Zobrazeno 1 - 10
of 37
pro vyhledávání: '"S R Stone"'
Autor:
Rainer Metternich, S R Stone, C Tapparelli, Michael F. Scully, C Ehrhardt, M Zurini, G. Claeson
Publikováno v:
Journal of Biological Chemistry. 268:4734-4741
Peptide boronic acid derivatives have proven to be very potent inhibitors of serine proteases with boroarginine derivatives being particularly potent thrombin inhibitors. The importance of the charged side chain of arginine has been investigated by s
Publikováno v:
Journal of Biological Chemistry. 266:24198-24204
Ribonuclease inhibitor (RI) is a protein that forms a very tight complex with ribonucleases (RNases) of the pancreatic type. RI contains 30 thiol groups, some of which are important for the enzyme-inhibitor interaction. To examine which thiols are af
Autor:
W. Bode, Jan Hofsteenge, Markus G. Grütter, S. R. Stone, John P. Priestle, Joseph Rahuel, Hugo Grossenbacher
Publikováno v:
The EMBO Journal. 9:2361-2365
Thrombin is a serine protease that plays a central role in blood coagulation. It is inhibited by hirudin, a polypeptide of 65 amino acids, through the formation of a tight, noncovalent complex. Tetragonal crystals of the complex formed between human
Autor:
S R Stone, Mariarosaria Bucci, Carla Cicala, Giuseppe Cirino, Ludovico Sorrentino, J M Maraganore
Publikováno v:
Scopus-Elsevier
The Journal of Experimental Medicine
The Journal of Experimental Medicine
A rat model of inflammation was used to investigate the biological effects of thrombin. The thrombin-specific inhibitor Hirulog markedly attentuated the carrageenin-induced edema of the paw of the rat. Injection of thrombin into the paw also produced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9b214f9f72d5e1ad5a585c8e31b0c47
http://hdl.handle.net/11588/165225
http://hdl.handle.net/11588/165225
Publikováno v:
European journal of biochemistry. 268(1)
The role of thrombin anion-binding exosite-I in the recognition and cleavage of the extracellular domain of the seven transmembrane domain thrombin receptor (PAR1) was determined using site-directed mutagenesis. Basic residues in anion-binding exosit
Publikováno v:
FEBS letters. 417(3)
In order to identify physiological activators of proteinase-activated receptor-2 (PAR-2), a peptide chloromethane inhibitor (biotinyl-Ser-Lys-Gly-Arg-CH2Cl) based on the cleavage site for activation of PAR-2 was synthesised and tested with 12 trypsin
Autor:
Wolfram Bode, Milton T. Stubbs, B. F. Le Bonniec, S R Stone, A. Van De Locht, Robert Huber, Charles T. Esmon
Publikováno v:
The EMBO journal. 16(11)
Previous crystal structures of thrombin indicate that the 60-insertion loop is a rigid moiety that partially occludes the active site, suggesting that this structural feature plays a decisive role in restricting thrombin's specificity. This restricte
Publikováno v:
Advances in experimental medicine and biology. 425
Publikováno v:
Leukemia. 10(4)
The platelet-type thrombin receptor was expressed by large granular lymphocytes (LGLs) in a variety of proliferative diseases. Twenty patients with LGL proliferative disease were examined, including five T cell clones and a variety of polyclonal prol
Publikováno v:
Clinical molecular pathology. 48(5)
Venous thromboembolism is a common feature of pancreatic cancer. The underlying mechanism is unclear, but is likely to involve thrombin generation on the cell surface. Human pancreatic carcinoma cell lines (n=8) have been studied immmunohistochemical