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Protein–protein interaction

About: Protein–protein interaction is a research topic. Over the lifetime, 5010 publications have been published within this topic receiving 209297 citations. The topic is also known as: protein–protein interaction & protein interaction.


Papers
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Journal ArticleDOI
TL;DR: Stable isotopic amino acids in cell culture is employed to differentially label proteins in EGF-stimulated versus unstimulated cells and SILAC combined with modification-based affinity purification is a useful approach to detect specific and functional protein-protein interactions.
Abstract: Mass spectrometry-based proteomics can reveal protein-protein interactions on a large scale, but it has been difficult to separate background binding from functionally important interactions and still preserve weak binders. To investigate the epidermal growth factor receptor (EGFR) pathway, we employ stable isotopic amino acids in cell culture (SILAC) to differentially label proteins in EGF-stimulated versus unstimulated cells. Combined cell lysates were affinity-purified over the SH2 domain of the adapter protein Grb2 (GST-SH2 fusion protein) that specifically binds phosphorylated EGFR and Src homologous and collagen (Shc) protein. We identified 228 proteins, of which 28 were selectively enriched upon stimulation. EGFR and Shc, which interact directly with the bait, had large differential ratios. Many signaling molecules specifically formed complexes with the activated EGFR-Shc, as did plectin, epiplakin, cytokeratin networks, histone H3, the glycosylphosphatidylinositol (GPI)-anchored molecule CD59, and two novel proteins. SILAC combined with modification-based affinity purification is a useful approach to detect specific and functional protein-protein interactions.

730 citations

Journal ArticleDOI
TL;DR: A novel gene for an O-GlcNAc transferase (OGT) that shares no sequence homology or structural similarities with other glycosyltransferases is cloned and characterized and suggests that OGT may be regulated by protein interactions that are independent of the enzyme's catalytic site.

729 citations

Journal ArticleDOI
TL;DR: Systems should be used with the aim of defining the correspondence between the in vitro regulatory role(s) attributed to individual members of this protein family and the in vivo function of each S100 protein.

700 citations

Journal ArticleDOI
01 Oct 2002
TL;DR: Property such as sequence conservation and co-regulation of genes and proteins involved in different types of physical interactions are discussed, given that all proteins consist of their evolutionary units, the domains, all interactions occur between these domains.
Abstract: In the postgenomic era, one of the most interesting and important challenges is to understand protein interactions on a large scale. The physical interactions between protein domains are fundamental to the workings of a cell: in multi-domain polypeptide chains, in multi-subunit proteins and in transient complexes between proteins that also exist independently. Thus experimental investigation of protein-protein interactions has been extensive, including recent large-scale screens using mass spectrometry. The role of computational research on protein-protein interactions encompasses not only prediction, but also understanding the nature of the interactions and their three-dimensional structures. I will discuss properties such as sequence conservation and co-regulation of genes and proteins involved in different types of physical interactions. Given that all proteins consist of their evolutionary units, the domains, all interactions occur between these domains. The interactions between domains belonging to different protein families will be the second topic of my talk.

697 citations

Journal ArticleDOI
01 Sep 2007-Proteins
TL;DR: The scope of this review is to summarize all the available information regarding hot spots for a better atomic understanding of their structure and function, to improve the rational design of complexes of high affinity and specificity as well as that of small molecules, which can mimic the functional epitopes of the proteic complexes.
Abstract: Proteins tendency to bind to one another in a highly specific manner forming stable complexes is fundamental to all biological processes A better understanding of complex formation has many practical applications, which include the rational design of new therapeutic agents, and the analysis of metabolic and signal transduction networks Alanine-scanning mutagenesis made possible the detection of the functional epitopes, and demonstrated that most of the protein-protein binding energy is related only to a group of few amino acids at intermolecular protein interfaces: the hot spots The scope of this review is to summarize all the available information regarding hot spots for a better atomic understanding of their structure and function The ultimate objective is to improve the rational design of complexes of high affinity and specificity as well as that of small molecules, which can mimic the functional epitopes of the proteic complexes

689 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023132
2022262
2021248
2020231
2019233
2018232