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Volumn 8, Issue 8, 2010, Pages 1863-1865

Effect of protein disulfide isomerase chaperone activity inhibition on tissue factor activity

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR; CHAPERONE; PROTEIN DISULFIDE ISOMERASE;

EID: 77958522684     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2010.03918.x     Document Type: Letter
Times cited : (14)

References (14)
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  • 5
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    • The integrity of the Cys186-Cys209 bond of the second disulfide loop of tissue factor is required for binding of factor VII
    • Rehemtulla A, Ruf W, Edgington TS. The integrity of the Cys186-Cys209 bond of the second disulfide loop of tissue factor is required for binding of factor VII. J Biol Chem 1991, 266:10294-9.
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  • 6
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    • Critical importance of the cell system when studying tissue factor de-encryption
    • Liang HP, Hogg PJ. Critical importance of the cell system when studying tissue factor de-encryption. Blood 2008, 112:912-13.
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  • 7
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    • Tissue factor activation: is disulfide bond switching a regulatory mechanism?
    • Pendurthi UR, Ghosh S, Mandal SK, Rao LV. Tissue factor activation: is disulfide bond switching a regulatory mechanism? Blood 2007, 110:3900-8.
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    • Pendurthi, U.R.1    Ghosh, S.2    Mandal, S.K.3    Rao, L.V.4
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    • A critical role for extracellular protein disulfide isomerase during thrombus formation in mice
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  • 10
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    • Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity
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    • Versteeg, H.H.1    Ruf, W.2
  • 11
    • 54049143232 scopus 로고    scopus 로고
    • Protein disulfide isomerase has no stimulatory chaperone effect on factor X activation by factor VIIa-soluble tissue factor
    • Persson E. Protein disulfide isomerase has no stimulatory chaperone effect on factor X activation by factor VIIa-soluble tissue factor. Thromb Res 2008, 123:171-6.
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  • 12
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  • 13
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    • The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • Klappa P, Ruddock LW, Darby NJ, Freedman RB. The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J 1998, 17:927-35.
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    • High resolution structures of p-aminobenzamidine- and benzamidine-VIIa/soluble tissue factor: unpredicted conformation of the 192-193 peptide bond and mapping of Ca2+, Mg2+, Na+, and Zn2+ sites in factor VIIa
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.