SCOPUS 정보 검색 플랫폼

Volumn 41, Issue 19, 2002, Pages 5968-5977

Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using 31P NMR spectroscopy

(6) Seifert, Markus H J a Breitenlechner, Christine B a Bossemeyer, Dirk b Huber, Robert a Holak, Tad A a Engh, Richard A c

a MAX PLANCK INSTITUTE OF BIOCHEMISTRY (Germany)

b GERMAN CANCER RESEARCH CENTER DKFZ (Germany)

c ROCHE DIAGNOSTICS GMBH (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHORYLATION;

BACTERIA; CATALYSIS; COMPLEXATION; CRYSTAL STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

ENZYMES;

ALKALINE PHOSPHATASE; CYCLIC AMP DEPENDENT PROTEIN KINASE; PHOSPHOSERINE; PHOSPHOTHREONINE; PROTEIN KINASE; SERINE; THREONINE;

ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; DEPHOSPHORYLATION; DIFFUSION; ENZYME ACTIVATION; ENZYME PHOSPHORYLATION; MOLECULAR DYNAMICS; MOUSE; NONHUMAN; PHOSPHORUS NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION;

ALKALINE PHOSPHATASE; ANIMALS; BINDING SITES; CYCLIC AMP-DEPENDENT PROTEIN KINASES; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHORUS; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SERINE; THREONINE;

EID: 0037076520 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi025509g Document Type: Article

Times cited : (27)

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