Zobrazeno 1 - 10
of 12
pro vyhledávání: '"E A, Komives"'
Publikováno v:
Journal of molecular biology. 307(4)
The crystal structure of the unphosphorylated state of methylesterase CheB shows that the regulatory domain blocks access of substrate to the active site of the catalytic domain. Phosphorylation of CheB at Asp56 results in a catalytically active tran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1eae1ec6e7922b450514717a4f2583f6
https://pubmed.ncbi.nlm.nih.gov/11286548
https://pubmed.ncbi.nlm.nih.gov/11286548
Publikováno v:
Journal of molecular biology. 306(3)
The kinetics of solvent accessibility at the protein-protein interface between thrombin and a fragment of thrombomodulin, TMEGF45, have been monitored by amide hydrogen/deuterium (H/2H) exchange detected by MALDI-TOF mass spectrometry. The interactio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::37a5ac03e674c729cfe2c405f0a24297
https://pubmed.ncbi.nlm.nih.gov/11178915
https://pubmed.ncbi.nlm.nih.gov/11178915
Autor:
B A, Sampoli Benitez, E A, Komives
Publikováno v:
Proteins. 40(1)
Epidermal growth factor (EGF) has a (1-3,2-4,5-6) disulfide-bonding pattern. This pattern is found in nearly all EGF-like domains, despite wide variation in sequences. Biological data from EGF and at least one EGF-like domain show that disulfide bond
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fb583af9bd454f9d56812250dc4f980b
https://pubmed.ncbi.nlm.nih.gov/10813841
https://pubmed.ncbi.nlm.nih.gov/10813841
Publikováno v:
Nature structural biology. 7(3)
A glycosylated fragment of thrombomodulin containing two epidermal growth factor-like domains (TMEGF45) was analyzed by NMR. The 4th-domains structure of this two-domain fragment is similar to that of the individual domain previously determined. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5757e4bb865fff5cb51f0549fadc9bbd
https://pubmed.ncbi.nlm.nih.gov/10700277
https://pubmed.ncbi.nlm.nih.gov/10700277
Publikováno v:
Journal of molecular biology. 296(2)
The rate constants for the binding interaction between thrombin and a fully active fragment of its anticoagulant cofactor, thrombomodulin, have been determined by surface plasmon resonance. At physiological ionic strength, the k(a) was 6.7x10(6) M(-1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d1f452db7d821810f06de9bb17116615
https://pubmed.ncbi.nlm.nih.gov/10669614
https://pubmed.ncbi.nlm.nih.gov/10669614
Autor:
M J, Wood, E A, Komives
Publikováno v:
Journal of biomolecular NMR. 13(2)
Heterologous expression in Pichia pastoris has many of the advantages of eukaryotic expression, proper folding and disulfide bond formation, glycosylation, and secretion. Contrary to other eukaryotic systems, protein production from P. pastoris occur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fb5f79231821626eff9fbb4030a7a2be
https://pubmed.ncbi.nlm.nih.gov/10070756
https://pubmed.ncbi.nlm.nih.gov/10070756
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 103
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6debb454cf76c366836396685ba307d7
https://pubmed.ncbi.nlm.nih.gov/9680635
https://pubmed.ncbi.nlm.nih.gov/9680635
Publikováno v:
Journal of molecular biology. 273(4)
The structure of the fifth EGF-like domain (residues Q387 to E426) of thrombomodulin (TMEGF5) has been determined by two-dimensional NMR. TMEGF5 binds to thrombin with a Ki of 1.9 microM and has been shown to have a novel disulfide bonding pattern in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::85b0184a16af5795fe939ae4f543d337
https://pubmed.ncbi.nlm.nih.gov/9367781
https://pubmed.ncbi.nlm.nih.gov/9367781
Publikováno v:
Cancer research. 47(8)
Diploid human lymphoblast cells exhibit apparent saturation of mutation induced by exposure to aflatoxin B1, despite a linear increase in the amount and proportion of the aflatoxin-DNA adducts formed. The saturation is neither a cell cycle phenomenon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::596d73549c1ac540f2a826a55d5d9765
https://pubmed.ncbi.nlm.nih.gov/3103909
https://pubmed.ncbi.nlm.nih.gov/3103909
Autor:
P R, Ortiz de Montellano, E A, Komives
Publikováno v:
The Journal of biological chemistry. 260(6)
Phenylacetylene and biphenylacetylene are oxidized by cytochrome P-450 to the corresponding arylacetic acids. The acetylenic hydrogen shifts to the adjacent carbon and one atom of molecular oxygen is incorporated into the carboxylic acid group in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b98c0f1105a27bfb1b3ee94cd53c3e10
https://pubmed.ncbi.nlm.nih.gov/3972828
https://pubmed.ncbi.nlm.nih.gov/3972828