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Volumn 9, Issue 12, 2000, Pages 2528-2534
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Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies
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Author keywords
Bad protein; Bcl xL; Helix propensity; NMR spectroscopy
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Indexed keywords
PROTEIN BAD;
PROTEIN BAK;
PROTEIN BCL X;
BAD PROTEIN, HUMAN;
BCL2L1 PROTEIN, HUMAN;
CARRIER PROTEIN;
PEPTIDE;
PROTEIN BCL 2;
ARTICLE;
BINDING AFFINITY;
BIOPHYSICS;
COMPLEX FORMATION;
MUTAGENESIS;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN PROTEIN INTERACTION;
PROTEIN STRUCTURE;
SITE DIRECTED MUTAGENESIS;
STRUCTURE ANALYSIS;
AMINO ACID SEQUENCE;
APOPTOSIS;
BINDING SITE;
CHEMICAL STRUCTURE;
CHEMISTRY;
COMPARATIVE STUDY;
HUMAN;
METABOLISM;
NUCLEAR MAGNETIC RESONANCE;
PROTEIN ENGINEERING;
PROTEIN SECONDARY STRUCTURE;
PROTEIN TERTIARY STRUCTURE;
STRUCTURE ACTIVITY RELATION;
SYNTHESIS;
AMINO ACID SEQUENCE;
APOPTOSIS;
BCL-ASSOCIATED DEATH PROTEIN;
BCL-X PROTEIN;
BINDING SITES;
CARRIER PROTEINS;
HUMANS;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
PEPTIDES;
PROTEIN BINDING;
PROTEIN ENGINEERING;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
PROTO-ONCOGENE PROTEINS C-BCL-2;
STRUCTURE-ACTIVITY RELATIONSHIP;
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EID: 17744396094
PISSN: 09618368
EISSN: None
Source Type: Journal
DOI: 10.1017/S096183680000331X Document Type: Article |
Times cited : (384)
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References (29)
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