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Algirdas Velyvis
Researcher at Cleveland Clinic
Publications - 6
Citations - 992
Algirdas Velyvis is an academic researcher from Cleveland Clinic. The author has contributed to research in topics: Focal adhesion & Signal transducing adaptor protein. The author has an hindex of 6, co-authored 6 publications receiving 954 citations. Previous affiliations of Algirdas Velyvis include Case Western Reserve University.
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Journal ArticleDOI
A Structural Mechanism of Integrin αIIbβ3 “Inside-Out” Activation as Regulated by Its Cytoplasmic Face
Olga Vinogradova,Algirdas Velyvis,Asta Velyviene,Bin Hu,Thomas A. Haas,Edward F. Plow,Jun Qin +6 more
TL;DR: These results provide a structural mechanism by which a handshake between the α and the β cytoplasmic tails restrains the integrin in a resting state and unclasping of this interaction triggers the inside-out conformational signal that leads to receptor activation.
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Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites.
TL;DR: Evidence is provided that the formation of the PINCH-ILK-CH- ILKBP complex, while necessary, is not sufficient for ILK localization to cell-extracellular matrix adhesion sites, and new insights are provided into the molecular mechanism underlying the assembly and regulation of cell-matrix adhesion structures.
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Structure of an Ultraweak Protein-Protein Complex and Its Crucial Role in Regulation of Cell Morphology and Motility
Julia Vaynberg,Julia Vaynberg,Tomohiko Fukuda,Ka Chen,Olga Vinogradova,Algirdas Velyvis,Yizeng Tu,Lily M. Ng,Chuanyue Wu,Jun Qin,Jun Qin +10 more
TL;DR: The NMR structure of an extremely weak focal adhesion complex between Nck-2 SH3 domain and PINCH-1 LIM4 domain is reported, which exhibits a remarkably small and polar interface with distinct binding modes for both SH3 and LIM domains.
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Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain.
TL;DR: The NMR structure of the PINCH LIM1 domain is solved and its binding to ILK is characterized, indicating that the LIM motif might have a highly variable mode in recognizing various target proteins.
Journal ArticleDOI
Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling.
Algirdas Velyvis,Algirdas Velyvis,Julia Vaynberg,Yanwu Yang,Olga Vinogradova,Yongjun Zhang,Chuanyue Wu,Jun Qin,Jun Qin +8 more
TL;DR: NMR spectroscopy shows that the PINCH LIM4 domain, while maintaining the conserved LIM scaffold, recognizes the third SH3 domain of another adaptor protein, Nck2 (also called Nckβ or Grb4), in a manner distinct from that of the LIM1 domain.