Bibliografías temáticas / Thr protein phosphatases

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Literatura académica sobre el tema "Thr protein phosphatases"

Autor: Grafiati
Publicado: 4 de junio de 2021
Última modificación: 1 de febrero de 2022

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Artículos de revistas sobre el tema "Thr protein phosphatases"

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Mizunuma, Masataka, Atsushi Kaneko, Shunta Imai, Kazuhiro Furukawa y Yoshiro Chuman. "Methods for Identification of Substrates/Inhibitors of FCP/SCP Type Protein Ser/Thr Phosphatases". Processes 8, n.º 12 (4 de diciembre de 2020): 1598. http://dx.doi.org/10.3390/pr8121598.

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Protein phosphorylation is the most widespread type of post-translational modification and is properly controlled by protein kinases and phosphatases. Regarding the phosphorylation of serine (Ser) and threonine (Thr) residues, relatively few protein Ser/Thr phosphatases control the specific dephosphorylation of numerous substrates, in contrast with Ser/Thr kinases. Recently, protein Ser/Thr phosphatases were reported to have rigid substrate recognition and exert various biological functions. Therefore, identification of targeted proteins by individual protein Ser/Thr phosphatases is crucial to clarify their own biological functions. However, to date, information on the development of methods for identification of the substrates of protein Ser/Thr phosphatases remains scarce. In turn, substrate-trapping mutants are powerful tools to search the individual substrates of protein tyrosine (Tyr) phosphatases. This review focuses on the development of novel methods for the identification of Ser/Thr phosphatases, especially small C-terminal domain phosphatase 1 (Scp1), using peptide-displayed phage library with AlF4−/BeF3−, and discusses the identification of putative inhibitors.
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Ariño, Joaquín, Antonio Casamayor y Asier González. "Type 2C Protein Phosphatases in Fungi". Eukaryotic Cell 10, n.º 1 (12 de noviembre de 2010): 21–33. http://dx.doi.org/10.1128/ec.00249-10.

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ABSTRACT Type 2C Ser/Thr phosphatases are a remarkable class of protein phosphatases, which are conserved in eukaryotes and involved in a large variety of functional processes. Unlike in other Ser/Thr phosphatases, the catalytic polypeptide is not usually associated with regulatory subunits, and functional specificity is achieved by encoding multiple isoforms. For fungi, most information comes from the study of type 2C protein phosphatase (PP2C) enzymes in Saccharomyces cerevisiae , where seven PP2C-encoding genes ( PTC1 to -7 ) with diverse functions can be found. More recently, data on several Candida albicans PP2C proteins became available, suggesting that some of them can be involved in virulence. In this work we review the available literature on fungal PP2Cs and explore sequence databases to provide a comprehensive overview of these enzymes in fungi.
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Yoshida, Takuya, Kazuki Yamazaki, Shunta Imai, Akinori Banno, Atsushi Kaneko, Kazuhiro Furukawa y Yoshiro Chuman. "Identification of a Specific Inhibitor of Human Scp1 Phosphatase Using the Phosphorylation Mimic Phage Display Method". Catalysts 9, n.º 10 (11 de octubre de 2019): 842. http://dx.doi.org/10.3390/catal9100842.

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Protein phosphatases are divided into tyrosine (Tyr) phosphatases and serine/threonine (Ser/Thr) phosphatases. While substrate trapping mutants are frequently used to identify substrates of Tyr phosphatases, a rapid and simple method to identify Ser/Thr phosphatase substrates is yet to be developed. The TFIIF-associating component of RNA polymerase II C-terminal domain (CTD) phosphatase/small CTD phosphatase (FCP/SCP) phosphatase family is one of the three types of Ser/Thr protein phosphatases. Defects in these phosphatases are correlated with the occurrence of various diseases such as cancer and neuropathy. Recently, we developed phosphorylation mimic phage display (PMPD) method with AlF4−, a methodology to identify substrates for FCP/SCP type Ser/Thr phosphatase Scp1. Here, we report a PMPD method using BeF3− to identify novel substrate peptides bound to Scp1. After screening peptide phages, we identified peptides that bound to Scp1 in a BeF3−-dependent manner. Synthetic phosphopeptide BeM12-1, the sequence of which was isolated at the highest frequency, directly bound to Scp1. The binding was inhibited by adding BeF3−, indicating that the peptide binds to the active center of catalytic site in Scp1. The phosphorylated BeM12-1 worked as a competitive inhibitor of Scp1. Thus, PMPD method may be applicable for the identification of novel substrates and inhibitors of the FCP/SCP phosphatase family.
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Andreeva, Alexandra V. y Mikhail A. Kutuzov. "PPEF/PP7 protein Ser/Thr phosphatases". Cellular and Molecular Life Sciences 66, n.º 19 (7 de agosto de 2009): 3103–10. http://dx.doi.org/10.1007/s00018-009-0110-7.

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Seok, Seung-Hyeon. "Structural Insights into Protein Regulation by Phosphorylation and Substrate Recognition of Protein Kinases/Phosphatases". Life 11, n.º 9 (13 de septiembre de 2021): 957. http://dx.doi.org/10.3390/life11090957.

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Protein phosphorylation is one of the most widely observed and important post-translational modification (PTM) processes. Protein phosphorylation is regulated by protein kinases, each of which covalently attaches a phosphate group to an amino acid side chain on a serine (Ser), threonine (Thr), or tyrosine (Tyr) residue of a protein, and by protein phosphatases, each of which, conversely, removes a phosphate group from a phosphoprotein. These reversible enzyme activities provide a regulatory mechanism by activating or deactivating many diverse functions of proteins in various cellular processes. In this review, their structures and substrate recognition are described and summarized, focusing on Ser/Thr protein kinases and protein Ser/Thr phosphatases, and the regulation of protein structures by phosphorylation. The studies reviewed here and the resulting information could contribute to further structural, biochemical, and combined studies on the mechanisms of protein phosphorylation and to drug discovery approaches targeting protein kinases or protein phosphatases.
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DESDOUITS, Frédéric, C. Julio SICILIANO, C. Angus NAIRN, Paul GREENGARD y Jean-Antoine GIRAULT. "Dephosphorylation of Ser-137 in DARPP-32 by protein phosphatases 2A and 2C: different roles in vitro and in striatonigral neurons". Biochemical Journal 330, n.º 1 (15 de febrero de 1998): 211–16. http://dx.doi.org/10.1042/bj3300211.

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DARPP-32 (dopamine- and cAMP-regulated phosphoprotein, Mr = 32000) is highly expressed in striatonigral neurons in which its phosphorylation is regulated by several neurotransmitters including dopamine and glutamate. DARPP-32 becomes a potent inhibitor of protein phosphatase 1 when it is phosphorylated on Thr-34 by cAMP- or cGMP-dependent protein kinases. DARPP-32 is also phosphorylated on Ser-137 by protein kinase CK1 (CK1), in vitro and in vivo. This phosphorylation has an important regulatory role since it inhibits the dephosphorylation of Thr-34 by calcineurin in vitro and in striatonigral neurons. Here, we show that DARPP-32 phosphorylated by CK1 is a substrate in vitro for protein phosphatases 2A and 2C, but not protein phosphatase 1 or calcineurin. However, in substantia nigra slices, dephosphorylation of Ser-137 was markedly sensitive to decreased temperature, and not detectably affected by the presence of okadaic acid under conditions in which dephosphorylation of Thr-34 by protein phosphatase 2A was inhibited. These results suggest that, in neurons, phospho-Ser-137-DARPP-32 is dephosphorylated by protein phosphatase 2C, but not 2A. Thus, DARPP-32 appears to be a component of a regulatory cascade of phosphatases in which dephosphorylation of Ser-136 by protein phosphatase 2C facilitates dephosphorylation of Thr-34 by calcineurin, removing the cyclic nucleotide-induced inhibition of protein phosphatase 1.
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Kutuzov, Mikhail A. y Alexandra V. Andreeva. "Protein Ser/Thr phosphatases of parasitic protozoa". Molecular and Biochemical Parasitology 161, n.º 2 (octubre de 2008): 81–90. http://dx.doi.org/10.1016/j.molbiopara.2008.06.008.

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IWANICKI, Adam, Anna HERMAN-ANTOSIEWICZ, Marcin PIERECHOD, Simone J. SÉROR y Michał OBUCHOWSKI. "PrpE, a PPP protein phosphatase from Bacillus subtilis with unusual substrate specificity". Biochemical Journal 366, n.º 3 (15 de septiembre de 2002): 929–36. http://dx.doi.org/10.1042/bj20011591.

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Bacillus subtilis is a Gram-positive bacterium with a relatively large number of protein phosphatases. Previous studies have shown that some Ser/Thr phosphatases play an important role in the life cycle of this bacterium [Losick and Stragier (1992) Nature (London) 355, 601—604; Yang, Kang, Brody and Price (1996) Genes Dev. 10, 2265—2275]. In this paper, we report the biochemical properties of a putative, previously uncharacterized phosphatase, PrpE, belonging to the PPP family. This enzyme shares homology with other PPP phosphatases as well as with symmetrical diadenosine tetraphosphatases related to ApaH (symmetrical Ap4A hydrolase) from Escherichia coli. A His-tagged recombinant PrpE was purified from E. coli and shown to have Ni2+-dependent and okadaic acid-resistant phosphatase activity against a synthetic phosphorylated peptide and hydrolase activity against diadenosine 5′,5′′′-tetraphosphate. Unexpectedly, PrpE was able to remove phosphate from phosphotyrosine, but not from phosphothreonine or phosphoserine.
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Sun, Haipeng y Yibin Wang. "Novel Ser/Thr Protein Phosphatases in Cell Death Regulation". Physiology 27, n.º 1 (febrero de 2012): 43–52. http://dx.doi.org/10.1152/physiol.00034.2011.

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Cell death is regulated by a myriad of intracellular molecular pathways, with many involving protein phosphorylation and dephosphorylation. In this review, we will focus on Ser/Thr phosphatases-mediated regulation in cell apoptosis as well as on their potential roles in cell necrosis. The emerging functional importance of Ser/Thr protein phosphatases in cell death regulation adds new dimension to the signaling mechanisms of cellular function, physiology, and diseases.
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Pyo, Jaehyuk, Jaewook Ryu, Wootae Kim, Jae-Sun Choi, Joo-Won Jeong y Ja-Eun Kim. "The Protein Phosphatase PPM1G Destabilizes HIF-1α Expression". International Journal of Molecular Sciences 19, n.º 8 (5 de agosto de 2018): 2297. http://dx.doi.org/10.3390/ijms19082297.

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Hypoxia-inducible factors (HIFs) are key regulators of hypoxic responses, and their stability and transcriptional activity are controlled by several kinases. However, the regulation of HIF by protein phosphatases has not been thoroughly investigated. Here, we found that overexpression of Mg2+/Mn2+-dependent protein phosphatase 1 gamma (PPM1G), one of Ser/Thr protein phosphatases, downregulated protein expression of ectopic HIF-1α under normoxic or acute hypoxic conditions. In addition, the deficiency of PPM1G upregulated protein expression of endogenous HIF-1α under normoxic or acute oxidative stress conditions. PPM1G decreased expression of HIF-1α via the proteasomal pathway. PPM1G-mediated HIF-1α degradation was dependent on prolyl hydroxylase (PHD), but independent of von Hippel-Lindau (VHL). These data suggest that PPM1G is critical for the control of HIF-1α-dependent responses.
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Tesis sobre el tema "Thr protein phosphatases"

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Haj, Slimane Ammar Zeineb. "Dynamique Spatiotemporelle de la protéine kinase AMPc dépendante dans les myocytes cardiaques". Phd thesis, Université Paris Sud - Paris XI, 2012. http://tel.archives-ouvertes.fr/tel-00954406.

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La protéine kinase AMPc-dépendante (PKA) joue un rôle crucial dans la régulation neurohormonale de la fonction cardiaque. L'activation aiguë de la PKA est bénéfique car elle conduit à une augmentation de la contraction cardiaque en phosphorylant les acteurs clés du couplage excitation-contraction. En revanche, son activation chronique est délétère et ces effets semblent faire intervenir la régulation de protéines nucléaires pouvant conduire au remodelage hypertrophique et à l'insuffisance cardiaque. La localisation subcellulaire de la PKA, assurée par des protéines d'ancrage (AKAPs), est importante pour la rapidité et la spécificité d'action des hormones mettant en jeu la voie de l'AMPc. Les niveaux d'AMPc sont régulés par l'activité des adénylate cyclases et des phosphodiestérases (PDEs), et l'état de phosphorylation des protéines cibles de la PKA dépend de l'activité des Ser/Thr phosphatases (PPs). Dans le cœur, les PDEs les plus importantes dégradant l'AMPc sont les PDE3 et les PDE4. Les principales PPs cardiaques sont PP1, PP2A et PP2B. Dans une première partie de mon travail, j'ai mis au point, dans les cardiomyocytes de rats adultes, une mesure de l'activité de la PKA en temps réel dans les compartiments cytoplasmiques et nucléaires. J'ai utilisé pour cela des sondes de type AKAR (A-kinase activity reporters) basées sur le transfert d'énergie de fluorescence (FRET) et localisées spécifiquement dans le noyau ou dans le cytoplasme par des séquences d'adressage ou d'exclusion nucléaires. J'ai ainsi pu montrer qu'une stimulation maintenue des récepteurs β-adrénergiques active la PKA de façon plus importante dans le cytoplasme que dans le noyau, et que cette activation se développe lentement au niveau nucléaire que dans le cytoplasme. De ce fait, une stimulation brève des récepteurs β-adrénergiques active maximalement la PKA dans le cytoplasme, mais de façon marginale dans le noyau. Dans une seconde partie de l'étude, je me suis intéressée au rôle des PDE3 et PDE4 ainsi qu'à celui de PP1, PP2A et PP2B dans la régulation de l'activité PKA cytoplasmique et nucléaire, en réponse à une stimulation β-adrénergique. J'ai montré que la PDE4, mais pas la PDE3, régule l'activité de la PKA cytoplasmique et nucléaire. L'utilisation de souris invalidées pour les gènes Pde4b et Pde4d a révélé que l'isoforme PDE4B est prédominante pour la modulation de l'activité PKA cytoplasmique, alors que les deux isoformes PDE4B et PDE4D contribuent à la régulation de l'activité PKA nucléaire. Finalement, j'ai montré que la PP1 et la PP2A, mais pas la PP2B, participent à la terminaison des réponses β-adrénergiques dans le cytoplasme, alors qu'au niveau nucléaire, la PP1 semble jouer un rôle majeur. En conclusion, ce travail a mis en évidence le rôle des phosphodiestérases et des phosphatases dans l'intégration différentielle des réponses PKA à une stimulation β-adrénergique dans le cytoplasme et le noyau de cardiomyocytes adultes.
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Galioot, Amandine. "Contribution à l'étude du rôle des SER/THR protéine-phosphatases PP1/PP2A dans les processus de mort cellulaire et de maturation du précurseur du peptide Beta-Amyloïde". Paris 7, 2013. http://www.theses.fr/2013PA077219.

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Notre laboratoire a précédemment proposé un concept appelé "Drug phosphatase Technology" (DPT) basé sur l'utilisation de séquences pénétrantes cationiques capables d'interagir avec les phosphatases PP1/PP2A pour déréguler spécifiquement des signaux intracellulaires. Les Ser. Thr protéine-phosphatases PP1 et PP2A sont des acteurs clé de la signalisation cellulaire et la dérégulation de leur activité via leur interaction avec des partenaires d'origine cellulaire ou virale conduit souvent à de graves dysfonctionnements. Par exemple, la protéine E4orf4 des adénovirus interagit avec PP2A1 et entraîne l'apoptose des cellules infectées ou transformées alors que les cellules saines ne sont pas affectées. Lors de cette étude nous avons identifié une séquence d'interaction entre E4orf4 et PP2A1 à partir de laquelle nous avons caractérisé le peptide DPT-E4orf44, qui provoque l'apoptose de certaines cellules tumorales humaines sans affecter les cellules saines de type fibroblastes. Les protéine-phosphatases de la famille PP1 et PP2A jouent également un rôle important dans la régulation physiologique des substrats neuronaux Tau et APP (précurseur de peptide amyloïde). La diminution de l'activité phosphatase dans les cellules nerveuses entraine une augmentation de l'état de phosphorylation de ces substrats chez les patients atteints de la maladie d'Alzheimer. La deuxième partie de ce travail de thèse a permis de mettre en évidence l'implication les protéine-phosphatases PP1 et PP2A dans la régulation de la phosphorylation du résidu T668 d'APP dont la modification post-traductionnelle est essentielle pour la maturation et le clivage de l'APP
OuTlabhas previousry proposed a concept denominated "Drug Phosphatase Technology" (DFT) based on the use of cationic penetrating sequences capable of interacting with PP1/PP2A phosphatases in order to deregulate specific intracellular signais Ser/Thr proteins-phosphatases of PP1 and PP2A family are key factors of the cellular signalization and deregulation of their activity through interaction with cellular or viral protein often leads to severe dysfunctions. For exemple, E4orf4 protein of adenoviruses interacts with PP2A1 and leads to apoptotic death in infected or transformed cells while healthy cells remain unaffected. In a first part of this work, we have identified an interacting sequence between PP2A1 and E4orf4 from which we - have characterized the peptide DFT-F4orf44, which provokes the apoptosis of a subset of human tumoral cellswithout affecting healthy cells of fibroblastic type. Protein-phosphatases of PP1 and PP2A family also play a crucial role in the physiological regulation of neuronal substracts Tau and APP (Amylold Peptid Precursor). A diminution of the phosphatase activity in nerve cells leads to a drastically increasjng of phosphorylation state of these proteins for patients affected by Alzheimer's disease. I The second part of this work has allowed the identification of the phosphatase proteins responsible for the regulation of phosphorylation of APP T668 residue, which is an essential modification for APP maturation and processing
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Tan, Yves S. H. "Regulation of the type 1 protein phosphatase in saccharomyces cerevisiae". free to MU campus, to others for purchase, 2001. http://wwwlib.umi.com/cr/mo/fullcit?p3013031.

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Rivera, Reyes Brenda Mariola. "Regulation of the TCR signaling pathway". Connect to text online, 2006. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=case1132588714.

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Mills, Elena Claire. "Characterisation of the trypanosomatid PPEF-like phosphatases : novel members of the RDGC/PP5-related protein phosphatase family". Thesis, Imperial College London, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.423156.

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Lee, Gui-in. "Structure and dynamics of the receptor kinase interacting FHA domain of kinase associated protein kinase from arabidopsis". Free to MU campus, others may purchase, 2003. http://wwwlib.umi.com/cr/mo/fullcit?p3100058.

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Conde, Rui Miguel Esteves Antunes Seabra. "Protein phosphatases acting on the replication checkpoint". Doctoral thesis, Universidade de Aveiro, 2010. http://hdl.handle.net/10773/3494.

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Doutoramento em Biologia
A génese de um cancro está dependente da acumulação de mutações genéticas que dão origem a instabilidade genómica, que por sua vez resulta na proliferação descontrolada. Para prevenir a acumulação destas mutações, as células têm mecanismos de controlo (checkpoints) que suspendem o ciclo celular e accionam as vias de reparação do ADN. Estes eventos são muitas vezes regulados por dinâmicas de (des)fosforilação de proteínas. As proteínas fosfatases (PPs), enzimas responsáveis pela remoção do grupo fosfato de resíduos fosforilados, desempenham funções cruciais na regulação de muitos mecanismos celulares. Enquanto que no início do projecto as cinases envolvidas no checkpoint da replicação estavam bem estabelecidas, as PPs envolvidas não eram conhecidas. A Chk1, um componente da maquinaria do checkpoint da replicação, é exemplo dessa regulação por (des)fosforilação, como sejam nos resíduos Ser317 e Ser345. Assim, como primeira abordagem para determinar quais os grupos de PPs envolvidos na regulação do checkpoint da replicação, decidimos investigar o seu papel na regulação da fosforilação da Chk1. A primeira conclusão é que a desfosforilação da Chk1 ao longo do tempo, tanto in vivo como in vitro, ocorre com uma dinâmica bi-fásica. Em segundo, a abordagem in vitro sugere que as famílias PP1, PP2A e PP2C estão envolvidas na desfosforilação da Chk1. Uma vez que a família PP2A foi a que mostrou a maior acção nesta reacção, decidimos investigar outros membros da família in vivo, primeiro com uma abordagem geral (tratando com OA ou sobreexpressando a PME-1), e depois com o knockdown específico da PP4 e PP6 (através de siRNA). Os resultados mostram que a inibição das PPs afectam tanto a desfosforilação como o estado de activação da Chk1 em resposta a tratamento com Hidroxiureia (HU). Todas as PPs testadas in vivo pareceram ser capazes de regular, a níveis diferentes, tanto a fosforilação como a desfosforilação da Chk1. A função das PPs foi também investigada ao nível: da regulação do disparo das origens de replicação, e da recuperação da suspensão da replicação, induzida pela HU. No último caso, os dados indicam que na situação simultânea de knockdown da PP4 com tratamento de HU, há um atraso do ciclo celular na resolução da transição de G2/M. No ensaio de replicação por pulse-chase, os resultamos mostram que tanto o tratamento com OA, como a sobre-expressão de I-2 ou PME-1, atrasam a cronologia do disparo programado das origens de replicação. No entanto, nenhum dos tratamentos efectuados parece desregular o início do checkpoint da replicação. Um rastreio de 2-híbrido de levedura com uma biblioteca de cDNA de testículo humano foi realizado, usando a Chk1 como isco, no sentido de descobrir novos interactores e definir novas possíveis funções para a Chk1 no contexto da meiose. Com base nos resultados do rastreio, duas novas funções são sugeridas: a interacção com a GAGE12 sugere uma função na recombinação genómica/vigilância do genoma durante a meiose, e as interacções com a EEF1α1 e a RPS5 sugerem uma função na regulação da síntese proteíca. Estas experiências fornecem um visão geral para a compreensão da diversidade de funções das proteínas fosfatases envolvidas no checkpoint da replicação, bem como, abre novos caminhos para o desenvolvimento de novas drogas para o tratamento do cancro.
The emergence of cancer is dependent on the accumulation of small numbers of genetic mutations that give rise to genomic instability, which in turn results in uncontrolled cell proliferation. To prevent the accumulation of such mutations and the evolution into a cancer state, cells operate checkpoints by arresting the cell cycle and triggering the DNA repair pathways. Often these events are regulated by protein (de)phosphorylation dynamics. Protein phosphatases (PPs), enzymes responsible for removing the phosphate from phosphorylated residues, play key roles in the regulation of many cellular mechanisms. While at the beginning of the project the kinases involved in the replication checkpoint were well established, PPs involved in the regulation of this pathway were not known. Chk1, a key component of the replication checkpoint machinery, is an example of regulation by (de)phosphorylation at several residues, such as Ser317 and Ser345. Hence, as a first approach to determine which PPs could be involved in the regulation of the replication checkpoint, we decided to investigate their role in the regulation of Chk1 phosphorylation state. The first finding from our study was that Chk1 dephosphorylation time course, both in vivo and in vitro, occurred with a bi-phasic dynamics. Secondly, a preliminary in vitro approach suggested that PP1, PP2A and PP2C families are involved in Chk1 dephosphorylation. Given that PP2A was shown to be the major contributor for this reaction, we investigated close family members in vivo, first by a general approach (either with OA treatment or PME-1 overexpression), and then by specific knockdown using siRNA for PP4 and PP6. Our data shows that besides affecting Chk1 dephosphorylation, the inhibition of PPs also affects Chk1 activation state in response to Hydroxyurea treatment. All the protein phosphatases tested in vivo seemed, to some extent, to be able to regulate either Chk1 phosphorylation or dephosphorylation. The PPs function was also investigated at the level of replication origin-firing regulation and the recovery from HU-induced replication arrest. In the latter study, our results indicate that PP4 knockdown triggers a HU-dependent cell cycle arrest in G2/M. In the pulse-chase replication assay, we show that OA treatment as well as I-2 or PME-1 overexpression, delay the timing of the normal replication origin-firing. None of the treatments performed seemed to abrogate the onset of the replication checkpoint. We have also performed a Yeast Two-hybrid screen in a human testis cDNA library using Chk1 as bait, in order to find novel interactors and identify new Chk1 putative functions in the context of meiosis. From this screen, two new Chk1 functions were defined due to the new putative interactions. Hence, the interaction with GAGE12 suggests a function in genomic recombination/ surveillance in meiosis and the interactions with both EEF1α1 and RPS5 suggest a function in protein synthesis regulation. These experiments provide a framework for understanding the diversity of the protein phosphatase functions involved in the replication checkpoint, as well as, for opening new avenues for the development of new drugs for cancer therapy.
FCT (POCI 2010) / FSE - SFRH/BD/11310/2002
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Luechapanichkul, Rinrada. "Determination of the Sequence Specificity and Protein Substrates of Protein Phosphatases". The Ohio State University, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=osu1398868380.

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Davis, Anthony John. "Characterization of the protein phosphatase 2A regulatory subunit PR70". Access to abstract only; dissertation is embargoed until after 12/19/2006, 2005. http://www4.utsouthwestern.edu/library/ETD/etdDetails.cfm?etdID=123.

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Bemporad, Francesco. "Folding and aggregation studies in the acylphosphatase-like family /". Firenze : Firenze University Press, 2009. http://digital.casalini.it/9788884539465.

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Libros sobre el tema "Thr protein phosphatases"

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International Conference on Second Messengers and Phosphoproteins (12th 2004 Montréal, Québec). Second messengers and phosphoprotein signaling: Proceedings of the 12th International Conference on Second Messengers and Phosphoproteins : Montreal, Canada, August 3-7, 2004. Editado por Anand-Srivastava Madhu B, Tremblay Michel y Srivastava Ashok K. Bologna: Medimond International Proceedings, 2004.

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Yuen, Kenneth Wing Hon. Analyses of the roles of protein tyrosine phosphatase SHP-2 and SLAM-associated protein (SAP) in regulation of T cell functions. Ottawa: National Library of Canada, 2002.

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Swain, James Edward. The effects of okaidic acid, a protein phosphatase inhibitor, on synaptic transmission at the crayfish neuromuscular junction. Ottawa: National Library of Canada, 1990.

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Tsiani, Evangelia. Regulation of metabolic effects in L6 muscle cells by sulfonylureas and the protein tyrosine phosphatase inhibitors vanadate and pervanadate. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1997.

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5

Hoof, C. Van. Prpa - a Protein Controlling the Dual Specificity of Protein Phosphatase. Leuven University Press, 1994.

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Waelkens, E. Regulation and Specificity of the Polycation-Stimulated Protein Phosphatases. Leuven University Press, 1988.

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Janssens, Veerle. Promoter Analysis and Characterization of Novel Splice Variants of the Human Phosphotyrosyl Phosphatase Activator Gene. Leuven Univ Pr, 2000.

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Jagiello, I. The Structure and Regulation of Protein Phosphatase-1 in the Nucleus. Leuven University Press, 1998.

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Wera, S. Purification and Characterisation of the Glycogen-Bound Protein Phosphatase from Rat Liver. Leuven University Press, 1991.

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Bollen, M. The Structure and Regulation of Type-1 Protein Phosphatases Involved in Hepatic Glycogen Metabolism. Leuven University Press, 1991.

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Capítulos de libros sobre el tema "Thr protein phosphatases"

1

Ariño, Joaquin, Francesc Posas y Josep Clotet. "The Search for the Biological Function of Novel Yeast Ser/Thr Phosphatases". En Protein Phosphatase Protocols, 305–13. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1385/0-89603-468-2:305.

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Inouye, Sumiko, Hirofumi Nariya y José Muñoz-Dorado. "Protein Ser/Thr Kinases and Phosphatases in Myxococcus xanthus". En Myxobacteria, 191–210. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555815677.ch11.

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Alexander, Denis R. "The CD45 phosphotyrosine phosphatase". En Protein Phosphatases, 231–52. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-40035-6_12.

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Chinkers, Michael. "PP5: the TPR phosphatase". En Protein Phosphatases, 107–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-40035-6_6.

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Lai, Lisa A., Chunmei Zhao, Eric E. Zhang y Gen-Sheng Feng. "The Shp-2 tyrosine phosphatase". En Protein Phosphatases, 275–99. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-40035-6_14.

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Alonso, Andres, Ana Rojas, Adam Godzik y Tomas Mustelin. "The dual-specific protein tyrosine phosphatase family". En Protein Phosphatases, 333–58. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-40035-6_16.

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Bourdeau, Annie, Krista M. Heinonen, Daniel V. Brunet, Pankaj Tailor, Wayne S. Lapp y Michel L. Tremblay. "Structure and function of the T-cell protein tyrosine phosphatase". En Protein Phosphatases, 185–200. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-40035-6_10.

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Hilioti, Zoe y Kyle W. Cunningham. "Calcineurin: Roles of the Ca2+/calmodulindependent protein phosphatase in diverse eukaryotes". En Protein Phosphatases, 73–90. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-40035-6_4.

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Tamura, Shinri, Ming Guang Li, Ken-ichiro Komaki, Masato Sasaki y Takayasu Kobayashi. "Roles of mammalian protein phosphatase 2C family members in the regulation of cellular functions". En Protein Phosphatases, 91–105. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-540-40035-6_5.

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Robinson, Matthew K. y Eric M. Phizicky. "Purification and Assay of the Ptc1/Tpd1 Protein Phosphatase 2C from the Yeast Saccharomyces cerevisiae". En Protein Phosphatase Protocols, 235–42. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1385/0-89603-468-2:235.

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Actas de conferencias sobre el tema "Thr protein phosphatases"

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Sakon, M., Y. Uemura, K. Suga, T. Tsujinaka, J. Kambayashi y T. Mori. "STUDIES ON PHOSPHATASES IN HUMAN PLATELETS". En XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644494.

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Activation of platelets by various agonists has been ascribed to be associated with phosphorylation and dephosphorylation of specific proteins such as 20K and 47K polypeptide. Although protein kinases such as myosin light chain kinase and C kinase have been extensively studied, little information is currently available on platelet phosphatases, which may play a crucial role in the regulation of stimulus-linked protein phosphorylation. Thereby, the present study was conducted to know some characters of platelet phosphatases. Glycerol loaded platelets prepared from human platelet concentrates were subjected to osmotic lysis in 20 mM HEPES-NaOH buffer containing 5 mM EDTA, 0.5 mM dithio-threitol and various protease inhibitors and a soluble fraction was obtained by centrifugation, The activity of phosphatase was assayed at pH 7.35, using paranitrophenylphosphate as a substrate. Leupeptin and EDTA were added to the reaction mixture to avoid proteolytic attack to the enzyme. The neutral phosphatase was partially purified from the soluble fraction by a combination of ammonium sulfate fractionation and column chromatographies. Five distinct peaks with neutral phosphatase activity were obtained by a linear gradient elution ( 0−0.5 M KCl ) in DEAE Sepharose CL-6B of 0−60 % ammonium sulfate precipitate. The phosphatase activity of one peak eluted at 0.2M KCl was maximum at pH below 6, which was considered to be acid phosphatase, and the remaining four peaks' optimal pH was between 7.0−7.5. These four peaks were termed as PH-I (passed through fraction), PH-II (0.1M KCl), PH-III (0.25M KCl) and PH-IV (0.3M KCl). The respective peak was eluted as a single peak on Ultrigel AcA 34 and the molecular weight was estmated as follows; I-55K, II-40K, III-55K, IV-37K. PH-I − II were active in the presnce of EDTA and were not affect ed by divalent cations (Mg++ , Mn++ , Ca++ ) , whereas PH-III was highly dependent upon Mg++. The activity of PH-IV was completely dependent on Mn++. From these observations, the following conclusions were obtained; (1) Human platelets contain four species of neutral phosphatases, in addition to acid phosphatase. (2) Each neutral phosphatase is distincive by molecular weight and requirement of divalent cations.
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2

Molina, Luis, y. Vedia y Eduardo G. Lapetina. "ENZYMES THAT DEPHOSPHORYLATE INOSITOL PHOSPHATES IN HUMAN PLATELETS". En XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644522.

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Inositol trisphosphate (IP3) is now recognized as a second messenger molecule that mobilizes Ca2+ from intracellular stores to the cytosol. The persistence of the action of IP3 depends on the specific phosphatase that converts IP3 to inositol bisphosphate (IP2). The activation of IP3 phosphatase is important in terminating the Ca2+ signal in stimulated cells. In platelets it has previously been shown that this enzyme is regulated by protein kinase C since it is stimulated by phorbol esters and 1,2-diacylglycerol (Molina y Vedia, L., and Lapetina, E.G. J. Biol Chem. 261, 10493-10495, 1986) and the cytosolic platelet enzyme is phosphorylated by brain protein kinase C, resulting in a 4-fold increase in IP3 phosphatase activity (Connolly, T. M., Lawing, W.J., Jr., and Majerus, P.W., Cell, 46, 951-958, 1986). We have studied the subcellular distribution of the phosphatases that hydrolyze IP3, IP2 and inositol monophosphate (IP) in human platelets. Three subcellular fractions were obtained from human platelets lysed by freezing and thawing: a cytosolic fraction, a membrane fraction and a mixed particulate fraction containing granules, mitochondria and membranes. These fractions have been characterized by specific marker enzymes. The highest specific activity of IP3 -phosphatase is associated with the membrane fraction and accounts for about 10-15% of the total activity. The mixed particulate fraction has 35-40% of the activity while about 50% is cytosolic. The Km of the membrane fraction enzyme is 100 μM. This enzyme is extracted by 1M NaCl and hydrodynamic studies revealed a molecular weight of 50 kDa. The NaCl extracted-enzyme has been further purified by hydrophobic and gel filtration chromatographies. This activity does not hydrolyses IP but hydrolyse IP2 at a lower rate. The enzyme that hydrolyses IP to inositol is confined to the cytosolic fraction, has a Km of 130 μM, is inhibited by Li+, and hydrodynamic studies show an apparent molecular weight of 91 kDa.
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Wallace, Robert W., E. Ann Tallant y Lynn M. Brumley. "POSSIBLE ROLE FOR THE CA2+-DEPENDENT PROTEASE (CALPAIN I) AS AN IRREVERSIBLE ACTIVATOR OF CA2+/CALMODULIN-MEDIATED REACTIONS IN THE HUMAN PLATELET". En XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644528.

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Calmodulin (CaM)-binding proteins have been identified in human platelets using Western blotting techniques and 125I-CaM. Ten proteins of 245, 225. 175, 150, 90. 82(2), 60 and 41(2) kilodaltons (kDa) bind 125I-CaM in a Ca2+-dependent manner; the binding is blocked by both trifluoperazine and nonradiolabeled CaM. The 225 and 90 kDa proteins are labeled by antisera against myosin light chain kinase (MLCK); the 60 kDa and one of the 82 kDa proteins have been identified as the CaM-dependent phosphatase (calcineurin) and caldesmon. The other proteins are presumed to be other Ca2+/CaM regulated enzymes and proteins which may be important in platelet function. Most of the CaM-binding proteins are degraded upon addition of Ca2+ to a platelet homogenate; the degradation may be blocked by either EGTA, leupeptin or N-ethylmaleimide which suggests that the degradation is due to a Ca2+-dependent protease. Activation of intact platelets under conditions which promote platelet aggregation (i.e. stirring with extracellular Ca2+) also results in limited proteolysis of CaM-binding proteins including those labeled with anti sera against MLCK and the phosphatase. In vitro studies utilizing purified phosphatase and calpain I indicate that the phosphatase is irreversibly activated upon Ca2+-dependent proteolysis. The proteolytically-activated enzyme is insensitive to either Ca2+ or Ca2+/CaM; in addition, its activity in the absence of Ca2+ is even greater than the activity of the unproteolyzed enzyme in the presence of Ca2+ and CaM. Proteolytic stimulation of the phosphatase is accompanied by degradation of the 60 kDa subunit of the enzyme (subunit A) to 56, 52 and 45 kDa fragments, sequentially; proteolysis results in the loss of CaM binding to the enzyme. These results suggest that the Ca2+-dependent protease may have a physiological role in platelet activation as an irreversible activator of Ca2+/ CaM-dependent reactions. Supported by NIH grant HL29766.
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Kuban-Jankowska, Alicja, Magdalena Gorska-Ponikowska y Pawel Niedzialkowski. "The oxidation-reduction reactions in regulation of protein tyrosine phosphatases activity". En RECENT ADVANCES ON ENVIRONMENT, CHEMICAL ENGINEERING AND MATERIALS. Author(s), 2018. http://dx.doi.org/10.1063/1.5060694.

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"The protein Tyrosine Phosphatase N22 variation and risk of Endometriosis". En International Conference on Medicine, Public Health and Biological Sciences. CASRP Publishing Company, Ltd. Uk, 2016. http://dx.doi.org/10.18869/mphbs.2016.113.

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Taylor, Derek y Goutham Narla. "Abstract 3403: Drugging the undruggable: Lessons learned from protein phosphatase 2A". En Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-3403.

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Moake, J. L., M. A. Harris, C. E. Whitley y C. P. Alfrey. "RAPID, SENSITIVE N0N-RADI0ACTIVE QUANTIFICATION AND ANALYSIS OF PLASMA VON WILLEBRAND FACTOR (vWF) MULTIMERS". En XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644085.

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Assessment of plasma vWF abnormalities by clinical coagulation laboratories is difficult because the available test systems for vWF antigen quantification and multimer analysis are expensive, laborious, and require days, radioactive anti-vWF antibodies and autoradiographic methods. We have devised simple, rapid, sensitive alternative techniques for vWF quantification and multimer analysis that can be readily installed in clinical laboratories. Plasma vWF antigen quantification is by a 2 hour enzyme immunoassay that accurately detects levels as low as 0.23% of normal. Plasma vWF to be quantified is bound to polyclonal monospecific antihuman vWF attached to small glass beads, and anti-human vWF conjugated with alkaline phosphatase is added to make an insoluble "sandwich." A substrate solution consisting of phenylphosphate and 4-amino-antipurine is added, followed by potassium ferricyanide. Optical density (at 490-510 nm) of the red color that develops is directly proportional to the plasma concentration of vWF antigen. Plasma vWF multimeric analysis is by a one-day electrophoretic immunobiot procedure. Plasma vWF multimer forms are solubilized in SDS-urea-Tris-EDTA, separated by horizontal 1% agarose gel electrophoresis, and transferred to a cationic membrane. Other protein binding sites on the membrane are blocked with milk proteins, and the membrane is overlaid with anti-vWF IgG linked to alkaline phosphatase. vWF multimers are then displayed as blue bands by soaking the membrane in an alkaline solution of the histochemical stain, fast blue RR (commonly used for leukocyte alkaline phosphatase scoring) dissolved in naphtol AS-MX phosphate. These simple, non-radioactive procedures performed together permit the rapid distinction of classical (Type I) von Willebrand's disease (vWD), characterized by low vWF antigen and normal multimers, from the Type II vWD syndromes, characterized by a relative deficiency of the largest plasma vWF forms. Unusually large vWF multimers, present in remission plasma of patients with chronic relapsing thrombotic thrombocytopenic purpura (TTP), are also easily detected using this rapid system of multimer analysis.
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Rocha, Sónia, Eduarda Fernandes, Marisa Freitas, Daniela Ribeiro, Vera Silva, Pedro Gomes, Artur Silva, Alberto Araújo y M. Luísa Corvo. "Insight into the protein tyrosine phosphatase 1B (PTP1B) inhibitory activity of pyrazoles". En 6th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2020. http://dx.doi.org/10.3390/ecmc2020-07490.

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McCluskey, Adam, Mirella Keane, Alistair Sim y Jenette Sakoff. "Cantharidin: The Next Generation. Towards Selective Inhibitors of Protein Phosphatase 1 and 2A". En The 2nd International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 1998. http://dx.doi.org/10.3390/ecsoc-2-01697.

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Smith, Caroline N., K. Martin Chow, Louis B. Hersh, Daniel Deredge y Jessica S. Blackburn. "Abstract 2305: Development and validation of nanobodies specific to the oncogenic phosphatase protein tyrosine phosphatase 4A3 (PTP4A3 or PRL-3)". En Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-2305.

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Informes sobre el tema "Thr protein phosphatases"

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Sap, Jan M. The Role of RPTP-Alpha-Like Protein Tyrosine Phosphatases in Mammary Tumorigenesis. Fort Belvoir, VA: Defense Technical Information Center, mayo de 2001. http://dx.doi.org/10.21236/ada395401.

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Oliver, Carey y Shirish Shenolikar. The Essential Role of Protein Phosphatase-1 in Mitogenic Signaling and Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, julio de 2001. http://dx.doi.org/10.21236/ada398153.

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