Results 261 to 270 of about 381,524 (309)

Rho, Rho, Rho Your Vaccinia

Science's STKE, 2006
Viruses subvert a variety of host cell mechanisms during infection, replication, and dissemination. Valderrama et al. now describe how vaccinia virus promotes cellular motility by interfering with the activity of RhoA, a small guanosine triphosphase-binding protein involved in intracellular signaling, which ...
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Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)

Science, 1996
The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP⋅RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase,
K, Kimura, M, Ito, M, Amano, K, Chihara, Y, Fukata, M, Nakafuku, B, Yamamori, J, Feng, T, Nakano, K, Okawa, A, Iwamatsu, K, Kaibuchi   +11 more
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rho and rho-Related Proteins

1993
The Rho-like proteins form a distinct subgroup of the ras superfamily of small GTPases. They act as molecular switches having an inactive, GDP-bound and an active, GTP-bound conformation and have many structural and biochemical features in common with p21ras.
A. J. Ridley, A. Hall
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Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)

Biochimie, 2001
The Rho-GDP dissociation inhibitor (Rho-GDI) was used as bait in a two-hybrid screen of a human leucocyte cDNA library. Most of the isolated cDNAs encoded GTPases of the Rho subfamily: RhoA, B, C, Rac1, 2, CDC42 and RhoG. The newly discovered RhoH interacted very poorly with Rho-GDI.
Fauré, J., Dagher, M. C.
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Phosphorylation of Rho GDI Stabilizes the Rho A-Rho GDI Complex in Neutrophil Cytosol

Biochemical and Biophysical Research Communications, 1996
The GDP dissociation inhibitor Rho GDI from bovine neutrophil cytosol was purified in association with prenylated Rho A. Upon treatment of this complex with alkaline phosphatase, the Rho A and Rho GDI components were released to their free forms. Following migration in 2D-PAGE and specific immunodetection, the shape of the spot of Rho GDI was found to ...
N, Bourmeyster, P V, Vignais
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[Rho-Rho kinase pathway].

Nihon rinsho. Japanese journal of clinical medicine, 2004
The serine/threonine protein kinase Rho kinase, a downstream effector of the small GTPase Rho, regulates actin cytoskeletal organization, cell adhesion, cell motility, smooth muscle contraction and gene expression. Rho kinase constitutes the essential regulatory system for myosin phosphatase, controlling myosin light chain phosphorylation and thereby ...
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On fuzzy normal RHO-filters and usual RHO-filters of RHO-algebras

AIP Conference Proceedings, 2023
Arkan Ajil Atshan, Shuker Mahmood Khalil
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A measurement of $\gamma\gamma \to$$\rho^+\rho^-$

1989
The reaction γγ→$\rho^+\rho^-$→$\pi^+\pi^-\pi^0\pi^0$ has been studied with the ARGUS detector at the e+e− storage ring DORIS II at DESY. Near threshold, the cross section for this reaction is about four times smaller than for the reaction γγ→$\rho^0\rho^0$
Albrecht, H., Böckmann, P., Schulz, H. D., Sefkow, F., Spengler, J., Wurth, R., Yagil, A., Appuhn, R. D., Drescher, A., Hast, C., Kamp, D., Kolanoski, H., Gläser, R., Lindner, A., Mankel, R., Matthiesen, U., Scheck, H., Schweda, G., Spaan, B., Walther, A., Wegener, D., Volland, U., Wegener, H., Harder, G., Funk, W., Gabriel, J. C., Stiewe, J., Werner, S., Charlesworth, C. E. K., Edwards, K. W., Frisken, W. R., Kapitza, H., Kutschke, R., MacFarlane, D. B., Krüger, A., McLean, K. W., Nilsson, A. W., Orr, R. S., Parsons, J. A., Patel, P. M., Prentice, J. D., Seidel, S. C., Swain, J. D., Tsipolitis, G., Yoon, T.-S., Nippe, A., Ammar, R., Ball, S., Coppage, D., Davis, R., Kanekal, S., Kwak, N., Ruf, T., Schael, S., Schubert, K. R., Strahl, K., Reidenbach, M., Waldi, R., Boštjančič, B., Kernel, G., Križan, P., Križnič, E., Pleško, M., Cronström, H. I., Jönsson, L., Babaev, A., Danilov, M., Schäfer, M., Fominykh, B., Golutvin, A., Gorelov, I., Lubimov, V., Rostovtsev, A., Semenov, A., Semenov, S., Shevchenko, V., Soloshenko, V., Tchistilin, V., Schmidt-Parzefall, W., Tichomirov, I., Zaitsev, Yu., Childers, R., Darden, C. W., Fernholz, R. C., ARGUS Collaboration, Schröder, H.   +85 more
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Rho

2000
Abstract Rho was first identified in 1985 as a cDNA encoding a small GTP-binding protein related to Ras. Later, Rho was identified as the target of the Clostridium botulinum exoenzyme C3 transferase, which had been shown previously to induce changes to the morphology of mammalian tissue-culture cells. Subsequently, Rho and then a closely
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$B \to \rho\pi, B \to \rho\rho$ and the measurement of $\alpha$ at LHCb

2007
The potential of LHCb for the extraction of the CKM angle α using the analysis of the B→(ρπ)0 and B→(ρρ)±,0 decay modes has been extensively studied. The expected performances are presented in this document.
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