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Volumn 357, Issue 1, 2001, Pages 269-274

Conformational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants

Author keywords

Conformational changes; High affinity binding; Protein stability; Site directed mutagenesis; Thermal denaturation

Indexed keywords

BINDING ENERGY; CONFORMATIONS; FLUORESCENCE; MUTAGENESIS; PH EFFECTS; PHYSIOLOGY; PROTEINS; THERMAL EFFECTS; YEAST;

EID: 0035397254     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3570269     Document Type: Article
Times cited : (59)

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    • Chen, R.F.1
  • 18
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    • Comparison of graphical procedures for estimating the intrinsic molar fluorescence of protein-bound drugs for drug-binding studies. A reevaluation of existing plots and introduction of two inverse hyperbolic plots
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    • Rajkowski, K.M.1
  • 25
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    • Evidence for a large and flexible region of human serum albumin possessing high affinity binding sites for salicylate, warfarin, and other ligands
    • (1988) Mol. Pharmacol. , vol.34 , pp. 160-171
    • Kragh-Hansen, U.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.