Relevant bibliographies by topics / PXXP-motif

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  2. Dissertations / Theses

Academic literature on the topic 'PXXP-motif'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "PXXP-motif"

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Yang, Sung-Tae, Song-Yub Shin, and Sung-Heui Shin. "The Central PXXP Motif Is Crucial for PMAP-23 Translocation across the Lipid Bilayer." International Journal of Molecular Sciences 22, no. 18 (2021): 9752. http://dx.doi.org/10.3390/ijms22189752.

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PMAP-23, a cathelicidin-derived host defense peptide, does not cause severe membrane permeabilization, but exerts strong and broad-spectrum bactericidal activity. We have previously shown that it forms an amphipathic α-helical structure with a central hinge induced by the PXXP motif, which is implicated in the interaction of PMAP-23 with negatively charged bacterial membranes. Here, we studied the potential roles of the PXXP motif in PMAP-23 translocation across the lipid bilayer by replacing Pro residues with either α-helix former Ala (PMAP-PA) or α-helix breaker Gly (PMAP-PG). Although both
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2

Dornan, David, Harumi Shimizu, Lindsay Burch, Amanda J. Smith, and Ted R. Hupp. "The Proline Repeat Domain of p53 Binds Directly to the Transcriptional Coactivator p300 and Allosterically Controls DNA-Dependent Acetylation of p53." Molecular and Cellular Biology 23, no. 23 (2003): 8846–61. http://dx.doi.org/10.1128/mcb.23.23.8846-8861.2003.

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ABSTRACT The transcription coactivator p300 cannot acetylate native p53 tetramers, thus revealing intrinsic conformational constraints on p300-catalyzed acetylation. Consensus site DNA is an allosteric effector that promotes acetylation of p53, suggesting that p300 has an undefined conformationally flexible interface within the p53 tetramer. To identify such conformationally responsive p300-binding sites, p300 was subjected to peptide selection from a phage-peptide display library, a technique that can define novel protein-protein interfaces. The enriched p300-binding peptides contained a prol
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3

Winters, Matthew J., and Peter M. Pryciak. "Interaction with the SH3 Domain Protein Bem1 Regulates Signaling by the Saccharomyces cerevisiae p21-Activated Kinase Ste20." Molecular and Cellular Biology 25, no. 6 (2005): 2177–90. http://dx.doi.org/10.1128/mcb.25.6.2177-2190.2005.

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ABSTRACT The Saccharomyces cerevisiae PAK (p21-activated kinase) family kinase Ste20 functions in several signal transduction pathways, including pheromone response, filamentous growth, and hyperosmotic resistance. The GTPase Cdc42 localizes and activates Ste20 by binding to an autoinhibitory motif within Ste20 called the CRIB domain. Another factor that functions with Ste20 and Cdc42 is the protein Bem1. Bem1 has two SH3 domains, but target ligands for these domains have not been described. Here we identify an evolutionarily conserved binding site for Bem1 between the CRIB and kinase domains
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Khan, Imran H., Earl T. Sawai, Erwin Antonio, et al. "Role of the SH3-Ligand Domain of Simian Immunodeficiency Virus Nef in Interaction with Nef-Associated Kinase and Simian AIDS in Rhesus Macaques." Journal of Virology 72, no. 7 (1998): 5820–30. http://dx.doi.org/10.1128/jvi.72.7.5820-5830.1998.

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ABSTRACT The nef gene of the human and simian immunodeficiency viruses (HIV and SIV) is dispensable for viral replication in T-cell lines; however, it is essential for high virus loads and progression to simian AIDS (SAIDS) in SIV-infected adult rhesus macaques. Nef proteins from HIV type 1 (HIV-1), HIV-2, and SIV contain a proline-Xaa-Xaa-proline (PxxP) motif. The region of Nef with this motif is similar to the Src homology region 3 (SH3) ligand domain found in many cell signaling proteins. In virus-infected lymphoid cells, Nef interacts with a cellular serine/threonine kinase, designated Nef
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5

Boelaert, K., R. Yu, L. A. Tannahill, et al. "PTTG’s C-terminal PXXP motifs modulate critical cellular processes in vitro." Journal of Molecular Endocrinology 33, no. 3 (2004): 663–77. http://dx.doi.org/10.1677/jme.1.01606.

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Human pituitary tumor-transforming gene (PTTG), known also as securin, is a multifunctional protein implicated in the control of mitosis and the pathogenesis of thyroid, colon, oesophageal and other tumour types. Critical to PTTG function is a C-terminal double PXXP motif, forming a putative SH3-interacting domain and housing the gene’s sole reported phosphorylation site. The exact role of phosphorylation and PXXP structure in the modulation of PTTG action in vitro remains poorly understood. We therefore examined the mitotic, transformation, proliferation and transactivation function of the C-
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Xie, Liji, Zhixun Xie, Sheng Wang, Xianwen Deng та Zhiqin Xie. "Study of the activation of the PI3K/Akt pathway by the motif of σA and σNS proteins of avian reovirus". Innate Immunity 26, № 4 (2019): 312–18. http://dx.doi.org/10.1177/1753425919890648.

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The present study was conducted to determine whether avian reovirus (ARV) activates the phosphatidylinositol 3-kinase-dependent Akt (PI3K/Akt) pathway according to the PXXP or YXXXM motifs of σA and σNS proteins. Gene splicing by overlap extension PCR was used to change the PXXP or YXXXM motifs of the σA and σNS genes. Plasmid constructs that contain mutant σA and σNS genes were generated and transfected into Vero cells, and the expression levels of the corresponding genes were quantified according to immunofluorescence and Western blot analyses. The Akt phosphorylation (P-Akt) profile of the
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7

Meirson, Tomer, David Bomze, Liron Kahlon, Hava Gil-Henn, and Abraham O. Samson. "A helical lock and key model of polyproline II conformation with SH3." Bioinformatics 36, no. 1 (2019): 154–59. http://dx.doi.org/10.1093/bioinformatics/btz527.

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Abstract Motivation More than half of the human proteome contains the proline-rich motif, PxxP. This motif has a high propensity for adopting a left-handed polyproline II (PPII) helix and can potentially bind SH3 domains. SH3 domains are generally grouped into two classes, based on whether the PPII binds in a positive (N-to-C terminal) or negative (C-to-N terminal) orientation. Since the discovery of this structural motif, over six decades ago, a systematic understanding of its binding remains poor and the consensus amino acid sequence that binds SH3 domains is still ill defined. Results Here,
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8

Shin, Yeun-Kyung, Yang Li, Qiang Liu, Deborah H. Anderson, Lorne A. Babiuk, and Yan Zhou. "SH3 Binding Motif 1 in Influenza A Virus NS1 Protein Is Essential for PI3K/Akt Signaling Pathway Activation." Journal of Virology 81, no. 23 (2007): 12730–39. http://dx.doi.org/10.1128/jvi.01427-07.

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ABSTRACT Recent studies have demonstrated that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway by binding of influenza NS1 protein to the p85 regulatory subunit of PI3K. Our previous study proposed that two polyproline motifs in NS1 (amino acids 164 to 167 [PXXP], SH3 binding motif 1, and amino acids 213 to 216 [PPXXP], SH3 binding motif 2) may mediate binding to the p85 subunit of PI3K. Here we performed individual mutational analyses on these two motifs and demonstrated that SH3 binding motif 1 contributes to the interactions of NS1 with p
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9

Risse, Sarah L., Belen Vaz, Matthew F. Burton, et al. "SH3-mediated targeting of Wrch1/RhoU by multiple adaptor proteins." Biological Chemistry 394, no. 3 (2013): 421–32. http://dx.doi.org/10.1515/hsz-2012-0246.

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Abstract Wrch1/RhoU is an atypical member of the Rho family. A major structural difference is the extended N-terminus of Wrch1 (nWrch1) containing three putative SH3 domain-binding motifs whose specificities are unknown. To define the impact of this extended region on coupling Wrch1 to cellular signaling, we analyzed in this study nWrch1 interaction with Src homology 3 (SH3) domains of different adaptor proteins. Using sedimentation and isothermal titration calorimetric (ITC) measurements, we identified isolated SH3 domains of growth factor receptor-bound protein 2 (Grb2), noncatalytic region
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10

Shin, Yeun-Kyung, Qiang Liu, Suresh K. Tikoo, Lorne A. Babiuk, and Yan Zhou. "Influenza A virus NS1 protein activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by direct interaction with the p85 subunit of PI3K." Journal of General Virology 88, no. 1 (2007): 13–18. http://dx.doi.org/10.1099/vir.0.82419-0.

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Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway, but the mechanism is not clear. Here, it is reported that influenza A virus NS1 protein is responsible for PI3K/Akt pathway activation. It was demonstrated that the NS1 protein interacts with the p85 regulatory subunit of PI3K via direct binding to the SH3 and C-terminal SH2 domains of p85. Consensus binding motifs for SH3 and SH2 domains were found in influenza A virus NS1, namely an SH2-binding motif (YXXXM) at aa 89, SH3-binding motif 1 (PXXP) around aa 164 and SH3-binding motif 2 around aa 212. Muta
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Dissertations / Theses on the topic "PXXP-motif"

1

Petzhold, Daria. "Funktionelle Untersuchungen von Ahnak durch Protein-Protein-Wechselwirkungen und in Ahnak-Defizienzmodellen." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2007. http://dx.doi.org/10.18452/15694.

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Ahnak ist ein ubiquitäres Protein, das an einer Vielzahl biologischer Prozesse beteiligt ist. In der Herzmuskelzelle ist Ahnak überwiegend am Sarkolemma lokalisiert und bindet an Aktin und an die regulatorischen Beta2-Untereinheit des L-Typ-Kalzium-Kanals. Das Ziel dieser Arbeit war die Funktion von Ahnak im Herzen mit Hilfe eines Knock-out-Maus-Modells und in Bindungsstudien zu untersuchen. Morphologische Untersuchungen zeigten, dass das Längenwachstum adulter Kardiomyozyten bei Ahnakdefizienz signifikant reduziert war. Die Kontraktionseigenschaften adulter isolierter Ahnak-defizienter Kardi
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