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Vi T. Tang

Researcher at University of Michigan

Publications -  22
Citations -  313

Vi T. Tang is an academic researcher from University of Michigan. The author has contributed to research in topics: Secretion & Medicine. The author has an hindex of 6, co-authored 14 publications receiving 149 citations. Previous affiliations of Vi T. Tang include Life Sciences Institute.

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The cargo receptor SURF4 promotes the efficient cellular secretion of PCSK9.

TL;DR: A novel approach that combines proximity-dependent biotinylation and proteomics together with genome-scale CRISPR screening to identify SURf4, a homologue of the yeast cargo receptor Erv29p, as a primary mediator of PCSK9 secretion in HEK293T cells supports a model in which SURF4 functions as an ER cargo receptor mediating the efficient cellular secretion of PC SK9.
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Genotype-Dependent and -Independent Calcium Signaling Dysregulation in Human Hypertrophic Cardiomyopathy.

TL;DR: Human HCM demonstrates calcium mishandling through both genotype-specific and common pathways, whereas sarcoplasmic endoplasmIC reticular calcium ATPase 2 abundance and sarcoplasmsic reticulum Ca uptake are depressed in both sarcomere mutation–positive and –negative HCM.
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Effects of MYBPC3 loss-of-function mutations preceding hypertrophic cardiomyopathy.

TL;DR: Cardiomyocytes have an innate capacity to attain normal MyBP-C stoichiometry despite MYBPC3 allelic loss of function due to truncating mutations, indicating protein-level compensation through a previously uncharacterized mechanism.
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HSC70 is a chaperone for wild-type and mutant cardiac myosin binding protein C

TL;DR: In an unbiased coimmunoprecipitation/mass spectrometry screen, HSP70-family chaperones were identified as interactors of both WT and mutant MYBPC3, and it is suggested that the HSC70 chaperone system plays a major role in regulating MYB PC3 protein turnover.
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The Endoplasmic Reticulum Cargo Receptor SURF4 Facilitates Efficient Erythropoietin Secretion.

TL;DR: This work demonstrates that SURF4 functions as an ER cargo receptor that mediates the efficient secretion of EPO, suggesting a new strategy for more efficient production of recombinant EPO.