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Volumn 127, Issue 34, 2005, Pages 11966-11968

Chimeric (α/β + α)-peptide ligands for the BH3-recognition cleft of Bcl-xL: Critical role of the molecular scaffold in protein surface recognition

Author keywords

[No Author keywords available]

Indexed keywords

BH3 PROTEIN; CHIMERIC PROTEIN; LIGAND; PROTEIN BCL XL;

EID: 24144488383     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja053678t     Document Type: Article
Times cited : (148)

References (38)
  • 8
    • 20444486559 scopus 로고    scopus 로고
    • (c) Oltersdorf, T., et al. Nature 2005, 435, 677-681.
    • (2005) Nature , vol.435 , pp. 677-681
    • Oltersdorf, T.1
  • 26
    • 33645583676 scopus 로고    scopus 로고
    • note
    • L. See Supporting Information for details.
  • 31
    • 33645607782 scopus 로고    scopus 로고
    • note
    • Rapid proteolysis of the α-peptide segment of 2 is observed upon treatment with Pronase, while the α/β segment remains intact for at least 24 h.
  • 32
    • 33645604402 scopus 로고    scopus 로고
    • note
    • 50 of 120 μM in the FP assay, suggesting that the α/β portions of 2 and 4 target the BH3 binding site and contribute substantially to binding.
  • 36
    • 0030816685 scopus 로고    scopus 로고
    • Among α- and β-peptides, alcohol solvents are known to promote secondary structure relative to water; the folding observed in such organic solvents generally reflects the conformational propensities in water, (a) Luo, P.; Baldwin, R. L. Biochemistry 1997, 36, 8413-8421.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.