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Li Zhang

Researcher at University of Maryland, Baltimore

Publications -  61
Citations -  6654

Li Zhang is an academic researcher from University of Maryland, Baltimore. The author has contributed to research in topics: Integrin alpha M & Integrin. The author has an hindex of 34, co-authored 59 publications receiving 6169 citations. Previous affiliations of Li Zhang include Cleveland Clinic & American Red Cross.

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Journal ArticleDOI

Ligand binding to integrins.

TL;DR: The number of integrins and the remarkable breadth of their cellular distribution support the statement that the phenotype of virtually every cell is uniquely influenced by its display ofintegrins.
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Identification of tendon stem/progenitor cells and the role of the extracellular matrix in their niche

TL;DR: It is shown that human and mouse tendons harbor a unique cell population, termed tendon stem/progenitor cells (TSPCs), that has universal stem cell characteristics such as clonogenicity, multipotency and self-renewal capacity and could regenerate tendon-like tissues after extended expansion in vitro and transplantation in vivo.
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Platelet Glycoprotein Ibα Is a Counterreceptor for the Leukocyte Integrin Mac-1 (Cd11b/Cd18)

TL;DR: The platelet counterreceptor is identified as glycoprotein (GP) Ibα, a component of the GP Ib-IX-V complex, the platelet von Willebrand factor (vWf) receptor, which provides a molecular target for disrupting leukocyte–platelet complexes that promote vascular inflammation in thrombosis, atherosclerosis, and angioplasty-related restenosis.
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A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans

TL;DR: A genetic disease in two human siblings that presented with severe bleeding, frequent infections and osteopetrosis at an early age is identified and an essential role of KINDLIN-3 in integrin activation in humans is established.
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Identification of a Urokinase Receptor-Integrin Interaction Site PROMISCUOUS REGULATOR OF INTEGRIN FUNCTION

TL;DR: Observations indicate that uPAR associates with integrins directly and that disruption of this association broadly impairs integrin function, suggesting a novel strategy for regulation ofIntegrins in the settings of inflammation and tumor progression.