentrale Organisation mit zentralisierter Verantwortung für betriebswirtschaftliche und koordinierende Aufgaben und über eine dezentrale fachliche Versorgung. Sie besteht aus sieben verschiedenen Fachambulanzen mit gegenwärtig 26 Planstellen verteilt auf sechs Berufsgruppen und betreut ca. 3 700 Personen jährlich (2 400 Patienten pro Quartal). Die Behandlungskosten belaufen sich auf 164 bis 196 Euro pro Patient und Quartal, dabei werden ca. 1 300 neue Patienten im Jahr versorgt. Wir analysieren die Entwicklung anhand von 18 Parametern und diskutieren das aktuelle Bedingungsgefüge. PIAs sind ein wichtiges Steuerungsinstrument der rationalen Versorgung sowie der stationären Aufnahmen und reduzieren sowohl durch Entlassungsvorbereitung als auch durch Behandlungskontinuität die Liegezeiten.

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Astrodjojo, Susilawati, Suratman Sudjud, and Sri Soenarsih DAS. "Effectiveness Test of Parasitization by Parasitoid Tricogramma japonicum in Controlling White Rice Stem Borer (Scirphopaga innotata)." International Journal on Food, Agriculture and Natural Resources 2, no. 1 (May 2, 2021): 25–30. http://dx.doi.org/10.46676/ij-fanres.v2i1.26.

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Rice is an essential food crop besides corn and soybeans. The need for rice each year increases along with population growth. One of the pests affecting rice is the white rice stem borer. The present research aimed to test the effectiveness and to examine the interaction between plant age and the number of Tricogramma japonicum parasitoid. The research was carried out at the Agrotechnology Laboratory of the Faculty of Agriculture, Khairun University, Ternate, and the rice fields of Bumi Restu village SP I, East Wasile district. The research design operative was a randomized block design where factor A (A1 = 21 DAS, A2 = 42 DAS, A3 = 56 DAS) was the age of the plant, and factor B (B0 = 0, B1 = 50, B2 = 100, B3 = 150) was the number of eggs of Corcyra cephalonica. Biological control using different amounts of Trichogramma japonicum parasitoid led to different interactions and results for each tested parameter. For the number of egg groups, there was no interaction with plant age, but the treatments which were found effective in suppressing stem borer populations were B2 and B3 (100 and 150). The most effective pias as indicated by damage intensity parameter was B3 (150), which was applied to plants aged 21 DAP. Furthermore, for plant height, different number of parasitoids poses significantly effective results. Percentage unhulled grain of pias B3 (150) causes insignificant damage. For production there is no interaction with plant age, but pias B2 (100) shows high yield. The conclusion is that pias B3 (150) applied to 21 days of plants is very effective in controlling white rice stem borer.

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Besperi, Besperi, Gusta Gunawan, and Tessa Dwi Utari. "Pemodelan Transpor Sedimen Pantai Kualo Kota Bengkulu." Inersia: Jurnal Teknik Sipil 13, no. 1 (April 27, 2021): 25–30. http://dx.doi.org/10.33369/ijts.13.1.25-30.

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Provinsi Bengkulu merupakan salah satu daerah dengan pantai terpanjang di Indonesia. Secara umum keadaan pantai di Bengkulu telah banyak mengalami kerusakan berupa abrasi dan sedimentasi. Perubahan garis pantai disebabkan oleh faktor alam dan/atau faktor manusia. Secara geografis, Pantai Kualo terletak di bagian Barat Pulau Sumatera yang berhadapan langsung dengan Samudera Hindia. Ini berarti, seluruh tepian barat merupakan daerah laut lepas dengan sedikit pulau yang menghalanginya. Sehingga pada saat nantinya, pihak yang berwenang dapat mempertimbangkan hal-hal yang harus dilakukan dalam menjaga pesisir pantai di Pantai Kualo ini. Berdasarkan hal ini, penelitian tentang peramalan perubahan garis pantai di Pantai kualo Kota Bengkulu dalam jangka waktu tertentu perlu dilakukan . Tujuan dari penelitian ini yaitu menganalisis besarnya transpor sedimen yang terjadi di Pantai Kualo Bengkulu dan memprediksi perubahan garis pantai dalam jangka waktu 5 tahun di Pantai Kualo Bengkulu. Penelitian ini dilakukan dengan menghitung transpor sedimen yang masuk dan keluar pesisir pantai dengan membagi pantai menjadi 10 sel (pias) sepanjang pantai 500 m dengan panjang 50 m pada setiap sel (pias) ditambah satu pias sebagai titik acuan. Penelitian yang dilakukan menghasilkan besarnya transpor sedimen dan perubahan garis pantai.

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Heo, Kyung-Sun, Hakjoo Lee, Patrizia Nigro, Tamlyn Thomas, Nhat-Tu Le, Eugene Chang, Carolyn McClain, et al. "PKCζ mediates disturbed flow-induced endothelial apoptosis via p53 SUMOylation." Journal of Cell Biology 193, no. 5 (May 30, 2011): 867–84. http://dx.doi.org/10.1083/jcb.201010051.

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Atherosclerosis is readily observed in regions of blood vessels where disturbed blood flow (d-flow) is known to occur. A positive correlation between protein kinase C ζ (PKCζ) activation and d-flow has been reported, but the exact role of d-flow–mediated PKCζ activation in atherosclerosis remains unclear. We tested the hypothesis that PKCζ activation by d-flow induces endothelial cell (EC) apoptosis by regulating p53. We found that d-flow–mediated peroxynitrite (ONOO−) increased PKCζ activation, which subsequently induced p53 SUMOylation, p53–Bcl-2 binding, and EC apoptosis. Both d-flow and ONOO− increased the association of PKCζ with protein inhibitor of activated STATy (PIASy) via the Siz/PIAS-RING domain (amino acids 301–410) of PIASy, and overexpression of this domain of PIASy disrupted the PKCζ–PIASy interaction and PKCζ-mediated p53 SUMOylation. En face confocal microscopy revealed increases in nonnuclear p53 expression, nitrotyrosine staining, and apoptosis in aortic EC located in d-flow areas in wild-type mice, but these effects were significantly decreased in p53−/− mice. We propose a novel mechanism for p53 SUMOylation mediated by the PKCζ–PIASy interaction during d-flow–mediated EC apoptosis, which has potential relevance to early events of atherosclerosis.

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Wright, David, Raphael Gellert, Serge Gutwirth, and Michael Friedewald. "Minimizing Technology Ricks with PIAs, Precaution, and Participation." IEEE Technology and Society Magazine 30, no. 4 (2011): 47–54. http://dx.doi.org/10.1109/mts.2011.943460.

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Takahashi, Yoshimitsu, and Yoshiko Kikuchi. "Cytoplasmic sumoylation by PIAS-type Siz1-SUMO ligase." Cell Cycle 7, no. 12 (June 15, 2008): 1738–44. http://dx.doi.org/10.4161/cc.7.12.6156.

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Shuai, Ke. "Regulation of cytokine signaling pathways by PIAS proteins." Cell Research 16, no. 2 (February 2006): 196–202. http://dx.doi.org/10.1038/sj.cr.7310027.

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Sayad, Arezou, Mohammad Taheri, Iman Azari, Vahid Kholghi Oskoei, and Soudeh Ghafouri‐Fard. "PIAS genes as disease markers in bipolar disorder." Journal of Cellular Biochemistry 120, no. 8 (March 12, 2019): 12937–42. http://dx.doi.org/10.1002/jcb.28564.

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Fitri, Yulia, Bibin Sulianto, Neneng Fitrya, and Sri Fitria Retnowati. "PERANCANGAN ALAT DIGITAL PENGUKUR INTENSITAS RADIASI MATAHARI DAN LAMA PENYINARAN MATAHARI." Photon: Jurnal Sain dan Kesehatan 9, no. 1 (October 28, 2018): 143–50. http://dx.doi.org/10.37859/jp.v9i1.1069.

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Intensitas radiasi matahari dan lama penyinaran matahari mempunyai pengaruh yang besar terhadap perubahan cuaca. Alat yang digunakan untuk mengukur intensitas radiasi matahari yaitu Phyrometer sedangkan lama penyinaran matahari diukur dengan alat Campbell Stokes dengan mengukur panjang jejak bakar di pias matahari. Prototype yang dirancang bertujuan sebagai alat alternatif untuk mengukur intensitas radiasi matahari dan lama penyinaran matahari. Prototype mengukur intensitas radiasi matahari dan lama penyinaran matahari menggunakan sensor LDR. Data intensitas radiasi matahari yang diperoleh dari prototype diolah menjadi data penyinaran matahari dengan metode regresi linear. Hasil data intensitas radiasi matahari yang diperoleh dari prototype dengan Phyrometer sebagai alat pembanding menggambarkan trend grafik yang sama. Hasil data lama penyinaran matahari dari prototype juga menggambarkan trend yang sama dengan alat pembanding Phyrometer dan pias matahari.

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Pascual-Le Tallec, Laurent, Olivier Kirsh, Marie-Christine Lecomte, Say Viengchareun, Maria-Christina Zennaro, Anne Dejean, and Marc Lombès. "Protein Inhibitor of Activated Signal Transducer and Activator of Transcription 1 Interacts with the N-Terminal Domain of Mineralocorticoid Receptor and Represses Its Transcriptional Activity: Implication of Small Ubiquitin-Related Modifier 1 Modification." Molecular Endocrinology 17, no. 12 (December 1, 2003): 2529–42. http://dx.doi.org/10.1210/me.2003-0299.

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Abstract:

Abstract Molecular mechanisms underlying mineralocorticoid receptor (MR)-mediated gene expression are not fully understood but seem to largely depend upon interactions with specific coregulators. To identify novel human MR (hMR) molecular partners, yeast two-hybrid screenings performed using the N-terminal domain as bait, allowed us to isolate protein inhibitor of activated signal transducer and activator of transcription (PIAS)1 and PIASxβ, described as SUMO (small ubiquitin-related modifier) E3-ligases. Specific interaction between PIAS1 and hMR was confirmed by glutathione-S-transferase pull-down experiments and N-terminal subdomains responsible for physical contacts were delineated. Transient transfections demonstrated that PIAS1 is a corepressor of aldosterone-activated MR transactivation but has no significant effect on human glucocorticoid receptor transactivation. The agonist or antagonist nature of the bound ligand also determines PIAS1 corepressive action. We provided evidence that PIAS1 conjugated SUMO-1 to hMR both in vitro and in vivo. Deciphering the unique sumoylation pattern of hMR, which possesses five consensus SUMO-1 binding sites, by combinatorial lysine substitutions, revealed a major impact of sumoylation on hMR properties. Using a murine mammary tumor virus promoter, PIAS1 action was independent of sumoylation whereas with glucocorticoid response element promoter, PIAS1 corepressive action depended on hMR sumoylation status. Taken together, our results identify a novel function for PIAS1 which interacts with the N-terminal domain of hMR and represses its ligand-dependent transcriptional activity, at least in part, through SUMO modifications.

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Journal articles on the topic 'PIAS'

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