Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator. - Wikidata - wikimedia - TriplyDB

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.

http://www.wikidata.org/entity/Q33177672

about

Unexpected crucial role of residue 225 in serine proteases Important role of the cys-191 cys-220 disulfide bond in thrombin function and allostery Engineering Protein Allostery: 1.05 Å Resolution Structure and Enzymatic Properties of a Na+-activated Trypsin Determinants of Affinity and Proteolytic Stability in Interactions of Kunitz Family Protease Inhibitors with Mesotrypsin Why Ser and not Thr brokers catalysis in the trypsin fold Soluble expression, purification, and characterization of active recombinant human tissue plasminogen activator by auto-induction in E. coli Role of Na+ and K+ in enzyme function.Role of residue Y99 in tissue plasminogen activator.Three-dimensional models of proteases involved in patterning of the Drosophila Embryo. Crucial role of predicted cation binding sites.Protonation state of a single histidine residue contributes significantly to the kinetics of the reaction of plasminogen activator inhibitor-1 with tissue-type plasminogen activator.Thrombin functions through its RGD sequence in a non-canonical conformation.

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P2860

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.

http://www.wikidata.org/entity/Q33177672

description

1998 nî lūn-bûn

@nan

1998 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.

@ast

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.

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type

label

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.

@ast

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.

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prefLabel

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.

@ast

Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.

@en

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Role of P225 and the C136-C201 disulfide bond in tissue plasminogen activator.

@en

P2093

A Vindigni

http://www.w3.org/2001/XMLSchema#string

E Di Cera

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P2860

Evolutionary families of peptidases

The 2.3 A crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator

On the size of the active site in proteases. I. Papain

Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin)

Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin

Amino acid residues that affect interaction of tissue-type plasminogen activator with plasminogen activator inhibitor 1

Identification of residues linked to the slow-->fast transition of thrombin.

Origins of the specificity of tissue-type plasminogen activator

An allosteric switch controls the procoagulant and anticoagulant activities of thrombin

Design of fast enzymes by optimizing interaction potential in active site.

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1728-1737

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scholarly article

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10.1002/PRO.5560070807

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8

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7

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1998-08-01T00:00:00Z

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10082369

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