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Barbara M. Vertel

Researcher at Rosalind Franklin University of Medicine and Science

Publications -  32
Citations -  1675

Barbara M. Vertel is an academic researcher from Rosalind Franklin University of Medicine and Science. The author has contributed to research in topics: Aggrecan & Chondroitin sulfate proteoglycan. The author has an hindex of 23, co-authored 32 publications receiving 1604 citations. Previous affiliations of Barbara M. Vertel include University of Illinois at Chicago.

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Sedlin Controls the ER Export of Procollagen by Regulating the Sar1 Cycle

TL;DR: It is reported that TANGO1 recruits Sedlin—also known as TRAPPC2, a homolog of the yeast TRAPP subunit Trs20—and helps to allow COPII-coated carriers to grow large enough to incorporate procollagen, and sustained the ER export of PC.
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cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia.

TL;DR: Analysis of a polymerase chain reaction-amplified fragment encoding the chick-specific repeat region revealed a single base mutation that converted the codon GAA for glutamate at amino acid 1513 to TAA, a stop codon, in nanomelic chondrocytes.
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Characterization of cartilage oligomeric matrix protein (COMP) in human normal and pseudoachondroplasia musculoskeletal tissues.

TL;DR: The results of human tissue distribution and cell secretion studies of human COMP lend further support to the hypothesis that retention of COMP is related to the terminal PSACH chondrocyte phenotype, processing of proteins related to extracellular matrix formation, and maintenance in cartilage.
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Xylosylation is an endoplasmic reticulum to Golgi event.

TL;DR: The subcellular site of xylosylation, the first carbohydrate modification of the core protein that initiates glycosaminoglycan chain synthesis, was characterized in situ using electron microscopic (EM) autoradiography and the radiolabeling of semi-intact chondrocytes to support the view that xylose addition begins in a late ER compartment and continues in intermediate compartments, perhaps including the cis-Golgi.