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Volumn 10, Issue 3, 2001, Pages 581-591

A general method for the quantitative analysis of functional chimeras: Applications from site-directed mutagenesis and macromolecular association

Author keywords

Aminotransferase; Chimera; Context dependence; Macromolecular interactions; Oncomodulin; Protein genetic engineering; Tat TAR

Indexed keywords

ASPARTIC ACID; DICARBOXYLIC ACID; ONCOMODULIN; TYROSINE AMINOTRANSFERASE;

EID: 0035106702     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.24101     Document Type: Article
Times cited : (12)

References (11)
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  • 4
    • 0025125731 scopus 로고
    • Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: Characterization of a monomeric intermediate
    • (1990) Biochemistry , vol.29 , pp. 1907-1913
    • Herold, M.1    Kirschner, K.2
  • 7
    • 0031281419 scopus 로고    scopus 로고
    • A continuous coupled spectrophotometric assay for tyrosine aminotransferase activity with aromatic and other nonpolar amino acids
    • (1997) Anal. Biochem. , vol.253 , pp. 46-49
    • Luong, T.N.1    Kirsch, J.F.2
  • 8
    • 0029079958 scopus 로고
    • Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis
    • (1995) Protein Sci. , vol.4 , pp. 1750-1757
    • Onuffer, J.J.1    Kirsch, J.F.2
  • 9
    • 0032958585 scopus 로고    scopus 로고
    • Energetic analysis of an antigen/ antibody interface: Alanine scanning mutagenesis and double mutant cycles in the HyHEL-10/lysozyme interaction
    • (1999) Protein Sci. , vol.8 , pp. 958-968
    • Pons, J.1    Rajpal, A.2    Kirsch, J.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.