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Article title matches
- Category:Autoinhibitory fragment (54 bytes)
1: List of pages with the keyword Autoinhibitory fragment - Category:Autoinhibitory helix (51 bytes)
1: List of pages with the keyword Autoinhibitory helix - Category:Autoinhibitory (45 bytes)
1: List of pages with the keyword Autoinhibitory - Category:Autoinhibitory region (52 bytes)
1: List of pages with the keyword Autoinhibitory region - Category:Autoinhibitory form (50 bytes)
1: List of pages with the keyword Autoinhibitory form - Category:Autoinhibitory domain (52 bytes)
1: List of pages with the keyword Autoinhibitory domain - Category:Autoinhibitory ialpha3 helix (59 bytes)
1: List of pages with the keyword Autoinhibitory ialpha3 helix - Category:Autoinhibitory regulation (56 bytes)
1: List of pages with the keyword Autoinhibitory regulation
Page text matches
- 2src (9,009 bytes)
28: ...rystal structures of c-Src reveal features of its autoinhibitory mechanism.,Xu W, Doshi A, Lei M, Eck MJ, Harrison... - 1cfp (5,102 bytes)
10: ...nd initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. In... - 2j6m (6,222 bytes)
26: ...t the mutations activate the kinase by disrupting autoinhibitory interactions, and that they accelerate catalysis ... - 1uwo (5,055 bytes)
10: ...nd initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. In... - 7e8d (3,534 bytes)
14: ...T1150A destabilize the interactions that keep the autoinhibitory loop closed, thereby enhancing catalytic turnover... - 4q5u (4,489 bytes)
16: ...ulting in a conformational change that removes an autoinhibitory domain from the active site of the phosphatase. W... - 2itu (6,171 bytes)
26: ...t the mutations activate the kinase by disrupting autoinhibitory interactions, and that they accelerate catalysis ... - 2itq (6,172 bytes)
26: ...t the mutations activate the kinase by disrupting autoinhibitory interactions, and that they accelerate catalysis ... - 2itt (6,238 bytes)
26: ...t the mutations activate the kinase by disrupting autoinhibitory interactions, and that they accelerate catalysis ... - 2itp (6,238 bytes)
26: ...t the mutations activate the kinase by disrupting autoinhibitory interactions, and that they accelerate catalysis ... - 2itn (6,234 bytes)
26: ...t the mutations activate the kinase by disrupting autoinhibitory interactions, and that they accelerate catalysis ... - 2itx (6,166 bytes)
26: ...t the mutations activate the kinase by disrupting autoinhibitory interactions, and that they accelerate catalysis ... - 2itv (6,181 bytes)
26: ...t the mutations activate the kinase by disrupting autoinhibitory interactions, and that they accelerate catalysis ... - 2itw (6,157 bytes)
26: ...t the mutations activate the kinase by disrupting autoinhibitory interactions, and that they accelerate catalysis ... - 4il1 (7,022 bytes)
14: ... Although commonly assumed that CaM displaces the autoinhibitory domain (AID) blocking substrate access to its act... - 2ux0 (6,542 bytes)
26: ... and to the closure of the binding groove for the autoinhibitory helix by helix alphaD. The structural data, toget... - 1ial (4,375 bytes)
23: ...ffinity form by binding to a site overlapping the autoinhibitory sequence. The structure also has implications for... - 1vzo (6,594 bytes)
2: ... N-terminal kinase domain of MSK1 reveals a novel autoinhibitory conformation for a dual kinase protein==
26: The structure of MSK1 reveals a novel autoinhibitory conformation for a dual kinase protein.,Smith KJ,... - 2v7o (6,656 bytes)
26: ... and to the closure of the binding groove for the autoinhibitory helix by helix alphaD. The structural data, toget... - 7gqo (9,472 bytes)
10: ...iggers host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-terminal fragment (PubMed:33410748).[UniP...
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