Results 11 to 20 of about 15,352 (140)
Expression Analysis of the Small GTP-Binding Protein Rac in Pterygium
Türk Oftalmoloji Dergisi, 2023 Objectives: To determine the roles of small GTP-binding proteins Rac1, Rac2, and Rac3 expression in pterygial tissue and to compare these expressions with normal conjunctival tissue.
Ahmet Saracaloğlu +6 more
doaj +3 more sources
Interaction of mastoparan with the low molecular mass GTP-binding proteins rho/rac [PDF]
FEBS Letters, 1991 Mastoparan, which has been shown to active G proteins [1], inhibits the ADP‐ribosylation of 20 kDa human platelet membrane proteins catalyzed by Clostridium botulinum exoenzyme C3 half‐maximally and maximally (90%) at 20 and 100 μM concentrations, respectively. Inhibition of ADP‐ribosylation was enhanced by GTP‐γS.
Ingo Just, Klaus Aktories
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GTP-binding proteins of the Rho/Rac family: regulation, effectors and functions in vivo [PDF]
BioEssays, 2007 AbstractRho/Rac proteins constitute a subgroup of the Ras superfamily of GTP hydrolases. Although originally implicated in the control of cytoskeletal events, it is currently known that these GTPases coordinate diverse cellular functions, including cell polarity, vesicular trafficking, the cell cycle and transcriptomal dynamics. In this review, we will
Xosé R Bustelo, Vincent Sauzeau
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Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1 [PDF]
Structure, 2000 Members of the Rho family of small GTP-binding proteins, such as Rho, Rac and Cdc42, have a role in a wide range of cell responses. These proteins function as molecular switches by virtue of a conformational change between the GTP-bound (active) and GDP-bound (inactive) forms.
Lu-Yun Lian +2 more
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The small GTP-binding proteins, Rac and Rho, regulate cytoskeletal organization and exocytosis in mast cells by parallel pathways. [PDF]
Molecular Biology of the Cell, 1996 In mast cells, activation of GTP-binding proteins induces centripetal reorganization of actin filaments. This effect is due to disassembly, relocalization, and polymerization of F-actin and is dependent on two small GTPases, Rac and Rho. Activities of Rac and Rho are also essential for the secretory function of mast cells.
A Koffer
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The cytokinesis regulator RacGAP1 is a Rac1-specific GAP on membranes. [PDF]
Protein SciAbstract Rho family small GTPases are essential for cytokinesis completion. RacGAP1, a dimeric multidomain protein with a lipid‐binding C1 domain and a GTPase‐activating protein (GAP) domain, is a major regulator in this process. However, despite many cellular and biochemical studies, whether RhoA or Rac1 is the actual substrate inactivated by RacGAP1 ...
Dubois P +5 more
europepmc +2 more sources
Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac [PDF]
Biochemical Journal, 1997 Bacterially expressed glutathione S-transferase fusion proteins containing Rac1 were used to identify binding proteins of this Rho family GTPase present in a bovine brain extract. Five proteins of 85, 110, 125, 140 and 170 kDa were detected, all of which were associated exclusively with guanosine 5´-[γ-thio]triphosphate-bound Rac1, not with GDP-bound ...
Y, Kitamura +10 more
openaire +3 more sources
Frontiers in Genetics, 2022 Small GTPases are the key to actin cytoskeleton signaling, which opens the lock of effector proteins to forward the signal downstream in several cellular pathways. Actin cytoskeleton assembly is associated with cell polarity, adhesion, movement and other
Preeti Umarao +2 more
doaj +1 more source
Effects of decreased Rac activity and malignant state on oral squamous cell carcinoma in vitro.
PLoS ONE, 2021 Rac proteins, members of the Rho family of small GTP-binding proteins, have been implicated in transducing a number of signals for various biological mechanisms, including cell cytoskeleton organization, transcription, proliferation, migration, and ...
Yudai Matsuoka +3 more
doaj +1 more source
Distinct Patterns of Actin Organization Regulated by the Small GTP-binding Proteins Rac and Rho
Cold Spring Harbor Symposia on Quantitative Biology, 1992 A J, Ridley, A, Hall
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