Увійти

Готові списки джерел за темами / Immunophilin molecules / Статті в журналах

Щоб переглянути інші типи публікацій з цієї теми, перейдіть за посиланням: Immunophilin molecules.

Статті в журналах з теми "Immunophilin molecules"

Автор: Grafiati

Опубліковано: 10 січня 2023

Оновлено: 29 січня 2023

Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями

Оберіть тип джерела:

Ознайомтеся з топ-50 статей у журналах для дослідження на тему "Immunophilin molecules".

Біля кожної праці в переліку літератури доступна кнопка «Додати до бібліографії». Скористайтеся нею – і ми автоматично оформимо бібліографічне посилання на обрану працю в потрібному вам стилі цитування: APA, MLA, «Гарвард», «Чикаго», «Ванкувер» тощо.

Також ви можете завантажити повний текст наукової публікації у форматі «.pdf» та прочитати онлайн анотацію до роботи, якщо відповідні параметри наявні в метаданих.

Переглядайте статті в журналах для різних дисциплін та оформлюйте правильно вашу бібліографію.

1

Zgajnar, Nadia R., Cristina Daneri-Becerra, Ana Cauerhff, and Mario D. Galigniana. "The Scaffold Immunophilin FKBP51 Is a Phosphoprotein That Undergoes Dynamic Mitochondrial-Nuclear Shuttling." Cells 11, no. 23 (November 25, 2022): 3771. http://dx.doi.org/10.3390/cells11233771.

Повний текст джерела

Анотація:

The immunophilin FKBP51 forms heterocomplexes with molecular chaperones, protein-kinases, protein-phosphatases, autophagy-related factors, and transcription factors. Like most scaffold proteins, FKBP51 can use a simple tethering mechanism to favor the efficiency of interactions with partner molecules, but it can also exert more complex allosteric controls over client factors, the immunophilin itself being a putative regulation target. One of the simplest strategies for regulating pathways and subcellular localization of proteins is phosphorylation. In this study, it is shown that scaffold immunophilin FKBP51 is resolved by resolutive electrophoresis in various phosphorylated isoforms. This was evidenced by their reactivity with specific anti-phosphoamino acid antibodies and their fade-out by treatment with alkaline phosphatase. Interestingly, stress situations such as exposure to oxidants or in vivo fasting favors FKBP51 translocation from mitochondria to the nucleus. While fasting involves phosphothreonine residues, oxidative stress involves tyrosine residues. Molecular modeling predicts the existence of potential targets located at the FK1 domain of the immunophilin. Thus, oxidative stress favors FKBP51 dephosphorylation and protein degradation by the proteasome, whereas FK506 binding protects the persistence of the post-translational modification in tyrosine, leading to FKBP51 stability under oxidative conditions. Therefore, FKBP51 is revealed as a phosphoprotein that undergoes differential phosphorylations according to the stimulus.

Стилі APA, Harvard, Vancouver, ISO та ін.

2

De Leo, Sonia A., Nadia R. Zgajnar, Gisela I. Mazaira, Alejandra G. Erlejman, and Mario D. Galigniana. "Role of the Hsp90-Immunophilin Heterocomplex in Cancer Biology." Current Cancer Therapy Reviews 16, no. 1 (February 6, 2020): 19–28. http://dx.doi.org/10.2174/1573394715666190102120801.

Повний текст джерела

Анотація:

The identification of new factors that may function as cancer markers and become eventual pharmacologic targets is a challenge that may influence the management of tumor development and management. Recent discoveries connecting Hsp90-binding immunophilins with the regulation of signalling events that can modulate cancer progression transform this family of proteins in potential unconventional factors that may impact on the screening and diagnosis of malignant diseases. Immunophilins are molecular chaperones that group a family of intracellular receptors for immunosuppressive compounds. A subfamily of the immunophilin family is characterized by showing structural tetratricopeptide repeats, protein domains that are able to interact with the C-terminal end of the molecular chaperone Hsp90, and via the proper Hsp90-immunophilin complex, the biological properties of a number of client-proteins involved in cancer biology are modulated. Recent discoveries have demonstrated that two of the most studied members of this Hsp90- binding subfamily of immunophilins, FKBP51 and FKBP52, participate in several cellular processes such as apoptosis, carcinogenesis progression, and chemoresistance. While the expression levels of some members of the immunophilin family are affected in both cancer cell lines and human cancer tissues compared to normal samples, novel regulatory mechanisms have emerged during the last few years for several client-factors of immunophilins that are major players in cancer development and progression, among them steroid receptors, the transctiption factor NF-κB and the catalytic subunit of telomerase, hTERT. In this review, recent findings related to the biological properties of both iconic Hsp90-binding immunophilins, FKBP51 and FKBP52, are reviewed within the context of their interactions with those chaperoned client-factors. The potential roles of both immunophilins as potential cancer biomarkers and non-conventional pharmacologic targets for cancer treatment are discussed.

Стилі APA, Harvard, Vancouver, ISO та ін.

3

Ramachandran, Surya, and C. C. Kartha. "Cyclophilin-A: a potential screening marker for vascular disease in type-2 diabetes." Canadian Journal of Physiology and Pharmacology 90, no. 8 (August 2012): 1005–15. http://dx.doi.org/10.1139/y2012-038.

Повний текст джерела

Анотація:

The pathophysiology of vascular disease in diabetes involves abnormalities in endothelial cells, vascular smooth muscle cells, and monocytes. The metabolic abnormalities that characterize diabetes, such as hyperglycemia, increased free fatty acids, and insulin resistance, each provoke molecular mechanisms that contribute to vascular dysfunction. Several molecules have been identified as risk markers, and have been studied to prevent progression of disease and long-term complications. Markers such as C-reactive protein and monocyte chemoattractant protein-1 are used to assess risk for adverse cardiac events, but elevated levels are possible due to the presence of other risk factors as part of the natural physiological defense mechanism. In this review we discuss potential of cyclophilin-A, a secreted oxidative-stress-induced immunophilin with diverse functions. We present evidence for a significant role of cyclophilin-A in the pathogenesis of atherosclerosis in diabetes, and its potential as a marker for vascular disease in type-2 diabetes.

Стилі APA, Harvard, Vancouver, ISO та ін.

4

Schreiber, Stuart L., Jun Lui, Mark W. Albers, Michael K. Rosen, Robert F. Standaert, Thomas J. Wandless, and Patricia K. Somers. "Molecular Recognition of Immunophilins and Immunophilin-Ligand Complexes." Tetrahedron 48, no. 13 (March 1992): 2545–58. http://dx.doi.org/10.1016/s0040-4020(01)88520-3.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

5

Marks, A. R. "Cellular functions of immunophilins." Physiological Reviews 76, no. 3 (July 1, 1996): 631–49. http://dx.doi.org/10.1152/physrev.1996.76.3.631.

Повний текст джерела

Анотація:

Immunophilins are members of a highly conserved family of proteins all of which are cis-trans peptidyl-prolyl isomerases. The prototypic members of the immunophilin family, cyclophilin A and FKPB12, were discovered on the basis of their ability to bind and mediate the immunosuppressive effects of the drugs cyclosporin, FK506, and rapamycin. However, the prolyl isomerase activity of these proteins is not involved in any of the immunosuppressive effects. Indeed, despite the fact that all members of the family are prolyl isomerases, the cellular role of this enzymatic function has not been clearly defined. In many cases, immunophilins are widely expressed and are present at high levels in some tissues. Moreover, while the number of proteins that belong to the immunophilin family continues to grow, the natural cellular functions of all but a few remain obscure. An example where immunophilins do appear to have a defined cellular role, in the absence of immunosuppressive ligands, is the modulation of intracellular calcium release channel function by FKBP12 and FKBP12.6. In this case, FKBPs are integral parts of three types of calcium release channel complexes, skeletal and cardiac ryanodine receptors and the inositol 1,4,5-trisphosphate receptor. In each case, FKBPs modulate channel function possibly by enhancing the cooperativity between subunits.

Стилі APA, Harvard, Vancouver, ISO та ін.

6

Nair, S. C., R. A. Rimerman, E. J. Toran, S. Chen, V. Prapapanich, R. N. Butts, and D. F. Smith. "Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor." Molecular and Cellular Biology 17, no. 2 (February 1997): 594–603. http://dx.doi.org/10.1128/mcb.17.2.594.

Повний текст джерела

Анотація:

A cDNA for human FKBP51 has been cloned and sequenced, and protein products have been expressed in both in vitro and bacterial systems. The deduced amino acid sequence for human FKBP51 is 90% identical to sequences of recently described murine proteins and is 55% identical to the sequence of human FKBP52. Human FKBP51 mRNA is expressed in a wide range of tissues, and the protein has peptidylprolyl isomerase activity that is inhibited by FK506 but not cyclosporine. FKBP51 is the same as a previously described progesterone receptor-associated immunophilin that, similar to FKBP52 and cyclophilin 40, is an Hsp90-binding protein and appears in functionally mature steroid receptor complexes along with Hsp90 and p23. Each of the three receptor-associated immunophilins displays interactions with progesterone receptor that are more dynamic than Hsp90-receptor interactions. Whereas FKBP52 and FKBP51 compete about equally well for binding to Hsp90 in a purified system, FKBP51 accumulates preferentially in progesterone receptor complexes assembled in a cell-free system. This observation provides a precedent for differential interactions between Hsp90-associated immunophilins and target proteins such as steroid receptors.

Стилі APA, Harvard, Vancouver, ISO та ін.

7

Han, Ruifang, Ying Wang, Chen Chen, Zhuo Zhao, and Huaifeng Mi. "De-Novo Cloning of FKBP23 cDNA from Pig ER Using Nested PCR." Zeitschrift für Naturforschung C 64, no. 3-4 (April 1, 2009): 297–302. http://dx.doi.org/10.1515/znc-2009-3-423.

Повний текст джерела

Анотація:

FK506 binding proteins (FKBPs) in cells are known as immunophilins. We have identifi ed and characterized a cDNA encoding an endoplasmic reticulum (ER) immunophilin, FKBP23, from pig liver by nested PCR. The predicted amino acid sequence of pig FKBP23 shows high identity to those of human FKBP23 and mouse FKBP23. It possesses a conserved FKBP-type peptidylprolyl cis-trans isomerase (PPIase) domain and EF-hand domain. We constructed a plasmid to express pFKBP23. Furthermore, we proved that the recombinant pFKBP23 can specifi cally bind to natural BiP, the main protein of the molecular chaperone Hsp70 in ER lumen; the binding is interrelated with the Ca2+ concentration just as the FKBP23 from mice.

Стилі APA, Harvard, Vancouver, ISO та ін.

8

Fedotcheva, Tatiana A., Nadezhda I. Fedotcheva, and Nikolai L. Shimanovsky. "Progesterone as an Anti-Inflammatory Drug and Immunomodulator: New Aspects in Hormonal Regulation of the Inflammation." Biomolecules 12, no. 9 (September 14, 2022): 1299. http://dx.doi.org/10.3390/biom12091299.

Повний текст джерела

Анотація:

The specific regulation of inflammatory processes by steroid hormones has been actively studied in recent years, especially by progesterone (P4) and progestins. The mechanisms of the anti-inflammatory and immunomodulatory P4 action are not fully clear. The anti-inflammatory effects of P4 can be defined as nonspecific, associated with the inhibition of NF-κB and COX, as well as the inhibition of prostaglandin synthesis, or as specific, associated with the regulation of T-cell activation, the regulation of the production of pro- and anti-inflammatory cytokines, and the phenomenon of immune tolerance. The specific anti-inflammatory effects of P4 and its derivatives (progestins) can also include the inhibition of proliferative signaling pathways and the antagonistic action against estrogen receptor beta-mediated signaling as a proinflammatory and mitogenic factor. The anti-inflammatory action of P4 is accomplished through the participation of progesterone receptor (PR) chaperones HSP90, as well as immunophilins FKBP51 and FKBP52, which are the validated targets of clinically approved immunosuppressive drugs. The immunomodulatory and anti-inflammatory effects of HSP90 inhibitors, tacrolimus and cyclosporine, are manifested, among other factors, due to their participation in the formation of an active ligand–receptor complex of P4 and their interaction with its constituent immunophilins. Pharmacological agents such as HSP90 inhibitors can restore the lost anti-inflammatory effect of glucocorticoids and P4 in chronic inflammatory and autoimmune diseases. By regulating the activity of FKBP51 and FKBP52, it is possible to increase or decrease hormonal signaling, as well as restore it during the development of hormone resistance. The combined action of immunophilin suppressors with steroid hormones may be a promising strategy in the treatment of chronic inflammatory and autoimmune diseases, including endometriosis, stress-related disorders, rheumatoid arthritis, and miscarriages. Presumably, the hormone receptor- and immunophilin-targeted drugs may act synergistically, allowing for a lower dose of each.

Стилі APA, Harvard, Vancouver, ISO та ін.

9

Bram, R. J., D. T. Hung, P. K. Martin, S. L. Schreiber, and G. R. Crabtree. "Identification of the immunophilins capable of mediating inhibition of signal transduction by cyclosporin A and FK506: roles of calcineurin binding and cellular location." Molecular and Cellular Biology 13, no. 8 (August 1993): 4760–69. http://dx.doi.org/10.1128/mcb.13.8.4760-4769.1993.

Повний текст джерела

Анотація:

The immunosuppressants cyclosporin A (CsA) and FK506 appear to block T-cell function by inhibiting the calcium-regulated phosphatase calcineurin. While multiple distinct intracellular receptors for these drugs (cyclophilins and FKBPs, collectively immunophilins) have been characterized, the functionally active ones have not been discerned. We found that overexpression of cyclophilin A or B or FKBP12 increased T-cell sensitivity to CsA or FK506, respectively, demonstrating that they are able to mediate the inhibitory effects of their respective immunosuppressants in vivo. In contrast, cyclophilin C, FKBP13, and FKBP25 had no effect. Direct comparison of the Ki of each drug-immunophilin complex for calcineurin in vitro revealed that although calcineurin binding was clearly necessary, it was not sufficient to explain the in vivo activity of the immunophilin. Subcellular localization was shown also to play a role, since gene deletions of cyclophilins B and C which changed their intracellular locations altered their activities significantly. Cyclophilin B has been shown previously to be located within calcium-containing intracellular vesicles; its ability to mediate CsA inhibition implies that certain components of the signal transduction machinery are also spatially restricted within the cell.

Стилі APA, Harvard, Vancouver, ISO та ін.

10

Norville, Isobel H., Katherine O'Shea, Mitali Sarkar-Tyson, Suxin Zheng, Richard W. Titball, Gabriele Varani, and Nicholas J. Harmer. "The structure of a Burkholderia pseudomallei immunophilin–inhibitor complex reveals new approaches to antimicrobial development." Biochemical Journal 437, no. 3 (July 13, 2011): 413–22. http://dx.doi.org/10.1042/bj20110345.

Повний текст джерела

Анотація:

Mips (macrophage infectivity potentiators) are a subset of immunophilins associated with virulence in a range of micro-organisms. These proteins possess peptidylprolyl isomerase activity and are inhibited by drugs including rapamycin and tacrolimus. We determined the structure of the Mip homologue [BpML1 (Burkholderia pseudomallei Mip-like protein 1)] from the human pathogen and biowarfare threat B. pseudomallei by NMR and X-ray crystallography. The crystal structure suggests that key catalytic residues in the BpML1 active site have unexpected conformational flexibility consistent with a role in catalysis. The structure further revealed BpML1 binding to a helical peptide, in a manner resembling the physiological interaction of human TGFβRI (transforming growth factor β receptor I) with the human immunophilin FKBP12 (FK506-binding protein 12). Furthermore, the structure of BpML1 bound to the class inhibitor cycloheximide N-ethylethanoate showed that this inhibitor mimics such a helical peptide, in contrast with the extended prolyl-peptide mimicking shown by inhibitors such as tacrolimus. We suggest that Mips, and potentially other bacterial immunophilins, participate in protein–protein interactions in addition to their peptidylprolyl isomerase activity, and that some roles of Mip proteins in virulence are independent of their peptidylprolyl isomerase activity.

Стилі APA, Harvard, Vancouver, ISO та ін.

11

Graziani, Francesca, Laura Aldegheri, and Georg C. Terstappen. "High Throughput Scintillation Proximity Assay for the Identification of FKBP-12 Ligands." Journal of Biomolecular Screening 4, no. 1 (February 1999): 3–7. http://dx.doi.org/10.1177/108705719900400102.

Повний текст джерела

Анотація:

A high throughput scintillation proximity assay (SPA) was developed to identify novel ligands of FKBP-12, an immunophilin with peptidyl prolyl isomerase (rotamase) activity. Recombinant histidine-tagged FKBP-12 was expressed in Escherichia coli, purified by metal ion affinity chromatography, and immobilized to SPA beads by an antibody that recognizes the histidine tag of the recombinant protein. Using 1 nM [3H] FK506, a well-known macrolid ligand of FKBP-12, specific binding was saturable and accounted for 95% of total binding. Analysis of saturation and homologous displacement isotherms indicated the existence of a single binding site with a KD value of 1.6 nM. The specificity of [3H] FK506 binding was demonstrated in displacement experiments and showed that rapamycin, another macrolid, was as active as FK506 (IC50 of 3.5 and 3.2 nM, respectively), whereas GPI-1046, a prototype of small molecular compounds with neurotrophic properties and affinity for FKBP-type immunophilins, was more than 1000-fold less active. The high signal-to-noise ratio of 30, together with small standard deviations, makes this novel assay well suited for automated high throughput screening.

Стилі APA, Harvard, Vancouver, ISO та ін.

12

Wang, Chin-Chou, Wan-Jou Shen, Gangga Anuraga, Yu-Hsiu Hsieh, Hoang Dang Khoa Ta, Do Thi Minh Xuan, Chiu-Fan Shen, Chih-Yang Wang, and Wei-Jan Wang. "Penetrating Exploration of Prognostic Correlations of the FKBP Gene Family with Lung Adenocarcinoma." Journal of Personalized Medicine 13, no. 1 (December 26, 2022): 49. http://dx.doi.org/10.3390/jpm13010049.

Повний текст джерела

Анотація:

The complexity of lung adenocarcinoma (LUAD), the development of which involves many interacting biological processes, makes it difficult to find therapeutic biomarkers for treatment. FK506-binding proteins (FKBPs) are composed of 12 members classified as conservative intracellular immunophilin family proteins, which are often connected to cyclophilin structures by tetratricopeptide repeat domains and have peptidyl prolyl isomerase activity that catalyzes proline from residues and turns the trans form into the cis form. Since FKBPs belong to chaperone molecules and promote protein folding, previous studies demonstrated that FKBP family members significantly contribute to the degradation of damaged, misfolded, abnormal, and foreign proteins. However, transcript expressions of this gene family in LUAD still need to be more fully investigated. In this research, we adopted high-throughput bioinformatics technology to analyze FKBP family genes in LUAD to provide credible information to clinicians and promote the development of novel cancer target drugs in the future. The current data revealed that the messenger (m)RNA levels of FKBP2, FKBP3, FKBP4, FKBP10, FKBP11, and FKBP14 were overexpressed in LUAD, and FKBP10 had connections to poor prognoses among LUAD patients in an overall survival (OS) analysis. Based on the above results, we selected FKBP10 to further conduct a comprehensive analysis of the downstream pathway and network. Through a DAVID analysis, we found that FKBP10 was involved in mitochondrial electron transport, NADH to ubiquinone transport, mitochondrial respiratory chain complex I assembly, etc. The MetaCore pathway analysis also indicated that FKBP10 was involved in "Ubiquinone metabolism", "Translation_(L)-selenoaminoacid incorporation in proteins during translation", and "Transcription_Negative regulation of HIF1A function". Collectively, this study revealed that FKBP family members are both significant prognostic biomarkers for lung cancer progression and promising clinical therapeutic targets, thus providing new targets for treating LUAD patients.

Стилі APA, Harvard, Vancouver, ISO та ін.

13

Baughman, G., G. J. Wiederrecht, N. F. Campbell, M. M. Martin, and S. Bourgeois. "FKBP51, a novel T-cell-specific immunophilin capable of calcineurin inhibition." Molecular and Cellular Biology 15, no. 8 (August 1995): 4395–402. http://dx.doi.org/10.1128/mcb.15.8.4395.

Повний текст джерела

Анотація:

The immunosuppressive drugs FK506 and cyclosporin A block T-lymphocyte proliferation by inhibiting calcineurin, a critical signaling molecule for activation. Multiple intracellular receptors (immunophilins) for these drugs that specifically bind either FK506 and rapamycin (FK506-binding proteins [FKBPs]) or cyclosporin A (cyclophilins) have been identified. We report the cloning and characterization of a new 51-kDa member of the FKBP family from murine T cells. The novel immunophilin, FKBP51, is distinct from the previously isolated and sequenced 52-kDa murine FKBP, demonstrating 53% identity overall. Importantly, Western blot (immunoblot) analysis showed that unlike all other FKBPs characterized to date, FKBP51 expression was largely restricted to T cells. Drug binding to recombinant FKBP51 was demonstrated by inhibition of peptidyl prolyl isomerase activity. As judged from peptidyl prolyl isomerase activity, FKBP51 had a slightly higher affinity for rapamycin than for FK520, an FK506 analog. FKBP51, when complexed with FK520, was capable of inhibiting calcineurin phosphatase activity in an in vitro assay system. Inhibition of calcineurin phosphatase activity has been implicated both in the mechanism of immunosuppression and in the observed toxic side effects of FK506 in nonlymphoid cells. Identification of a new FKBP that can mediate calcineurin inhibition and is restricted in its expression to T cells suggests that new immunosuppressive drugs may be identified that, by virtue of their specific interaction with FKBP51, would be targeted in their site of action.

Стилі APA, Harvard, Vancouver, ISO та ін.

14

Vittorioso, Paola, Rachel Cowling, Jean-Denis Faure, Michel Caboche, and Catherine Bellini. "Mutation in the Arabidopsis PASTICCINO1Gene, Which Encodes a New FK506-Binding Protein-Like Protein, Has a Dramatic Effect on Plant Development." Molecular and Cellular Biology 18, no. 5 (May 1, 1998): 3034–43. http://dx.doi.org/10.1128/mcb.18.5.3034.

Повний текст джерела

Анотація:

ABSTRACT The pasticcino (pas) mutants ofArabidopsis thaliana are a new class of plant developmental mutants; members of this class show ectopic cell proliferation in cotyledons, extra layers of cells in the hypocotyl, and an abnormal apical meristem. This phenotype is correlated with both cell division and cell elongation defects. There are three complementation groups ofpas mutants (pas1, pas2, andpas3, with, respectively 2, 1, and 4 alleles). Here we describe in more detail the pas1-1 allele, which was obtained by insertional mutagenesis. The PAS1 gene has been cloned and characterized; it encodes an immunophilin-like protein similar to the p59 FK506-binding protein (FKBP52). PAS1 is characterized by an FKBP-like domain and three tetratricopeptide repeat units. Although the presence of immunophilins in plants has already been demonstrated, the pas1-1 mutant represents the first inactivation of an FKBP-like gene in plants. PAS1expression is altered in pas1 mutants and in thepas2 and pas3 mutants. The expression of thePAS1 gene is increased in the presence of cytokinins, a class of phytohormones originally discovered because of their ability to stimulate cell division. These results are of particular relevance as they show for the first time that an FKBP-like protein plays an important role in the control of plant development.

Стилі APA, Harvard, Vancouver, ISO та ін.

15

Zgajnar, Nadia, Sonia De Leo, Cecilia Lotufo, Alejandra Erlejman, Graciela Piwien-Pilipuk, and Mario Galigniana. "Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52." Biomolecules 9, no. 2 (February 1, 2019): 52. http://dx.doi.org/10.3390/biom9020052.

Повний текст джерела

Анотація:

Immunophilins are a family of proteins whose signature domain is the peptidylprolyl-isomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) through which they bind to the 90-kDa heat-shock protein (Hsp90), and via this chaperone, immunophilins contribute to the regulation of the biological functions of several client-proteins. Among these Hsp90-binding immunophilins, there are two highly homologous members named FKBP51 and FKBP52 (FK506-binding protein of 51-kDa and 52-kDa, respectively) that were first characterized as components of the Hsp90-based heterocomplex associated to steroid receptors. Afterwards, they emerged as likely contributors to a variety of other hormone-dependent diseases, stress-related pathologies, psychiatric disorders, cancer, and other syndromes characterized by misfolded proteins. The differential biological actions of these immunophilins have been assigned to the structurally similar, but functionally divergent enzymatic domain. Nonetheless, they also require the complementary input of the TPR domain, most likely due to their dependence with the association to Hsp90 as a functional unit. FKBP51 and FKBP52 regulate a variety of biological processes such as steroid receptor action, transcriptional activity, protein conformation, protein trafficking, cell differentiation, apoptosis, cancer progression, telomerase activity, cytoskeleton architecture, etc. In this article we discuss the biology of these events and some mechanistic aspects.

Стилі APA, Harvard, Vancouver, ISO та ін.

16

Orłowski, Marek, Katarzyna Popławska, Joanna Pieprzyk, Aleksandra Szczygieł-Sommer, Anna Więch, Mirosław Zarębski, Aneta Tarczewska, Jurek Dobrucki, and Andrzej Ożyhar. "Molecular determinants of Drosophila immunophilin FKBP39 nuclear localization." Biological Chemistry 399, no. 5 (April 25, 2018): 467–84. http://dx.doi.org/10.1515/hsz-2017-0251.

Повний текст джерела

Анотація:

AbstractFK506-binding proteins (FKBPs) belong to a distinct class of immunophilins that interact with immunosuppressants. They use their peptidyl-prolyl isomerase (PPIase) activity to catalyze thecis-transconversion of prolyl bonds in proteins during protein-folding events. FKBPs also act as a unique group of chaperones. TheDrosophila melanogasterpeptidyl-prolylcis-transisomerase FK506-binding protein of 39 kDa (FKBP39) is thought to act as a transcriptional modulator of gene expression in 20-hydroxyecdysone and juvenile hormone signal transduction. The aim of this study was to analyze the molecular determinants responsible for the subcellular distribution of an FKBP39-yellow fluorescent protein (YFP) fusion construct (YFP-FKBP39). We found that YFP-FKBP39 was predominantly nucleolar. To identify the nuclear localization signal (NLS), a series of YFP-tagged FKBP39 deletion mutants were prepared and examinedin vivo. The identified NLS signal is located in a basic domain. Detailed mutagenesis studies revealed that residues K188 and K191 are crucial for the nuclear targeting of FKBP39 and its nucleoplasmin-like (NPL) domain contains the sequence that controls the nucleolar-specific translocation of the protein. These results show that FKBP39 possesses a specific NLS in close proximity to a putative helix-turn-helix (HTH) motif and FKBP39 may bind DNAin vivoandin vitro.

Стилі APA, Harvard, Vancouver, ISO та ін.

17

Mesa, Annia, Jason A. Somarelli, and Rene J. Herrera. "Spliceosomal immunophilins." FEBS Letters 582, no. 16 (June 9, 2008): 2345–51. http://dx.doi.org/10.1016/j.febslet.2008.06.006.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

18

Ratner, Mark. "Immunophilin Structure Via NMR." Nature Biotechnology 9, no. 6 (June 1991): 506. http://dx.doi.org/10.1038/nbt0691-506.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

19

Marks, Andrew R. "Immunophilin Modulation of Calcium Channel Gating." Methods 9, no. 2 (April 1996): 177–87. http://dx.doi.org/10.1006/meth.1996.0024.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

20

Andrianov, A. M., and I. V. Anishchenko. "Computer modeling of the promising inhibitors of the hiv-1 subtype a replication as a framework for the rational anti-aids drug design." Biomeditsinskaya Khimiya 57, no. 2 (2011): 161–73. http://dx.doi.org/10.18097/pbmc20115702161.

Повний текст джерела

Анотація:

The model of the structural complex of cyclophilin B belonging to the immunophilins family with the HIV-1 subtype A V3 loop presenting the principal neutralizing determinant of the virus gp120 envelope protein as well as determinants of cell tropism and syncutium formation was generated by molecular docking methods. Basing on the conformational and energy characteristics of the built complex, computer-aided design of the polypeptide able to block effectively the functionally crucial V3 segments was implemented. From the joint analysis of the results derived with the data of literature, the generated molecule was suggested to offer a promising pharmacological substance for making a reality of the protein engineering projects aimed at developing the anti-AIDS drugs able to stop the HIV's spread.

Стилі APA, Harvard, Vancouver, ISO та ін.

21

Munn, Kirsteen, and Ruth Steward. "The shut-down Gene of Drosophila melanogaster Encodes a Novel FK506-Binding Protein Essential for the Formation of Germline Cysts During Oogenesis." Genetics 156, no. 1 (September 1, 2000): 245–56. http://dx.doi.org/10.1093/genetics/156.1.245.

Повний текст джерела

Анотація:

Abstract In Drosophila melanogaster, the process of oogenesis is initiated with the asymmetric division of a germline stem cell. This division results in the self-renewal of the stem cell and the generation of a daughter cell that undergoes four successive mitotic divisions to produce a germline cyst of 16 cells. Here, we show that shut-down is essential for the normal function of the germline stem cells. Analysis of weak loss-of-function alleles confirms that shut-down is also required at later stages of oogenesis. Clonal analysis indicates that shut-down functions autonomously in the germline. Using a positional cloning approach, we have isolated the shut-down gene. Consistent with its function, the RNA and protein are strongly expressed in the germline stem cells and in 16-cell cysts. The RNA is also present in the germ cells throughout embryogenesis. shut-down encodes a novel Drosophila protein similar to the heat-shock protein-binding immunophilins. Like immunophilins, Shut-down contains an FK506-binding protein domain and a tetratricopeptide repeat. In plants, high-molecular-weight immunophilins have been shown to regulate cell divisions in the root meristem in response to extracellular signals. Our results suggest that shut-down may regulate germ cell divisions in the germarium.

Стилі APA, Harvard, Vancouver, ISO та ін.

22

Luan, S., J. Kudla, W. Gruissem, and S. L. Schreiber. "Molecular characterization of a FKBP-type immunophilin from higher plants." Proceedings of the National Academy of Sciences 93, no. 14 (July 9, 1996): 6964–69. http://dx.doi.org/10.1073/pnas.93.14.6964.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

23

Gough, N. R. "Targeting Immunophilins for Neuroprotection." Science Signaling 1, no. 2 (January 8, 2008): ec18-ec18. http://dx.doi.org/10.1126/stke.12ec18.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

24

Goel, Monu, Reynaldo Garcia, Mark Estacion, and William P. Schilling. "Regulation ofDrosophilaTRPL Channels by Immunophilin FKBP59." Journal of Biological Chemistry 276, no. 42 (August 20, 2001): 38762–73. http://dx.doi.org/10.1074/jbc.m104125200.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

25

Davis, Diane L., and Steven J. Soldin. "Identification of Ubiquitin as an Immunophilin." Biochemical and Biophysical Research Communications 277, no. 2 (October 2000): 325–29. http://dx.doi.org/10.1006/bbrc.2000.3684.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

26

Kallen, Joerg, Richard Sedrani, Gerhard Zenke, and Juergen Wagner. "Structure of Human Cyclophilin A in Complex with the Novel Immunosuppressant Sanglifehrin A at 1.6 Å Resolution." Journal of Biological Chemistry 280, no. 23 (March 16, 2005): 21965–71. http://dx.doi.org/10.1074/jbc.m501623200.

Повний текст джерела

Анотація:

Sanglifehrin A (SFA) is a novel immunosuppressant isolated from Streptomyces sp. that binds strongly to the human immunophilin cyclophilin A (CypA). SFA exerts its immunosuppressive activity through a mode of action different from that of all other known immunophilin-binding substances, namely cyclosporine A (CsA), FK506, and rapamycin. We have determined the crystal structure of human CypA in complex with SFA at 1.6 Å resolution. The high resolution of the structure revealed the absolute configuration at all 17 chiral centers of SFA as well as the details of the CypA/SFA interactions. In particular, it was shown that the 22-membered macrocycle of SFA is deeply embedded in the same binding site as CsA and forms six direct hydrogen bonds with CypA. The effector domain of SFA, on the other hand, has a chemical and three-dimensional structure very different from CsA, already strongly suggesting different immunosuppressive mechanisms. Furthermore, two CypA·SFA complexes form a dimer in the crystal as well as in solution as shown by light scattering and size exclusion chromatography experiments. This observation raises the possibility that the dimer of CypA·SFA complexes is the molecular species mediating the immunosuppressive effect.

Стилі APA, Harvard, Vancouver, ISO та ін.

27

Snyder, Solomon H., and David M. Sabatini. "Immunophilins and nervous system." Nature Medicine 1, no. 1 (January 1995): 32–37. http://dx.doi.org/10.1038/nm0195-32.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

28

Quintá, Héctor R., Natalia M. Galigniana, Alejandra G. Erlejman, Mariana Lagadari, Graciela Piwien-Pilipuk, and Mario D. Galigniana. "Management of cytoskeleton architecture by molecular chaperones and immunophilins." Cellular Signalling 23, no. 12 (December 2011): 1907–20. http://dx.doi.org/10.1016/j.cellsig.2011.07.023.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

29

Tanaka, Ken-ichi, and Norio Ogawa. "Molecular Basis for the Neuroprotective Properties of FKBP-Binding Immunophilin Ligands." Current Medicinal Chemistry-Central Nervous System Agents 4, no. 1 (March 1, 2004): 27–34. http://dx.doi.org/10.2174/1568015043477568.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

30

Clipstone, N. A., D. F. Fiorentino, and G. R. Crabtree. "Molecular analysis of the interaction of calcineurin with drug-immunophilin complexes." Journal of Biological Chemistry 269, no. 42 (October 1994): 26431–37. http://dx.doi.org/10.1016/s0021-9258(18)47212-2.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

31

GALAT, Andrzej. "Peptidylproline cis-trans-isomerases: immunophilins." European Journal of Biochemistry 216, no. 3 (September 1993): 689–707. http://dx.doi.org/10.1111/j.1432-1033.1993.tb18189.x.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

32

Barik, Sailen. "Dual-Family Peptidylprolyl Isomerases (Immunophilins) of Select Monocellular Organisms." Biomolecules 8, no. 4 (November 15, 2018): 148. http://dx.doi.org/10.3390/biom8040148.

Повний текст джерела

Анотація:

The dual-family peptidylprolyl cis-trans isomerases (immunophilins) represent a naturally occurring chimera of the classical FK506-binding protein (FKBP) and cyclophilin (CYN), connected by a flexible linker. They are found exclusively in monocellular organisms. The modular builds of these molecules represent two distinct types: CYN-(linker)-FKBP and FKBP-3TPR (tetratricopeptide repeat)-CYN. Abbreviated respectively as CFBP and FCBP, the two classes also exhibit distinct organism preference, the CFBP being found in prokaryotes, and the FCBP in eukaryotes. This review summarizes the mystery of these unique class of prolyl isomerases, focusing on their host organisms, potential physiological role, and likely routes of evolution.

Стилі APA, Harvard, Vancouver, ISO та ін.

33

Singh, Khushwant, Mark Winter, Miloslav Zouhar, and Pavel Ryšánek. "Cyclophilins: Less Studied Proteins with Critical Roles in Pathogenesis." Phytopathology® 108, no. 1 (January 2018): 6–14. http://dx.doi.org/10.1094/phyto-05-17-0167-rvw.

Повний текст джерела

Анотація:

Cyclophilins (EC 5.2.1.8) belong to a subgroup of proteins known as immunophilins, which also include FK506-binding proteins and parvulins. Members of the immunophilins have two main characteristic properties: (i) peptidyl-prolyl cis-trans isomerase activity and (ii) the ability to bind immunosuppressant molecules of fungal origin. Cyclophilins are some of the most conserved proteins present in eukaryotes and prokaryotes, and they have been implicated in diverse cellular processes and responses to multiple biotic and abiotic stresses. Cyclophilins have been exploited in humans and plants extensively, but they have only recently received attention in regard to phytopathogens. In Phellinus sulphurascens and species of the genus Leptosphaeria and Phytophthora, high expression of cyclophilins was found to be related to infection. Moreover, recent studies of cyclophilins in certain phytopathogens, such as Magnaporthe oryzae, Botrytis cinerea, Cryphonectria parasitica, and Puccinia triticina, demonstrated their roles as a pathogenicity factors. In addition to pathogenicity, cyclophilins have high affinity for the immunosuppressive drug cyclosporin A, which is a potent antifungal agent. Although cyclophilins are highly conserved in phytopathogens, because they have been less studied, their role remains largely unknown. In this review, we provide detailed information on the cyclophilins in several phytopathogens, including fungi and oomycetes, as well as their role in suppressing plant immunity.

Стилі APA, Harvard, Vancouver, ISO та ін.

34

Zhang, Ziyang, and Kevan M. Shokat. "Bifunctional Small‐Molecule Ligands of K‐Ras Induce Its Association with Immunophilin Proteins." Angewandte Chemie 131, no. 45 (September 26, 2019): 16460–65. http://dx.doi.org/10.1002/ange.201910124.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

35

Zhang, Ziyang, and Kevan M. Shokat. "Bifunctional Small‐Molecule Ligands of K‐Ras Induce Its Association with Immunophilin Proteins." Angewandte Chemie International Edition 58, no. 45 (September 26, 2019): 16314–19. http://dx.doi.org/10.1002/anie.201910124.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

36

Wang, Jingjing, Qunfang Weng, and Qiongbo Hu. "Effects of Destruxin A on Silkworm’s Immunophilins." Toxins 11, no. 6 (June 18, 2019): 349. http://dx.doi.org/10.3390/toxins11060349.

Повний текст джерела

Анотація:

Destruxin A (DA), a major secondary metabolite of Metarhizium anisopliae, has anti-immunity to insects. However, the detailed mechanism and its interactions with target proteins are elusive. Previously, three immunophilins, peptidyl–prolyl cis–trans isomerase (BmPPI), FK506 binding-protein 45 (BmFKBP45) and BmFKBP59 homologue, were isolated from the silkworm, Bombyx mori Bm12 cell line following treatment with DA, which suggested that these proteins were possible DA-binding proteins. To validate the interaction between DA and the three immunophilins, we performed bio-layer interferometry (BLI) assay, and the results showed that DA has interaction with BmPPI, whose affinity constant value is 1.98 × 10−3 M and which has no affinity with FKBP45 and FKBP59 homologue in vitro. Furthermore, we investigated the affinity between DA and human PPI protein (HsPPIA) and the affinity constant (KD) value is 2.22 × 10−3 M. Additionally, we compared the effects of silkworm and human PPI proteins produced by DA and immunosuppressants, cyclosporine A (CsA), and tacrolimus (FK506), by employing I2H (insect two-hybrid) in the SF-9 cell line. The results indicated that in silkworm, the effects created by DA and CsA were stronger than FK506. Furthermore, the effects created by DA in silkworm were stronger than those in humans. This study will offer new thinking to elucidate the molecular mechanism of DA in the immunity system of insects.

Стилі APA, Harvard, Vancouver, ISO та ін.

37

Ivery, Michael T. G. "Immunophilins: Switched on protein binding domains?" Medicinal Research Reviews 20, no. 6 (2000): 452–84. http://dx.doi.org/10.1002/1098-1128(200011)20:6<452::aid-med2>3.0.co;2-6.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

38

Toneatto, Judith, Nancy L. Charó, Natalia M. Galigniana, and Graciela Piwien-Pilipuk. "Adipogenesis is under surveillance of Hsp90 and the high molecular weight Immunophilin FKBP51." Adipocyte 4, no. 4 (May 13, 2015): 239–47. http://dx.doi.org/10.1080/21623945.2015.1049401.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

39

Sabatini, David M., Michael M. Lai, and Solomon H. Snyder. "Neural roles of immunophilins and their ligands." Molecular Neurobiology 15, no. 2 (October 1997): 223–39. http://dx.doi.org/10.1007/bf02740635.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

40

Hopkins, Sam, and Philippe A. Gallay. "The role of immunophilins in viral infection." Biochimica et Biophysica Acta (BBA) - General Subjects 1850, no. 10 (October 2015): 2103–10. http://dx.doi.org/10.1016/j.bbagen.2014.11.011.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

41

HOKE, A. "Neuroprotection in the PNS: Erythropoietin and Immunophilin Ligands." Annals of the New York Academy of Sciences 1053, no. 1 (August 1, 2005): 491–501. http://dx.doi.org/10.1196/annals.1344.043.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

42

HÖKE, AHMET, and SANJAY C. KESWANI. "Neuroprotection in the PNS: Erythropoietin and Immunophilin Ligands." Annals of the New York Academy of Sciences 1053, no. 1 (June 28, 2008): 491–501. http://dx.doi.org/10.1111/j.1749-6632.2005.tb00059.x.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

43

Stein, Ross L. "Exploring the catalytic activity of immunophilins." Current Biology 1, no. 4 (August 1991): 234–36. http://dx.doi.org/10.1016/0960-9822(91)90067-7.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

44

Kato, Hiroyuki, Takanori Oikawa, Kazuyuki Otsuka, Akira Takahashi, and Yasuto Itoyama. "Postischemic changes in the immunophilin FKBP12 in the rat brain." Molecular Brain Research 84, no. 1-2 (December 2000): 58–66. http://dx.doi.org/10.1016/s0169-328x(00)00210-2.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

45

Adams, Brian, Alla Musiyenko, Rajinder Kumar, and Sailen Barik. "A Novel Class of Dual-family Immunophilins." Journal of Biological Chemistry 280, no. 26 (April 21, 2005): 24308–14. http://dx.doi.org/10.1074/jbc.m500990200.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

46

Sinkins, William G., Monu Goel, Mark Estacion, and William P. Schilling. "Association of Immunophilins with Mammalian TRPC Channels." Journal of Biological Chemistry 279, no. 33 (June 15, 2004): 34521–29. http://dx.doi.org/10.1074/jbc.m401156200.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

47

Fruman, David A., Steven J. Burakoff, and Barbara E. Bierer. "Immunophilins in protein folding and immunosuppression 1." FASEB Journal 8, no. 6 (April 1994): 391–400. http://dx.doi.org/10.1096/fasebj.8.6.7513288.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

48

Schreiber, Stuart L. "Immunophilin-sensitive protein phosphatase action in cell signaling pathways." Cell 70, no. 3 (August 1992): 365–68. http://dx.doi.org/10.1016/0092-8674(92)90158-9.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

49

DiLella, Anthony G. "Chromosomal assignment of the human immunophilin FKBP-12 gene." Biochemical and Biophysical Research Communications 179, no. 3 (September 1991): 1427–33. http://dx.doi.org/10.1016/0006-291x(91)91732-r.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

50

Wang, Tongwen. "The immunophilin FKBP12: a molecular guardian of the TGF-beta family type I receptors." Frontiers in Bioscience 9, no. 1-3 (2004): 619. http://dx.doi.org/10.2741/1095.

Повний текст джерела

Стилі APA, Harvard, Vancouver, ISO та ін.

Ми пропонуємо знижки на всі преміум-плани для авторів, чиї праці увійшли до тематичних добірок літератури. Зв'яжіться з нами, щоб отримати унікальний промокод!