STAM Proteins Bind Ubiquitinated Proteins on the Early Endosome via the VHS Domain and Ubiquitin-interacting Motif [PDF]
Molecular Biology of the Cell, 2003 Conjugation with ubiquitin acts as a sorting signal for proteins in the endocytic and biosynthetic pathways at the endosome. Signal-transducing adaptor molecule (STAM) proteins, STAM1 and STAM2, are associated with hepatocyte growth factor-regulated substrate (Hrs) but their function remains unknown.
Mizuno, E. +4 more
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Inhibition of HIV budding by a genetically selected cyclic peptide targeting the Gag?TSG101 interaction [PDF]
, 2008 The egress of HIV particles from virus-infected cells is accomplished by the recruitment of proteins that normally mediate host cell endocytic functions.
Gam, Jongsik +5 more
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Biomolecules, 2022 The S100A1 protein in humans is a calcium-binding protein. Upon Ca2+ binding to S100A1 EF-hand motifs, the conformation of S100A1 changes and promotes interactions with target proteins.
Nuzhat Parveen +5 more
doaj +1 more source
The role of TNRC6 proteins in gene silencing [PDF]
, 2013 Proteins of the GW182 family have recently emerged as key players in miRNAmediated gene silencing. They have been shown to interact with Argonaute proteins, components of the RISC and are assumed to mediate the repression in metazoa. Three paralogues are
Zipprich, Jakob Theophil
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The MoVIN server for the analysis of protein interaction networks
BMC Bioinformatics, 2008 Background Protein-protein interactions are at the basis of most cellular processes and crucial for many bio-technological applications. During the last few years the development of high-throughput technologies has produced several large-scale protein ...
Bussotti Giovanni +2 more
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WD40-Repeat Proteins in Ciliopathies and Congenital Disorders of Endocrine System [PDF]
Endocrinology and Metabolism, 2020 WD40-repeat (WDR)-containing proteins constitute an evolutionarily conserved large protein family with a broad range of biological functions. In human proteome, WDR makes up one of the most abundant protein-protein interaction domains. Members of the WDR
Yeonjoo Kim, Soo-Hyun Kim
doaj +1 more source
PLoS Computational Biology, 2006 Protein-protein interactions, particularly weak and transient ones, are often mediated by peptide recognition domains, such as Src Homology 2 and 3 (SH2 and SH3) domains, which bind to specific sequence and structural motifs. It is important but challenging to determine the binding specificity of these domains accurately and to predict their ...
Tingjun Hou +4 more
openaire +5 more sources
Structural Mechanism for the Specific Assembly and Activation of the Extracellular Signal Regulated Kinase 5 (ERK5) Module [PDF]
, 2013 Mitogen-activated protein kinase (MAPK) activation depends on a linear binding motif found in all MAPK kinases (MKK). In addition, the PB1 (Phox and Bem1) domain of MKK5 is required for extracellular signal regulated kinase 5 (ERK5) activation.
Remenyi, A +11 more
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Genes2Networks: Connecting Lists of Proteins by Using Background Literature-based Mammalian Networks [PDF]
, 2007 In recent years, in-silico literature-based mammalian protein-protein interaction network datasets have been developed. These datasets contain binary interactions extracted manually from legacy experimental biomedical research literature.
Avi Ma'ayan
core +4 more sources
Cholesterol Interaction with the MAGUK Protein Family Member, MPP1, via CRAC and CRAC-Like Motifs: An In Silico Docking Analysis. [PDF]
PLoS ONE, 2015 Cholesterol is essential for the proper organization of the biological membrane. Therefore, predicting which proteins can bind cholesterol is important in understanding how proteins participate in lateral membrane organization.
Marcin A Listowski +3 more
doaj +1 more source