Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Geoffrey F. Lee"'
Publikováno v:
Thrombosis and Haemostasis. 87:450-458
SummaryComplexation of factor VIIa (FVIIa) and tissue factor (TF) initiates the extrinsic pathway of blood coagulation. Inappropriate triggering of this pathway has been linked to thrombotic disorders. We have previously shown that a mutant form of s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8df63d609c55221fccbfee2b460418bc
https://doi.org/10.1055/s-0037-1613025
https://doi.org/10.1055/s-0037-1613025
Publikováno v:
Biochemistry. 36:5607-5611
A strategy to design potent antagonists of human coagulation factor VIIa (FVIIa) by linking two proteins that independently inhibit activity and bind at separate, nonoverlapping sites is presented. A bifunctional inhibitor (KDTF5), comprising a Kunit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ef8d810e9e8f685b75904d5b4582a36
https://doi.org/10.1021/bi970388j
https://doi.org/10.1021/bi970388j
Publikováno v:
Protein Science. 6:315-322
Oxidative crosslinking of cysteines introduced by site-specific mutagenesis is a powerful tool for structural analysis of proteins, but the approach has been limited to studies in vitro. We recently reported that intact cells of Escherichia coli coul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5890a0e530698a04bb1b4c890cf3f785
https://doi.org/10.1002/pro.5560060206
https://doi.org/10.1002/pro.5560060206
Publikováno v:
Proceedings of the National Academy of Sciences. 92:5416-5420
We applied mutational analysis to a protein domain that functions in neither catalysis nor binding but, rather, in transmembrane signaling. The domain is part of chemoreceptor Trg from Escherichia coli. It contains four transmembrane segments, two fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae68be9f1b37ccaf5c5911470aacc3b2
https://doi.org/10.1073/pnas.92.12.5416
https://doi.org/10.1073/pnas.92.12.5416
Autor:
Gerald L. Hazelbauer, Geoffrey F. Lee
Publikováno v:
Protein Science. 4:1100-1107
The transmembrane domain of chemoreceptor Trg from Escherichia coli contains four transmembrane segments in its native homodimer, two from each subunit. We had previously used mutational analysis and sulfhydryl cross-linking between introduced cystei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0492bf157f3861d83fc61a3448b1209b
https://doi.org/10.1002/pro.5560040608
https://doi.org/10.1002/pro.5560040608
Publikováno v:
Proceedings of the National Academy of Sciences. 92:3391-3395
Transmembrane signaling by bacterial chemoreceptors is thought to involve conformational changes within a stable homodimer. We investigated the functional consequences of constraining movement between pairs of helices in the four-helix structure of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6ec0d3c01e7c0d162e442e2e2ebb50f
https://doi.org/10.1073/pnas.92.8.3391
https://doi.org/10.1073/pnas.92.8.3391
Publikováno v:
Journal of Biological Chemistry. 269:29920-29927
The transmembrane domain of chemoreceptor Trg from Escherichia coli contains four segments, two from each subunit of the homodimer. We used site-specific mutagenesis to introduce cysteines into those segments and oxidative cross-linking of cysteine p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91dd5cde23538258658b235016e69833
https://doi.org/10.1016/s0021-9258(18)43969-5
https://doi.org/10.1016/s0021-9258(18)43969-5
Autor:
D. C. Anderson, Geoffrey F. Lee
Publikováno v:
Bioconjugate Chemistry. 2:367-374
We have examined and optimized several parameters to generate efficient, high-resolution, high-information tryptic peptide maps of monoclonal antibodies and their Fab fragments, without separating the H and L chains, using reversed-phase high-pressur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd1458ebef0fda23211dc7a20fb65901
https://doi.org/10.1021/bc00011a012
https://doi.org/10.1021/bc00011a012
Publikováno v:
Thrombosis and haemostasis. 87(3)
Complexation of factor VIIa (FVIIa) and tissue factor (TF) initiates the extrinsic pathway of blood coagulation. Inappropriate triggering of this pathway has been linked to thrombotic disorders. We have previously shown that a mutant form ofsoluble t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::93452b4bfd0297c65c7b26471718f716
https://pubmed.ncbi.nlm.nih.gov/11916078
https://pubmed.ncbi.nlm.nih.gov/11916078
Autor:
Yung-Hsiang Kao, Michael W. Spellman, Geoffrey F. Lee, Robert F. Kelley, Laura Lerner, Yang Wang, Melissa A. Starovasnik
Publikováno v:
Biochemistry. 38(22)
The first epidermal growth factor-like domain (EGF-1) from blood coagulation factor VII (FVII) contains two unusual O-linked glycosylation sites at Ser-52 and Ser-60. We report here a detailed study of the effect of O-fucosylation at Ser-60 on the st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2373bb39729faa55f74ba3e4557cfb82
https://pubmed.ncbi.nlm.nih.gov/10353820
https://pubmed.ncbi.nlm.nih.gov/10353820