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TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger  mechanism | Nature
TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism | Nature

Structural plasticity mediates distinct GAP‐dependent GTP hydrolysis  mechanisms in Rab33 and Rab5 - Majumdar - 2017 - The FEBS Journal - Wiley  Online Library
Structural plasticity mediates distinct GAP‐dependent GTP hydrolysis mechanisms in Rab33 and Rab5 - Majumdar - 2017 - The FEBS Journal - Wiley Online Library

Energy profile and chemical transformations upon GTP hydrolysis in the... |  Download Scientific Diagram
Energy profile and chemical transformations upon GTP hydrolysis in the... | Download Scientific Diagram

Modeling the mechanisms of biological GTP hydrolysis - ScienceDirect
Modeling the mechanisms of biological GTP hydrolysis - ScienceDirect

Inhibition and Termination of Physiological Responses by GTPase Activating  Proteins | Physiological Reviews
Inhibition and Termination of Physiological Responses by GTPase Activating Proteins | Physiological Reviews

See previous page) (A) rates of intrinsic and GAP-mediated hydrolysis... |  Download Scientific Diagram
See previous page) (A) rates of intrinsic and GAP-mediated hydrolysis... | Download Scientific Diagram

Solved Nuclear import is driven by the hydrolysis of GTP, | Chegg.com
Solved Nuclear import is driven by the hydrolysis of GTP, | Chegg.com

Phospholipase C-β1 Directly Accelerates GTP Hydrolysis by Gαq and  Acceleration Is Inhibited by Gβγ Subunits* - Journal of Biological Chemistry
Phospholipase C-β1 Directly Accelerates GTP Hydrolysis by Gαq and Acceleration Is Inhibited by Gβγ Subunits* - Journal of Biological Chemistry

Physicochemical Insights into Microscopic Events Driven by GTP Hydrolysis  Reaction in Ras-GAP system | bioRxiv
Physicochemical Insights into Microscopic Events Driven by GTP Hydrolysis Reaction in Ras-GAP system | bioRxiv

Molecules | Free Full-Text | Structural Insights into the Regulation  Mechanism of Small GTPases by GEFs | HTML
Molecules | Free Full-Text | Structural Insights into the Regulation Mechanism of Small GTPases by GEFs | HTML

GTPase cycles control Ras and Tubulin - YouTube
GTPase cycles control Ras and Tubulin - YouTube

Rab Proteins Regulate Membrane Fusion Through GTP Hydrolysis. (Left)... |  Download Scientific Diagram
Rab Proteins Regulate Membrane Fusion Through GTP Hydrolysis. (Left)... | Download Scientific Diagram

GTP Hydrolysis Is Not Important for Ypt1 GTPase Function in Vesicular  Transport | Molecular and Cellular Biology
GTP Hydrolysis Is Not Important for Ypt1 GTPase Function in Vesicular Transport | Molecular and Cellular Biology

Ras and GTPase-activating protein (GAP) drive GTP into a precatalytic state  as revealed by combining FTIR and biomolecular simulations | PNAS
Ras and GTPase-activating protein (GAP) drive GTP into a precatalytic state as revealed by combining FTIR and biomolecular simulations | PNAS

Figure 3 from Hydrolysis of Guanosine Triphosphate (GTP) by the Ras·GAP  Protein Complex: Reaction Mechanism and Kinetic Scheme. | Semantic Scholar
Figure 3 from Hydrolysis of Guanosine Triphosphate (GTP) by the Ras·GAP Protein Complex: Reaction Mechanism and Kinetic Scheme. | Semantic Scholar

PDF] Modeling the mechanisms of biological GTP hydrolysis. | Semantic  Scholar
PDF] Modeling the mechanisms of biological GTP hydrolysis. | Semantic Scholar

GTPase-activating protein - Wikiwand
GTPase-activating protein - Wikiwand

Frontiers | This Is the End: Regulation of Rab7 Nucleotide Binding in  Endolysosomal Trafficking and Autophagy | Cell and Developmental Biology
Frontiers | This Is the End: Regulation of Rab7 Nucleotide Binding in Endolysosomal Trafficking and Autophagy | Cell and Developmental Biology

Common mechanisms of catalysis in small and heterotrimeric GTPases and  their respective GAPs
Common mechanisms of catalysis in small and heterotrimeric GTPases and their respective GAPs

Diversity of mechanisms in Ras–GAP catalysis of guanosine triphosphate  hydrolysis revealed by molecular modeling - Organic & Biomolecular  Chemistry (RSC Publishing) DOI:10.1039/C9OB00463G
Diversity of mechanisms in Ras–GAP catalysis of guanosine triphosphate hydrolysis revealed by molecular modeling - Organic & Biomolecular Chemistry (RSC Publishing) DOI:10.1039/C9OB00463G

Diversity of mechanisms in Ras–GAP catalysis of guanosine triphosphate  hydrolysis revealed by molecular modeling - Organic & Biomolecular  Chemistry (RSC Publishing) DOI:10.1039/C9OB00463G
Diversity of mechanisms in Ras–GAP catalysis of guanosine triphosphate hydrolysis revealed by molecular modeling - Organic & Biomolecular Chemistry (RSC Publishing) DOI:10.1039/C9OB00463G

Gβγ inhibits GTPase accelerating protein (GAP) activity of NF1 (A)... |  Download Scientific Diagram
Gβγ inhibits GTPase accelerating protein (GAP) activity of NF1 (A)... | Download Scientific Diagram

GTPase-activating protein - Wikipedia
GTPase-activating protein - Wikipedia

The GTPase-activating Protein RGS4 Stabilizes the Transition State for  Nucleotide Hydrolysis* - Journal of Biological Chemistry
The GTPase-activating Protein RGS4 Stabilizes the Transition State for Nucleotide Hydrolysis* - Journal of Biological Chemistry

Solved Small GTPases are generally active in the GTP-bound | Chegg.com
Solved Small GTPases are generally active in the GTP-bound | Chegg.com

The pre-hydrolysis state of p21ras in complex with GTP: new insights into  the role of water molecules in the GTP hydrolysis reaction of ras-like  proteins: Structure
The pre-hydrolysis state of p21ras in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins: Structure

RCSB PDB - 2NGR: TRANSITION STATE COMPLEX FOR GTP HYDROLYSIS BY CDC42:  COMPARISONS OF THE HIGH RESOLUTION STRUCTURES FOR CDC42 BOUND TO THE ACTIVE  AND CATALYTICALLY COMPROMISED FORMS OF THE CDC42-GAP.
RCSB PDB - 2NGR: TRANSITION STATE COMPLEX FOR GTP HYDROLYSIS BY CDC42: COMPARISONS OF THE HIGH RESOLUTION STRUCTURES FOR CDC42 BOUND TO THE ACTIVE AND CATALYTICALLY COMPROMISED FORMS OF THE CDC42-GAP.