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Volumn 8, Issue 3, 2001, Pages 633-644

The structure of calnexin, an ER chaperone involved in quality control of protein folding

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CHAPERONE; GLYCOPROTEIN; LECTIN; LIGAND; PROLINE;

EID: 0034799402     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(01)00318-5     Document Type: Article
Times cited : (337)

References (54)
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 13
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 16
  • 20
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 31
    • 0034657712 scopus 로고    scopus 로고
    • Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation
    • (2000) Biochem. J. , vol.348 , pp. 1-13
    • Parodi, A.J.1
  • 40
    • 0031588904 scopus 로고    scopus 로고
    • Analyses of carbohydrate recognition by legume lectins: Size of the combining site loops and their primary specificity
    • (1997) J. Mol. Biol. , vol.267 , pp. 433-445
    • Sharma, V.1    Surolia, A.2
  • 41
    • 0014842614 scopus 로고
    • Iodination of a single tyrosine in crystals of alpha-chymotrypsin
    • (1970) Biochemistry , vol.9 , pp. 3609-2617
    • Sigler, P.B.1
  • 52
    • 0027078720 scopus 로고
    • Analysis of sequence variation among legume lectins. A ring of hypervariable residues forms the perimeter of the carbohydrate-binding site
    • (1992) J. Mol. Biol. , vol.228 , pp. 924-934
    • Young, N.M.1    Oomen, R.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.