Results 211 to 220 of about 61,508 (249)
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Rho-GTP binding proteins in Yersinia target cell interaction.
Advances in Experimental Medicine and Biology, 2003Among the more than 10 Yersinia species known three are pathogenic for humans: (i) Y. pestis is the causative agent of plaque, (ii) Y. pseudotuberculosis and (iii) Y. enterocolitica are enteropathogenic. The infection process of enteropathogenic yersiniae involves invasive as well as antiphagocytic and other immunomodulatory components.
M. Aepfelbacher +3 more
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Glucosylation of small GTP-binding Rho proteins disrupts endothelial barrier function [PDF]
American Journal of Physiology-Lung Cellular and Molecular Physiology, 1997 The endothelial cytoskeleton is important for the regulation of endothelial barrier function. Small GTP-binding Rho proteins play a central role in the organization of the microfilament system. Clostridium difficile toxin B (TcdB) inactivates Rho proteins by glucosylation at Thr-37.
Hippenstiel, Stefan +7 more
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Cellular responses regulated by rho-related small GTP-binding proteins
Philosophical Transactions of the Royal Society B: Biological Sciences, 1993Abstract Rho-related proteins are members of the ras superfamily of small GTP-binding proteins. Their function in fibroblasts has been analysed using microinjection of living cells. Rho appears to link plasma membrane receptors to the assembly of focal adhesions and actin stress fibres.
Anne Ridley +2 more
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Monoglucosylation of low-molecular-mass GTP-binding Rho proteins by clostridial cytotoxins
Trends in Cell Biology, 1995Rho proteins, which are involved in receptor-mediated regulation of the actin cytoskeleton, are substrates for ADP-ribosylation by Clostridium botulinum C3 toxins. Recently, it was shown that Rho and other members of the Rho subfamily of low-molecular-mass GTP-binding proteins are glucosylated by C. difficile toxins A and B.
Klaus Aktories, Ingo Just
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Tissue-specific variations in the expression and regulation of the small GTP-binding protein Rho
Biochimica Et Biophysica Acta - Molecular Cell Research, 1994Rho proteins are involved in the regulation of the assembly of the microfilamental cellular network and are known to be specific substrates for the ADP-ribosyltransferase C3 from Clostridium botulinum. Here, we studied the distribution of Rho and Rho-regulating proteins in extracts from various rabbit tissues.
Ingo Just
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Current Opinion in Cell Biology, 1998
Accumulating evidence indicates that Rho family small GTP-binding proteins regulate reorganization of the actin cytoskeleton. There are members of the Rho family in the budding yeast Saccharomyces cerevisiae, in which powerful molecular genetical approaches are applicable.
Yoshimi Takai, Kazuma Tanaka
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Accumulating evidence indicates that Rho family small GTP-binding proteins regulate reorganization of the actin cytoskeleton. There are members of the Rho family in the budding yeast Saccharomyces cerevisiae, in which powerful molecular genetical approaches are applicable.
Yoshimi Takai, Kazuma Tanaka
exaly +3 more sources
Small GTP-binding proteins. [PDF]
Physiological Reviews, 2001 Small GTP-binding proteins (G proteins) exist in eukaryotes from yeast to human and constitute a superfamily consisting of more than 100 members. This superfamily is structurally classified into at least five families: the Ras, Rho, Rab, Sar1/Arf, and ...
Takashi Matozaki +2 more
semanticscholar +2 more sources
An immunologist's look at the Rho and Rab GTP-binding proteins
Immunology Today, 1993The ras superfamily of small GTP-binding proteins contains three major branches: the Ras, Rho and Rab protein subfamilies. Recent advances in the field of ras-related small GTP-binding proteins suggest that it may be worthwhile to look at this superfamily from the standpoint of immunology.
P, Chavrier, J P, Gorvel, J, Bertoglio
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Effect of Rho family GTP-binding proteins on Amoeba proteus
Protoplasma, 2003While there is a number of studies on the effects of Rho GTPases on the actin-based cytoskeleton in higher eukaryotes, studies in protozoans are rather limited. The problem seems to be intriguing since the structure of protozoan cytoskeletons is distinct from most vertebrate cells.
W, Kłopocka, M J, Redowicz
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