Results 21 to 30 of about 221,192 (198)
Chromium GTP (CrGTP) has been used to probe the stereochemistry of metal-GTP binding to exchangeable site of tubulin and to examine the fate and role of nucleotide-bound metal ion in GTP hydrolysis associated with microtubule assembly. The absolute stereoconfiguration of the two pairs of diastereomers of beta,gamma-bidentate CrGTP has been determined ...
C Valentin-Ranc+2 more
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An intermolecular G-quadruplex as the basis for GTP recognition in the class V–GTP aptamer [PDF]
Many naturally occurring or artificially created RNAs are capable of binding to guanine or guanine derivatives with high affinity and selectivity. They bind their ligands using very different recognition modes involving a diverse set of hydrogen bonding and stacking interactions.
Nasiri, Amir Hossein+4 more
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Crystallographic Evidence for Substrate-Assisted GTP Hydrolysis by a Small GTP Binding Protein [PDF]
GTP hydrolysis by small GTP binding proteins of the Ras superfamily is a universal reaction that controls multiple cellular regulations. Its enzymic mechanism has been the subject of long-standing debates as to the existence/identity of the general base and the electronic nature of its transition state.
Jacqueline Cherfils+1 more
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KRAS G13D sensitivity to neurofibromin-mediated GTP hydrolysis
Significance The protooncogene KRAS, a GTPase, is responsible for activating the MAPK pathway. Cancer mutations at codons 12, 13, or 61 are thought to stabilize KRAS-GTP primarily by preventing GAP protein-stimulated GTP hydrolysis, thereby stabilizing ...
Dana Rabara+6 more
semanticscholar +1 more source
Severing enzymes amplify microtubule arrays through lattice GTP-tubulin incorporation
Severing to build microtubules Microtubules are essential intracellular polymers, built from tubulin subunits, that establish cell shape, move organelles, and segregate chromosomes during cell division. Vemu et al.
Annapurna Vemu+6 more
semanticscholar +1 more source
Going in GTP cycles in the nucleolus [PDF]
Proteins are directed to cellular compartments by specific localization signals. A GTP-driven cycle has now been identified as a mechanism for protein targeting to the nucleolus. The involvement of a GTP switch suggests that nucleolar localization can be regulated and may be responsive to extracellular stimuli via signaling pathways.
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Dynamin superfamily proteins are multidomain mechano‐chemical GTPases which are implicated in nucleotide‐dependent membrane remodeling events. A prominent feature of these proteins is their assembly‐ stimulated mechanism of GTP hydrolysis.
O. Daumke, Gerrit J. K. Praefcke
semanticscholar +1 more source
GTP is a major regulator of multiple cellular processes, but tools for quantitative evaluation of GTP levels in live cells have not been available. We report the development and characterization of genetically encoded GTP sensors, which we constructed by
A. Bianchi-Smiraglia+16 more
semanticscholar +1 more source
Conversion of GDP into GTP by nucleoside diphosphate kinase on the GTP-binding proteins.
A direct interaction of alpha beta gamma trimeric GTP binding proteins (G proteins; G0 and Gs) with nucleoside diphosphate kinase (NDP kinase) was investigated with homogeneously purified proteins. There was a progressive release of 32Pi from [gamma-32P]ATP when GDP-bound G0 was incubated together with NDP kinase.
S, Kikkawa+6 more
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![Graphic][1] Localization of nucleostemin to the nucleolus (top) is controlled by a GTP switch.Nucleolar size and cell growth rate are positively correlated, perhaps based on ribosome biogenesis being localized to the nucleolus, but little is known about how nucleolar size ...
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