Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Hazel L. Fitton"'
Autor:
Michael Makris, Timothy R. Dafforn, Hazel L. Fitton, Robin W. Carrell, Ian R. Peake, Robert N. Pike, L. Butler, Martina E. Daly, Aiwu Zhou, N. J. Beauchamp, F.E. Preston
Publikováno v:
Blood. 92:2696-2706
The inherent variability of conformational diseases is demonstrated by two families with different mutations of the same conserved aminoacid in antithrombin. Threonine 85 underlies the opening of the main β-sheet of the molecule and its replacement,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::765604ea7ffc06c2f02fc47f6de9ecb3
https://doi.org/10.1182/blood.v92.8.2696
https://doi.org/10.1182/blood.v92.8.2696
Autor:
Robert N. Pike, Stephen P. Bottomley, Noelene Sheila Quinsey, James C. Whisstock, Timothy R. Dafforn, Robin W Carrell, Hazel L. Fitton, Paul Bernard Coughlin
Publikováno v:
Biochemistry. 42(34)
The shutter region of serpins consists of a number of highly conserved residues that are critical for both stability and function. Several variants of antithrombin with substitutions in this region are unstable and predispose the carrier to thrombosi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::379f047d9d4992572e4435dc94f752fd
https://pubmed.ncbi.nlm.nih.gov/12939144
https://pubmed.ncbi.nlm.nih.gov/12939144
The binding of heparin causes a conformational change in antithrombin to give an increased heparin binding affinity and activate the inhibition of thrombin and factor Xa. The areas of antithrombin involved in binding heparin and stabilizing the inter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1674bc207994ee9ee1398800bf7135e1
https://europepmc.org/articles/PMC2143940/
https://europepmc.org/articles/PMC2143940/
Autor:
Jan Potempa, Walker T. McGraw, Robert N. Pike, Hazel L. Fitton, James Travis, Lei Jin, Robin W. Carrell, Richard Skinner, Maurice C. Owen
Publikováno v:
The Journal of biological chemistry. 272(32)
Antithrombin, the principal plasma inhibitor of coagulation proteinases, circulates in a form with low inhibitory activity due to partial insertion of its reactive site loop into the A-beta-sheet of the molecule. Recent crystallographic structures re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a174caee9ed21d82a2c9ad643f55b66d
https://pubmed.ncbi.nlm.nih.gov/9242619
https://pubmed.ncbi.nlm.nih.gov/9242619
Autor:
L Jones, Robin W. Carrell, K. Brown, Hazel L. Fitton, Isobel D. Walker, Paul Bernard Coughlin
Publikováno v:
Blood coagulationfibrinolysis : an international journal in haemostasis and thrombosis. 8(2)
We have identified five mutations in antithrombin by direct sequencing of exons amplified using polymerase chain reaction. Four of these mutations are associated with thrombosis, three cause type I antithrombin deficiency and one has features of a ty
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42327a64420b1a955cb2a495811261cf
https://pubmed.ncbi.nlm.nih.gov/9518046
https://pubmed.ncbi.nlm.nih.gov/9518046
Publikováno v:
Biological Chemistry. 378
Incubation of antithrombin with a series of synthetic reactive loop peptides showed that 6-mer and 7-mer peptides, P14-P9 and P14-P8 of antithrombin respectively, induced loop-sheet polymerisation and binary complex formation. These peptides are like
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::09f586a93627a3c11920fe714e91188a
https://doi.org/10.1515/bchm.1997.378.9.1059
https://doi.org/10.1515/bchm.1997.378.9.1059