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Volumn 1, Issue 6, 1995, Pages 375-385

Structure and ligand‐binding modes of human serum albumin studied by UV resonance raman spectroscopy

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EID: 84984232996     PISSN: 10754261     EISSN: 15206343     Source Type: Journal    
DOI: 10.1002/bspy.350010603     Document Type: Article
Times cited : (38)

References (51)
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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
  • 34
    • 0020484713 scopus 로고
    • Phosphorescence and optically detected magnetic resonance study of the tryptophan residue in human serum albumin
    • (1982) Biochemistry , vol.21 , pp. 799-804
    • Bell, K.L.1    Brenner, H.C.2
  • 39
  • 46
    • 0014698525 scopus 로고
    • Optical studies of drug–protein complexes. IV. The interaction of warfarin and dicoumarol with human serum albumin
    • (1970) Mol. Pharmacol. , vol.6 , pp. 1-12
    • Chignell, C.F.1
  • 51
    • 0018383903 scopus 로고
    • Effects of drug bindings on esterase activity of human serum albumin. Dissociation constants of the complexes between the protein and drugs such as N‐arylanthranilic acids, coumarin derivatives and prostaglandins
    • (1979) Chem. Pharm. Bull. , vol.27 , pp. 80-87
    • Ikeda, K.1    Kurono, Y.2    Ozeki, Y.3    Yotsuyanagi, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.