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Volumn 284, Issue 41, 2009, Pages 28292-28305

Structural studies of soybean calmodulin isoform 4 bound to the calmodulin-binding domain of tobacco mitogen-activated protein kinase phosphatase-1 provide insights into a sequential target binding mode

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTER PROTEINS; AMINO ACID SEQUENCE; CALMODULIN BINDING DOMAIN; DATA SUPPORT; FUSION PROTEINS; HELICAL PEPTIDE; HIGH RESOLUTION; ISOFORMS; ISOTOPE LABELING; MITOGEN ACTIVATED PROTEIN KINASE; MULTI-PROTEIN COMPLEX; NICOTIANA TABACUM; PLANT STRESS; REGULATORY PROTEIN; SIDE CHAINS; SOLUTION STRUCTURES; STRONG BINDING; STRUCTURAL STUDIES; STRUCTURE DETERMINATION; TARGET BINDING; TARGET PROTEINS;

EID: 70350488894     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.025080     Document Type: Article
Times cited : (16)

References (59)
  • 13
  • 22
    • 0038714319 scopus 로고    scopus 로고
    • MAPK Group
    • MAPK Group (2002) Trends Plant Sci. 7, 301-308
    • (2002) Trends Plant Sci , vol.7 , pp. 301-308
  • 57
    • 70350514022 scopus 로고    scopus 로고
    • Yamniuk, A. P., Rainaldi, M., and Vogel, H. J. (2007) Plant Signal. Behav. 2, e1-4
    • Yamniuk, A. P., Rainaldi, M., and Vogel, H. J. (2007) Plant Signal. Behav. 2, e1-4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.