G
Gerald J. Roth
Researcher at United States Department of Veterans Affairs
Publications - 15
Citations - 1598
Gerald J. Roth is an academic researcher from United States Department of Veterans Affairs. The author has contributed to research in topics: Peptide sequence & Glycoprotein. The author has an hindex of 13, co-authored 15 publications receiving 1579 citations.
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Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein.
José A. López,Dominic W. Chung,Kazuo Fujikawa,Frederick S. Hagen,Thalia Papayannopoulou,Gerald J. Roth +5 more
TL;DR: The amino acid sequence of the alpha chain of GPIb predicted from the cDNA agreed completely with the sequence of 156 amino acids that was determined by Edman degradation of peptides isolated from human platelet glycocalicin after digestion with trypsin or Staphylococcus aureus V8 protease.
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The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence.
José A. López,Dominic W. Chung,Kazuo Fujikawa,Frederick S. Hagen,Earl W. Davie,Gerald J. Roth +5 more
TL;DR: The primary structure of the beta chain of human glycoprotein Ib (GPIb), the platelet receptor for von Willebrand factor, has been established by a combination of cDNA cloning and amino acid sequence analysis.
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Human platelet glycoprotein IX: an adhesive prototype of leucine-rich glycoproteins with flank-center-flank structures
TL;DR: GPIX contains a leucine-rich glycoprotein (LRG) sequence of 24 amino acids similar to conserved LRG sequences in GPIb and other proteins from humans, Drosophila, and yeast.
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Sustained ex vivo expansion of hematopoietic stem cells mediated by thrombopoietin.
TL;DR: The results demonstrate that TPO can mediate the self-replication of HSC in LTBMC, and provide proof that HSC can self-Replication ex vivo.
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Localization of binding sites within human von Willebrand factor for monomeric type III collagen
TL;DR: A murine anti-human vWF monoclonal antibody (MR5), which blocks the binding of vWf to collagen, bound selectively to both M11 and M20 when tested in an enzyme-linked immunoadsorbent assay.