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ProteomicsLight-mediated discovery of surfaceome nanoscale organization and intercellular receptor interaction networks
Delineating the extracellular interaction network of the cell surface proteotype (the surfaceome) is fundamental to understanding cellular signaling function in health and disease. Here, we developed LUX-MS, an optoproteomic technology that enables the spatiotemporal and proteome-wide study of surfa...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) Listeria monocytogenes serotype 4b Listeria phage A500 Escherichia coli 
2021-06-14 | PXD020481 | Pride
Lc-ms/ms 
UnknownSystematic discovery of linear binding motifs targeting an ancient protein interaction surface on MAP kinases.
Not available
S-EPMC4670726 | biostudies-literature
UnknownQuantitative measurements of protein-surface interaction thermodynamics.
Not available
S-EPMC6099891 | biostudies-literature
ProteomicsIdentification of the effect of a CRISPR interference knockdown of Borrelia burgdorferi strain B31 BB0838, a outer membrane lipoprotein flippase candidate, on surface lipoprotein secretion using Multidimensional Protein Identification Technology.
To identify the effect of a CRISPR interference knockdown of Borrelia burgdorferi strain B31 BB0838, a outer membrane lipoprotein flippase candidate, on surface lipoprotein secretion using Multidimensional Protein Identification Technology.
ORGANISM(S): Borrelia Burgdorferi B31 (ncbitaxon:224326) 
2022-07-27 | MSV000089990 | MassIVE
UnknownTargeting a key protein-protein interaction surface on mitogen-activated protein kinases by a precision-guided warhead scaffold.
Not available
S-EPMC11452651 | biostudies-literature
ProteomicsUltrafast and Chemoselective Biotinylation of Living Cell Surface for Time-Resolved Surfaceome Analysis - final
Cell surface proteins participate in many important biological processes such as cell-to-cell interaction, signal transduction, cell adhesion, and protein transportation. In-depth study of the cell surface protein group is of great significance. Nevertheless, detection and analysis of the surfaceome...
ORGANISM(S): Homo Sapiens 
PXD053733 |
UnknownQuantitative comparison of protein-protein interaction interface using physicochemical feature-based descriptors of surface patches.
Not available
S-EPMC9939524 | biostudies-literature
ProteomicsP. micra surface protein TmpC interacts directly with OSCC cell lines via CKAP4
P. micra surface protein TmpC interacts directly with OSCC cell lines via CKAP4, a receptor frequently overexpressed in human OSCC tumors. The interaction of TmpC and CKAP4 mediates bacterial attachment, invasion, and metastasis-promoting effects of P. micra on OSCC and subsequently activates HIF-1α...
ORGANISM(S): Homo Sapiens 
PXD054166 |
ProteomicsLibrary-Based, Multiplexed Strategy for Mapping Protein Interaction Networks via Crosslinking
Protein-protein interactions are fundamental to cellular function, yet resolving their interaction interfaces and dynamic behaviors in native biological contexts remains challenging, particularly for weak or transient interactions. Crosslinking strategies based on noncanonical amino acids offer an e...
ORGANISM(S): Homo Sapiens 
2026-02-28 | PXD075032 |
UnknownPrediction of Protein-Ligand Binding Affinities Using Atomic Surface Site Interaction Points.
Not available
S-EPMC12848979 | biostudies-literature
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