Log in

Relevant bibliographies by topics / PXXP-motif / Journal articles

To see the other types of publications on this topic, follow the link: PXXP-motif.

Journal articles on the topic 'PXXP-motif'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 44 journal articles for your research on the topic 'PXXP-motif.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

4

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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-

APA, Harvard, Vancouver, ISO, and other styles

6

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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,

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

Abstract:

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

APA, Harvard, Vancouver, ISO, and other styles

11

Barletta, Frank, Chi-Wai Wong, Chris McNally, Barry S. Komm, Benita Katzenellenbogen, and Boris J. Cheskis. "Characterization of the Interactions of Estrogen Receptor and MNAR in the Activation of cSrc." Molecular Endocrinology 18, no. 5 (2004): 1096–108. http://dx.doi.org/10.1210/me.2003-0335.

Full text

Abstract:

Abstract In this study, we have evaluated the molecular mechanism of Src activation after its interaction with estrogen receptor α (ERα) and a newly identified scaffold protein, called MNAR (modulator of nongenomic activity of ER). Under basal condition, Src enzymatic activity is inhibited by intramolecular interactions. The enzyme can be activated by interaction between the SH2 domain of Src and phosphotyrosine-containing sequences and/or by interaction between the SH3 domain of Src and proteins containing PXXP motifs. Mutational analysis and functional evaluation of MNAR and the use of ERα a

APA, Harvard, Vancouver, ISO, and other styles

12

Sang, Yurou, Rui Zhang, A. Louise Creagh, Charles A. Haynes, and Suzana K. Straus. "Interactions of U24 from Roseolovirus with WW domains: canonical vs noncanonical." Biochemistry and Cell Biology 95, no. 3 (2017): 350–58. http://dx.doi.org/10.1139/bcb-2016-0250.

Full text

Abstract:

U24 is a C-terminal membrane-anchored protein found in both human herpes virus type 6 and 7 (HHV-6 and HHV-7), with an N-terminal segment that is rich in prolines (PPxY motif in both HHV-6A and 7; PxxP motif in HHV-6A). Previous work has shown that U24 interacts strongly with Nedd4 WW domains, in particular, hNedd4L-WW3*. It was also shown that this interaction depends strongly on the nature of the amino acids that are upstream from the PY motif in U24. In this contribution, data was obtained from pull-downs, isothermal titration calorimetry, and NMR to further determine what modulates U24:WW

APA, Harvard, Vancouver, ISO, and other styles

13

Togashi, Masaru, Shin Okuyama, Hideki Wakui, et al. "Interaction of Alpha-Actinin-4 with Class I PxxP Motif-Containing OK/SW-CL.16 Protein." Nephron Experimental Nephrology 107, no. 2 (2007): e65-e72. http://dx.doi.org/10.1159/000108644.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Hanna, Zaher, Xiaoduan Weng, Denis G. Kay, Johanne Poudrier, Clifford Lowell, and Paul Jolicoeur. "The Pathogenicity of Human Immunodeficiency Virus (HIV) Type 1 Nef in CD4C/HIV Transgenic Mice Is Abolished by Mutation of Its SH3-Binding Domain, and Disease Development Is Delayed in the Absence of Hck." Journal of Virology 75, no. 19 (2001): 9378–92. http://dx.doi.org/10.1128/jvi.75.19.9378-9392.2001.

Full text

Abstract:

ABSTRACT The human immunodeficiency virus type 1 (HIV-1) Nef protein is an important determinant of AIDS pathogenesis. We have previously reported that HIV-1 Nef is responsible for the induction of a severe AIDS-like disease in CD4C/HIV transgenic (Tg) mice. To understand the molecular mechanisms of this Nef-induced disease, we generated Tg mice expressing a mutated Nef protein in which the SH3 ligand-binding domain (P72XXP75XXP78) was mutated to A72XXA75XXQ78. This mutation completely abolished the pathogenic potential of Nef, although a partial downregulation of the CD4 cell surface expressi

APA, Harvard, Vancouver, ISO, and other styles

15

Wuertenberger, Silvia, and Yvonne Groemping. "A single PXXP motif in the C-terminal region of srGAP3 mediates binding to multiple SH3 domains." FEBS Letters 589, no. 10 (2015): 1156–63. http://dx.doi.org/10.1016/j.febslet.2015.03.014.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Bottger, Gina, Phil Barnett, AndréT J. Klein, Astrid Kragt, Henk F. Tabak, and Ben Distel. "Saccharomyces cerevisiae PTS1 Receptor Pex5p Interacts with the SH3 Domain of the Peroxisomal Membrane Protein Pex13p in an Unconventional, Non-PXXP–related Manner." Molecular Biology of the Cell 11, no. 11 (2000): 3963–76. http://dx.doi.org/10.1091/mbc.11.11.3963.

Full text

Abstract:

A number of peroxisome-associated proteins have been described that are involved in the import of proteins into peroxisomes, among which is the receptor for peroxisomal targeting signal 1 (PTS1) proteins Pex5p, the integral membrane protein Pex13p, which contains an Src homology 3 (SH3) domain, and the peripheral membrane protein Pex14p. In the yeast Saccharomyces cerevisiae, both Pex5p and Pex14p are able to bind Pex13p via its SH3 domain. Pex14p contains the classical SH3 binding motif PXXP, whereas this sequence is absent in Pex5p. Mutation of the conserved tryptophan in the PXXP binding po

APA, Harvard, Vancouver, ISO, and other styles

17

Shi, Xiaoli, Sandrine Opi, Adrien Lugari, et al. "Identification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein X." Biochemical Journal 431, no. 1 (2010): 93–102. http://dx.doi.org/10.1042/bj20100314.

Full text

Abstract:

SFKs (Src family kinases) are central regulators of many signalling pathways. Their functions are tightly regulated through SH (Src homology) domain-mediated protein–protein interactions. A yeast two-hybrid screen using SH3 domains as bait identified Alix [ALG-2 (apoptosis-linked gene 2)-interacting protein X] as a novel Hck (haemopoietic cell kinase) SH3 domain interactor. The Alix–Hck-SH3 interaction was confirmed in vitro by a GST (glutathione transferase) pull-down assay and in intact cells by a mammalian two-hybrid assay. Furthermore, the interaction was demonstrated to be biologically re

APA, Harvard, Vancouver, ISO, and other styles

18

Helton, E. Scott, Jianhui Zhu та Xinbin Chen. "The Unique NH2-terminally Deleted (ΔN) Residues, the PXXP Motif, and the PPXY Motif Are Required for the Transcriptional Activity of the ΔN Variant of p63". Journal of Biological Chemistry 281, № 5 (2005): 2533–42. http://dx.doi.org/10.1074/jbc.m507964200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Brown, Amanda, Shaghayegh Moghaddam, Thomas Kawano, and Cecilia Cheng-Mayer. "Multiple human immunodeficiency virus type 1 Nef functions contribute to efficient replication in primary human macrophages." Journal of General Virology 85, no. 6 (2004): 1463–69. http://dx.doi.org/10.1099/vir.0.79946-0.

Full text

Abstract:

The human immunodeficiency virus type 1 (HIV-1) Nef protein has been shown to accelerate viral growth kinetics in primary human T-lymphocytes and macrophages; however, the specific function(s) of Nef responsible for this phenotype in macrophages is unknown. To address this issue, mutants of a molecularly cloned macrophage-tropic isolate, HIV-1SF162, were generated expressing single point mutations that abrogate the ability of Nef to interact with cellular kinases or mediate CD4 down-regulation. Infection of primary monocyte-derived macrophages (MDM) with these mutant viruses revealed that resi

APA, Harvard, Vancouver, ISO, and other styles

20

Rajasekaran, Ganesan, and Song Yub Shin. "Fowlicidin-3 Analog with Improved Cell Selectivity Synthesized by Shifting a PXXP Motif from the N-Terminus to a Central Position." Bulletin of the Korean Chemical Society 39, no. 3 (2018): 287–93. http://dx.doi.org/10.1002/bkcs.11381.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Gubar, Olga, Pauline Croisé, Sergii Kropyvko, et al. "The atypical Rho GTPase RhoU interacts with intersectin-2 to regulate endosomal recycling pathways." Journal of Cell Science 133, no. 16 (2020): jcs234104. http://dx.doi.org/10.1242/jcs.234104.

Full text

Abstract:

ABSTRACTRho GTPases play a key role in various membrane trafficking processes. RhoU is an atypical small Rho GTPase related to Rac/Cdc42, which possesses unique N- and C-terminal domains that regulate its function and its subcellular localization. RhoU localizes at the plasma membrane, on endosomes and in cell adhesion structures where it governs cell signaling, differentiation and migration. However, despite its endomembrane localization, RhoU function in vesicular trafficking has been unexplored. Here, we identified intersectins (ITSNs) as new binding partners for RhoU and showed that the se

APA, Harvard, Vancouver, ISO, and other styles

22

Li, Bo, Lei Zhuang, and Beat Trueb. "Zyxin Interacts with the SH3 Domains of the Cytoskeletal Proteins LIM-nebulette and Lasp-1." Journal of Biological Chemistry 279, no. 19 (2004): 20401–10. http://dx.doi.org/10.1074/jbc.m310304200.

Full text

Abstract:

Zyxin is a versatile component of focal adhesions in eukaryotic cells. Here we describe a novel binding partner of zyxin, which we have named LIM-nebulette. LIM-nebulette is an alternative splice variant of the sarcomeric protein nebulette, which, in contrast to nebulette, is expressed in non-muscle cells. It displays a modular structure with an N-terminal LIM domain, three nebulin-like repeats, and a C-terminal SH3 domain and shows high similarity to another cytoskeletal protein, Lasp-1 (LIM and SH3 protein-1). Co-precipitation studies and results obtained with the two-hybrid system demonstra

APA, Harvard, Vancouver, ISO, and other styles

23

Kenney, Scott P., Jacquelyn L. Wentworth, Connie L. Heffron, and Xiang-Jin Meng. "Replacement of the hepatitis E virus ORF3 protein PxxP motif with heterologous late domain motifs affects virus release via interaction with TSG101." Virology 486 (December 2015): 198–208. http://dx.doi.org/10.1016/j.virol.2015.09.012.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Carl, Silke, A. John Iafrate, Sabine M. Lang, et al. "Simian Immunodeficiency Virus Containing Mutations in N-Terminal Tyrosine Residues and in the PxxP Motif in Nef Replicates Efficiently in Rhesus Macaques." Journal of Virology 74, no. 9 (2000): 4155–64. http://dx.doi.org/10.1128/jvi.74.9.4155-4164.2000.

Full text

Abstract:

ABSTRACT SIVmac Nef contains two N-terminal tyrosines that were proposed to be part of an SH2-ligand domain and/or a tyrosine-based endocytosis signal and a putative SH3-ligand domain (P104xxP107). In the present study, we investigated the effects of combined mutations in these tyrosine and proline residues on simian immunodeficiency virus (SIV) Nef interactions with the cellular signal transduction and endocytic machinery. We found that mutation of Y28F, Y39F, P104A, and P107A (FFAA-Nef) had little effect on Nef functions such as the association with the cellular tyrosine kinase Src, downregu

APA, Harvard, Vancouver, ISO, and other styles

25

Lewitzky, Marc, Maria Harkiolaki, Marie-Charlotte Domart, E. Yvonne Jones, and Stephan M. Feller. "Mona/Gads SH3C Binding to Hematopoietic Progenitor Kinase 1 (HPK1) Combines an Atypical SH3 Binding Motif, R/KXXK, with a Classical PXXP Motif Embedded in a Polyproline Type II (PPII) Helix." Journal of Biological Chemistry 279, no. 27 (2004): 28724–32. http://dx.doi.org/10.1074/jbc.m402745200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Foray, Nicolas, Didier Marot, Voahangy Randrianarison, et al. "Constitutive Association of BRCA1 and c-Abl and Its ATM-Dependent Disruption after Irradiation." Molecular and Cellular Biology 22, no. 12 (2002): 4020–32. http://dx.doi.org/10.1128/mcb.22.12.4020-4032.2002.

Full text

Abstract:

ABSTRACT BRCA1 plays an important role in mechanisms of response to double-strand breaks, participating in genome surveillance, DNA repair, and cell cycle checkpoint arrests. Here, we identify a constitutive BRCA1-c-Abl complex and provide evidence for a direct interaction between the PXXP motif in the C terminus of BRCA1 and the SH3 domain of c-Abl. Following exposure to ionizing radiation (IR), the BRCA1-c-Abl complex is disrupted in an ATM-dependent manner, which correlates temporally with ATM-dependent phosphorylation of BRCA1 and ATM-dependent enhancement of the tyrosine kinase activity o

APA, Harvard, Vancouver, ISO, and other styles

27

Rogers, Edward M., Andrew J. Spracklen, Colleen G. Bilancia, et al. "Abelson kinase acts as a robust, multifunctional scaffold in regulating embryonic morphogenesis." Molecular Biology of the Cell 27, no. 16 (2016): 2613–31. http://dx.doi.org/10.1091/mbc.e16-05-0292.

Full text

Abstract:

Abelson family kinases (Abls) are key regulators of cell behavior and the cytoskeleton during development and in leukemia. Abl’s SH3, SH2, and tyrosine kinase domains are joined via a linker to an F-actin–binding domain (FABD). Research on Abl’s roles in cell culture led to several hypotheses for its mechanism of action: 1) Abl phosphorylates other proteins, modulating their activity, 2) Abl directly regulates the cytoskeleton via its cytoskeletal interaction domains, and/or 3) Abl is a scaffold for a signaling complex. The importance of these roles during normal development remains untested.

APA, Harvard, Vancouver, ISO, and other styles

28

Shi, Jing, and James E. Casanova. "Invasion of Host Cells bySalmonella typhimuriumRequires Focal Adhesion Kinase and p130Cas." Molecular Biology of the Cell 17, no. 11 (2006): 4698–708. http://dx.doi.org/10.1091/mbc.e06-06-0492.

Full text

Abstract:

Salmonella typhimurium colonizes the intestinal epithelium by injecting an array of effector proteins into host cells that induces phagocytic uptake of attached bacteria. However, the host molecules targeted by these effectors remain poorly defined. Here, we demonstrate that S. typhimurium induces formation of focal adhesion-like complexes at sites of bacterial attachment and that both focal adhesion kinase (FAK) and the scaffolding protein p130Cas are required for Salmonella uptake. Entry of Salmonella into FAK−/−cells is dramatically impaired and can be restored to control levels by expressi

APA, Harvard, Vancouver, ISO, and other styles

29

Gould, Christine M., Natarajan Kannan, Susan S. Taylor, and Alexandra C. Newton. "The Chaperones Hsp90 and Cdc37 Mediate the Maturation and Stabilization of Protein Kinase C through a Conserved PXXP Motif in the C-terminal Tail." Journal of Biological Chemistry 284, no. 8 (2008): 4921–35. http://dx.doi.org/10.1074/jbc.m808436200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Weins, Astrid, Karin Schwarz, Christian Faul, Laura Barisoni, Wolfgang A. Linke, and Peter Mundel. "Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein." Journal of Cell Biology 155, no. 3 (2001): 393–404. http://dx.doi.org/10.1083/jcb.200012039.

Full text

Abstract:

We report the cloning and functional characterization of myopodin, the second member of the synaptopodin gene family. Myopodin shows no significant homology to any known protein except synaptopodin. Northern blot analysis resulted in a 3.6-kb transcript for mouse skeletal and heart muscle. Western blots showed an 80-kD signal for skeletal and a 95-kD signal for heart muscle. Myopodin contains one PPXY motif and multiple PXXP motifs. Myopodin colocalizes with α-actinin and is found at the Z-disc as shown by immunogold electron microscopy. In myoblasts, myopodin shows preferential nuclear locali

APA, Harvard, Vancouver, ISO, and other styles

31

Schaeper, Ute, Niels H. Gehring, Klaus P. Fuchs, Martin Sachs, Bettina Kempkes, and Walter Birchmeier. "Coupling of Gab1 to C-Met, Grb2, and Shp2 Mediates Biological Responses." Journal of Cell Biology 149, no. 7 (2000): 1419–32. http://dx.doi.org/10.1083/jcb.149.7.1419.

Full text

Abstract:

Gab1 is a substrate of the receptor tyrosine kinase c-Met and involved in c-Met–specific branching morphogenesis. It associates directly with c-Met via the c-Met–binding domain, which is not related to known phosphotyrosine-binding domains. In addition, Gab1 is engaged in a constitutive complex with the adaptor protein Grb2. We have now mapped the c-Met and Grb2 interaction sites using reverse yeast two-hybrid technology. The c-Met–binding site is localized to a 13–amino acid region unique to Gab1. Insertion of this site into the Gab1-related protein p97/Gab2 was sufficient to confer c-Met–bin

APA, Harvard, Vancouver, ISO, and other styles

32

Kirchhoff, Frank, Philippa J. Easterbrook, Nigel Douglas, et al. "Sequence Variations in Human Immunodeficiency Virus Type 1 Nef Are Associated with Different Stages of Disease." Journal of Virology 73, no. 7 (1999): 5497–508. http://dx.doi.org/10.1128/jvi.73.7.5497-5508.1999.

Full text

Abstract:

ABSTRACT nef alleles derived from a large number of individuals infected with human immunodeficiency virus type 1 (HIV-1) were analyzed to investigate the frequency of disrupted nef genes and to elucidate whether specific amino acid substitutions in Nef are associated with different stages of disease. We confirm that deletions or gross abnormalities in nef are rarely present. However, a comparison of Nef consensus sequences derived from 41 long-term nonprogressors and from 50 individuals with progressive HIV-1 infection revealed that specific variations are associated with different stages of

APA, Harvard, Vancouver, ISO, and other styles

33

Emerson, Suzanne U., Hanh T. Nguyen, Udana Torian, Danielle Burke, Ronald Engle, and Robert H. Purcell. "Release of Genotype 1 Hepatitis E Virus from Cultured Hepatoma and Polarized Intestinal Cells Depends on Open Reading Frame 3 Protein and Requires an Intact PXXP Motif." Journal of Virology 84, no. 18 (2010): 9059–69. http://dx.doi.org/10.1128/jvi.00593-10.

Full text

Abstract:

ABSTRACT Hepatitis E virus genotype 1 strain Sar55 replicated in subcloned Caco-2 intestinal cells and Huh7 hepatoma cells that had been transfected with in vitro transcribed viral genomes, and hepatitis E virions were released into the culture medium of both cell lines. Virus egress from cells depended on open reading frame 3 (ORF3) protein, and a proline-rich sequence in ORF3 was important for egress from cultured cells and for infection of macaques. Both intracellular ORF3 protein accumulation and virus release occurred at the apical membrane of polarized Caco-2 cells. ORF3 protein and lipi

APA, Harvard, Vancouver, ISO, and other styles

34

Kim, Mee-Ohk, Hyeon-Sook Suh, Qiusheng Si, Bruce I. Terman, and Sunhee C. Lee. "Anti-CD45RO Suppresses Human Immunodeficiency Virus Type 1 Replication in Microglia: Role of Hck Tyrosine Kinase and Implications for AIDS Dementia." Journal of Virology 80, no. 1 (2006): 62–72. http://dx.doi.org/10.1128/jvi.80.1.62-72.2006.

Full text

Abstract:

ABSTRACT Macrophages and microglia are productively infected by HIV-1 and play a pivotal role in the pathogenesis of AIDS dementia. Although macrophages and microglia express CD45, a transmembrane protein tyrosine phosphatase, whether modulation of its activity affects human immunodeficiency virus type 1 (HIV-1) replication is unknown. Here, we report that of the five human CD45 isoforms, microglia express CD45RB and CD45RO (RB > RO) and treatment of microglia with a CD45 agonist antibody αCD45RO (UCHL-1) inhibits HIV-1 replication. αCD45RO prevented HIV-1 negative factor (Nef)-induced auto

APA, Harvard, Vancouver, ISO, and other styles

35

Rauch, Susanne, Kati Pulkkinen, Kalle Saksela, and Oliver T. Fackler. "Human Immunodeficiency Virus Type 1 Nef Recruits the Guanine Exchange Factor Vav1 via an Unexpected Interface into Plasma Membrane Microdomains for Association with p21-Activated Kinase 2 Activity." Journal of Virology 82, no. 6 (2007): 2918–29. http://dx.doi.org/10.1128/jvi.02185-07.

Full text

Abstract:

ABSTRACT Alterations of T-cell receptor signaling by human immunodeficiency virus type 1 (HIV-1) Nef involve its association with a highly active subpopulation of p21-activated kinase 2 (PAK2) within a dynamic signalosome assembled in detergent-insoluble membrane microdomains. Nef-PAK2 complexes contain the GTPases Rac and Cdc42 as well as a factor providing guanine nucleotide exchange factor (GEF) activity for Rac/Cdc42. However, the identity of this GEF has remained controversial. Previous studies suggested the association of Nef with at least three independent GEFs, Vav, DOCK2/ELMO1, and βP

APA, Harvard, Vancouver, ISO, and other styles

36

Smith, Donald B., Jeff Vanek, Sandeep Ramalingam, Ingolfur Johannessen, Kate Templeton, and Peter Simmonds. "Evolution of the hepatitis E virus hypervariable region." Journal of General Virology 93, no. 11 (2012): 2408–18. http://dx.doi.org/10.1099/vir.0.045351-0.

Full text

Abstract:

The presence of a hypervariable (HVR) region within the genome of hepatitis E virus (HEV) remains unexplained. Previous studies have described the HVR as a proline-rich spacer between flanking functional domains of the ORF1 polyprotein. Others have proposed that the region has no function, that it reflects a hypermutable region of the virus genome, that it is derived from the insertion and evolution of host sequences or that it is subject to positive selection. This study attempts to differentiate between these explanations by documenting the evolutionary processes occurring within the HVR. We

APA, Harvard, Vancouver, ISO, and other styles

37

Harriff, Melanie J., Lia Danelishvili, Martin Wu, et al. "Mycobacterium avium Genes MAV_5138 and MAV_3679 Are Transcriptional Regulators That Play a Role in Invasion of Epithelial Cells, in Part by Their Regulation of CipA, a Putative Surface Protein Interacting with Host Cell Signaling Pathways." Journal of Bacteriology 191, no. 4 (2008): 1132–42. http://dx.doi.org/10.1128/jb.01359-07.

Full text

Abstract:

ABSTRACT The Mycobacterium avium complex (MAC) is an important group of opportunistic pathogens for birds, cattle, swine, and immunosuppressed humans. Although invasion of epithelial cells lining the intestine is the chief point of entry for these organisms, little is known about the mechanisms by which members of the MAC are taken up by these cells. Studies with M. avium have shown that cytoskeletal rearrangement via activation of the small G-protein Cdc42 is involved and that this activation is regulated in part by the M. avium fadD2 gene. The fadD2 gene indirectly regulates a number of gene

APA, Harvard, Vancouver, ISO, and other styles

38

Swigut, Tomek, A. John Iafrate, Jan Muench, Frank Kirchhoff, and Jacek Skowronski. "Simian and Human Immunodeficiency Virus Nef Proteins Use Different Surfaces To Downregulate Class I Major Histocompatibility Complex Antigen Expression." Journal of Virology 74, no. 12 (2000): 5691–701. http://dx.doi.org/10.1128/jvi.74.12.5691-5701.2000.

Full text

Abstract:

ABSTRACT Simian immunodeficiency virus (SIV) and human immunodeficiency virus type 1 (HIV-1) Nef proteins are related regulatory proteins that share several functions, including the ability to downregulate class I major histocompatibility complex (MHC) and CD4 expression on the cell surface and to alter T-cell-receptor-initiated signal transduction in T cells. We compared the mechanisms used by SIV mac239 Nef and HIV-1 Nef to downregulate class I MHC and found that the ability of SIV Nef to downregulate class I MHC requires a unique C-terminal region of the SIV mac239 Nef molecule which is not

APA, Harvard, Vancouver, ISO, and other styles

39

Su, Yi-Chi, Corinne Maurel-Zaffran, Jessica E. Treisman, and Edward Y. Skolnik. "The Ste20 Kinase Misshapen Regulates Both Photoreceptor Axon Targeting and Dorsal Closure, Acting Downstream of Distinct Signals." Molecular and Cellular Biology 20, no. 13 (2000): 4736–44. http://dx.doi.org/10.1128/mcb.20.13.4736-4744.2000.

Full text

Abstract:

ABSTRACT We have previously shown that the Ste20 kinase encoded bymisshapen (msn) functions upstream of the c-Jun N-terminal kinase (JNK) mitogen-activated protein kinase module inDrosophila. msn is required to activate theDrosophila JNK, Basket (Bsk), to promote dorsal closure of the embryo. A mammalian homolog of Msn, Nck interacting kinase, interacts with the SH3 domains of the SH2-SH3 adapter protein Nck. We now show that Msn likewise interacts with Dreadlocks (Dock), theDrosophila homolog of Nck. dock is required for the correct targeting of photoreceptor axons. We have performed a struct

APA, Harvard, Vancouver, ISO, and other styles

40

Kamakari, Smaragda, Anastasia Roussou, Andrew Jefferson, Ioannis Chatzidakis, Ioannis Ragoussis, and Nicholas Anagnou. "Definitive Chromosomal Orientation of the IL3-GMCSF to TCF-1 5q23 Region: Structural Analysis and Expression Profiles of a Novel Gene Encoding a Golgi-Associated Protein and of Two New Splice Isoforms Oo the Chondroitin Synthase 3 Gene Involved within the 5q Deletion in Ph(−) CML and MDS." Blood 104, no. 11 (2004): 3421. http://dx.doi.org/10.1182/blood.v104.11.3421.3421.

Full text

Abstract:

Abstract Interstitial deletion or loss of chromosome 5 [del (5q) or -5], is a frequent finding in myeloid leukemias and myelodysplasias (MDS) including a small subset of chronic myelogenous leukemia patients. Our group has focused on the 5q23–31 region encompassing the IL3-GMCSF and TCF-1 genes. To this end, we have initiated a systematic analysis of this subregion by generating a physical and transcript map employing a series of molecular and bioinformatics approaches. In our systematic search for genes involved in leukemogenesis, we have identified in the present study a novel gene and two n

APA, Harvard, Vancouver, ISO, and other styles

41

Siebert, Matthias, Mathias A. Böhme, Jan H. Driller, et al. "A high affinity RIM-binding protein/Aplip1 interaction prevents the formation of ectopic axonal active zones." eLife 4 (August 14, 2015). http://dx.doi.org/10.7554/elife.06935.

Full text

Abstract:

Synaptic vesicles (SVs) fuse at active zones (AZs) covered by a protein scaffold, at Drosophila synapses comprised of ELKS family member Bruchpilot (BRP) and RIM-binding protein (RBP). We here demonstrate axonal co-transport of BRP and RBP using intravital live imaging, with both proteins co-accumulating in axonal aggregates of several transport mutants. RBP, via its C-terminal Src-homology 3 (SH3) domains, binds Aplip1/JIP1, a transport adaptor involved in kinesin-dependent SV transport. We show in atomic detail that RBP C-terminal SH3 domains bind a proline-rich (PxxP) motif of Aplip1/JIP1 w

APA, Harvard, Vancouver, ISO, and other styles

42

Zhan, Yang, Wanting Yu, Xiong Cai, et al. "The Carboxyl Terminus of the Porcine Circovirus Type 2 Capsid Protein Is Critical to Virus-Like Particle Assembly, Cell Entry, and Propagation." Journal of Virology 94, no. 9 (2020). http://dx.doi.org/10.1128/jvi.00042-20.

Full text

Abstract:

ABSTRACT The capsid protein (Cap) is the sole structural protein and the main antigen of porcine circovirus type 2 (PCV2). Structural loops of the Cap play crucial roles in viral genome packaging, capsid assembly, and virus-host interactions. Although the molecular mechanisms are yet unknown, the carboxyl terminus (CT) of the PCV2 Cap is known to play critical roles in the evolution, pathogenesis, and proliferation of this virus. In this study, we investigated functions of CT. Removal of this loop leads to abrogation of the in vitro Cap self-assembly into virus-like particles (VLPs). Likewise,

APA, Harvard, Vancouver, ISO, and other styles

43

Tang, Wenqing, Zhiying Zhao, Chen Wang, Tao Ye та Biwei Yang. "Molecular design and optimization of hepatic cancer SLP76‐derived PLCγ1 SH3‐binding peptide with the systematic N‐substitution of peptide PXXP motif". Journal of Molecular Recognition 32, № 12 (2019). http://dx.doi.org/10.1002/jmr.2806.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Rogers, Edward M., S. Colby Allred, and Mark Peifer. "Abelson kinase’s intrinsically disordered region plays essential roles in protein function and protein stability." Cell Communication and Signaling 19, no. 1 (2021). http://dx.doi.org/10.1186/s12964-020-00703-w.

Full text

Abstract:

AbstractBackgroundThe non-receptor tyrosine kinase Abelson (Abl) is a key player in oncogenesis, with kinase inhibitors serving as paradigms of targeted therapy. Abl also is a critical regulator of normal development, playing conserved roles in regulating cell behavior, brain development and morphogenesis. Drosophila offers a superb model for studying Abl’s normal function, because, unlike mammals, there is only a single fly Abl family member. In exploring the mechanism of action of multi-domain scaffolding proteins like Abl, one route is to define the roles of their individual domains. Resear

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!