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Jake Y. Chen

Researcher at University of Alabama at Birmingham

Publications -  285
Citations -  11784

Jake Y. Chen is an academic researcher from University of Alabama at Birmingham. The author has contributed to research in topics: Bone regeneration & Bone sialoprotein. The author has an hindex of 54, co-authored 273 publications receiving 10463 citations. Previous affiliations of Jake Y. Chen include Third Military Medical University & Purdue University.

Papers
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DisProt: the Database of Disordered Proteins

TL;DR: The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs) by collecting and organizing knowledge regarding the experimental characterization and the functional associations of IDPs.
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Silk implants for the healing of critical size bone defects

TL;DR: The feasibility of silk-based implants with engineered bone for the (re-)generation of bone tissues is demonstrated and the class of protein-based bone-implant materials with a mechanically stable and durable option is expanded.
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Azimuthal charged-particle correlations and possible local strong parity violation

B. I. Abelev, +375 more
TL;DR: In this article, the authors investigate a three-particle azimuthal correlator which is a P even observable, but directly sensitive to the charge separation effect, and report measurements of charged hadrons near center-of-mass rapidity with this observable in Au+Au and Cu+Cu collisions at s(NN)=200 GeV using the STAR detector.
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Transverse momentum and centrality dependence of high-pT nonphotonic electron suppression in Au+Au collisions at sNN=200GeV

B. I. Abelev, +368 more
TL;DR: In this paper, the Star collaboration at the BNL Relativistic Heavy-Ion Collider (RHIC) reports measurements of the inclusive yield of nonphotonic electrons, which arise dominantly from semileptonic decays of heavy flavor mesons, over a broad range of transverse momenta (1.2
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Disorder and sequence repeats in hub proteins and their implications for network evolution.

TL;DR: This view contradicts the prevailing view that scaling in protein interactomes arose from gene duplication and preferential attachment of equivalent proteins and proposes an alternative evolutionary network specialization process, in which certain components of the protein interactome improved their fitness for binding by becoming longer or accruing regions of disorder and/or internal repeats and have become specialized in network organization.