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Volumn 383, Issue 1, 2002, Pages 149-158

Random peptide bacteriophage display as a probe for urokinase receptor ligands

Author keywords

Adhesion; Integrins; Invasion; Proteolysis; Vitronectin

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALANINE; LIGAND; PEPTIDE; PEPTIDE LIBRARY; POLYMER; UROKINASE; UROKINASE RECEPTOR; VITRONECTIN; CELL SURFACE RECEPTOR; INTEGRIN; OLIGOPEPTIDE; PLASMINOGEN ACTIVATOR, UROKINASE RECEPTORS;

EID: 0036005967     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2002.015     Document Type: Article
Times cited : (11)

References (51)
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  • 29
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    • Identification of specific sites involved in ligand binding by photoaffinity labeling of the receptor for the urokinase-type plasminogen activator. Residues located at equivalent positions in uPAR domains I and III participate in the assem
    • (1998) Biochemistry , vol.37 , pp. 16494-16505
    • Ploug, M.1
  • 30
    • 0028017993 scopus 로고
    • Ligand interaction between uPA and its receptor probed with 8-anilino-1-naphthalenesulfonate. Evidence for a hydrophobic binding site exposed only on the intact receptor
    • (1994) Biochemistry , vol.33 , pp. 8991-8997
    • Ploug, M.1    Ellis, V.2    Dano, K.3
  • 38
    • 0034678053 scopus 로고    scopus 로고
    • Domain 1 of the urokinase receptor (uPAR) is required for uPAR-mediated cell binding to vitronectin
    • (2000) FEBS Lett. , vol.470 , pp. 40-46
    • Sidenius, N.1    Blasi, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.