(Q27638215)

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The methyl group of N(alpha)(Me)Arg-containing peptides disturbs the active-site geometry of thrombin, impairing efficient cleavage

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The methyl group of N(alpha)(Me)Arg-containing peptides disturbs the active-site geometry of thrombin, impairing efficient cleavage (English)

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3

Robert Huber

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Wolfram Bode

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5

object named as

Wolfram Bode

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Jörg Stürzebecher

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4

object named as

Jörg Stürzebecher

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author name string

Rainer Friedrich

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1

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Torsten Steinmetzer

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2

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language of work or name

English

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publication date

1 March 2002

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published in

Journal of Molecular Biology

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volume

316

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issue

4

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page(s)

869-74

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Structure of the hirulog 3-thrombin complex and nature of the S' subsites of substrates and inhibitors

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Synthesis of a homologous series of ketomethylene arginyl pseudodipeptides and application to low molecular weight hirudin-like thrombin inhibitors

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Differentiation between proteolytic activation and autocatalytic conversion of human prothrombin. Activation of recombinant human prothrombin and recombinant D419N-prothrombin by snake venoms from Echis carinatus and Oxyuranus scutellatus

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A player of many parts: the spotlight falls on thrombin's structure.

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Potent bivalent thrombin inhibitors: replacement of the scissile peptide bond at P(1)-P(1)' with arginyl ketomethylene isosteres

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The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin

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Refined 2.3 A X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA. A starting point for improving antithrombotics

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10.1006/JMBI.2001.5394

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PubMed publication ID

11884127

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(Q27638215)

The methyl group of N(alpha)(Me)Arg-containing peptides disturbs the active-site geometry of thrombin, impairing efficient cleavage

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