R W Carrell
Overview
Explore the profile of R W Carrell including associated specialties, affiliations and a list of published articles.
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Articles
210
Citations
4855
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Recent Articles
1.
Mushunje A, Evans G, Brennan S, Carrell R, Zhou A
J Thromb Haemost
. 2004 Dec;
2(12):2170-7.
PMID: 15613023
It is now apparent that the inactivated latent and cleaved conformers of antithrombin (AT) are of pathological significance. Using a single-run electrophoretic technique that allows the quantitative assessment of these...
2.
Corral J, Huntington J, Gonzalez-Conejero R, Mushunje A, Navarro M, Marco P, et al.
J Thromb Haemost
. 2004 May;
2(6):931-9.
PMID: 15140129
Background: Missense mutations causing conformational alterations in serpins can be responsible for protein deficiency associated with human diseases. However, there are few data about conformational consequences of mutations affecting antithrombin,...
3.
Morris E, Carrell R, Coughlin P
Br J Haematol
. 2002 Feb;
115(4):758-66.
PMID: 11843806
No abstract available.
4.
Huntington J, Carrell R
Sci Prog
. 2001 Aug;
84(Pt 2):125-36.
PMID: 11525014
A special family of inhibitors, known as the serpins, has evolved an extraordinary mechanism to enable the control of the proteolytic pathways essential to life. The serpins undergo a profound...
5.
Carrell R, Huntington J, Mushunje A, Zhou A
Thromb Haemost
. 2001 Aug;
86(1):14-22.
PMID: 11487000
Antithrombin readily undergoes a spontaneous transition from its active five-stranded form to a six-stranded inactive latent form. The recognition of this change in plasma has been obscured by the immediate...
6.
Silverman G, Bird P, Carrell R, Church F, Coughlin P, Gettins P, et al.
J Biol Chem
. 2001 Jul;
276(36):33293-6.
PMID: 11435447
No abstract available.
7.
Zhou A, Carrell R, Huntington J
J Biol Chem
. 2001 Apr;
276(29):27541-7.
PMID: 11325972
The recent crystallographic structure of a serpin-protease complex revealed that protease inactivation results from a disruption of the catalytic site architecture caused by the displacement of the catalytic serine. We...
8.
Zhou A, Faint R, Charlton P, Dafforn T, Carrell R, Lomas D
J Biol Chem
. 2000 Dec;
276(12):9115-22.
PMID: 11102455
The activity of the serine proteinase inhibitor (serpin) plasminogen activator inhibitor-1 (PAI-1) is controlled by the intramolecular incorporation of the reactive loop into beta-sheet A with the generation of an...
9.
Huntington J, Read R, Carrell R
Nature
. 2000 Nov;
407(6806):923-6.
PMID: 11057674
The serpins have evolved to be the predominant family of serine-protease inhibitors in man. Their unique mechanism of inhibition involves a profound change in conformation, although the nature and significance...
10.
Whisstock J, Pike R, Jin L, Skinner R, Pei X, Carrell R, et al.
J Mol Biol
. 2000 Sep;
301(5):1287-305.
PMID: 10966821
Antithrombin, uniquely among plasma serpins acting as proteinase inhibitors in the control of the blood coagulation cascade, circulates in a relatively inactive form. Its activation by heparin, and specifically by...