Results 321 to 330 of about 232,963 (342)

Activation of Small GTP-Binding Proteins

1999
Guanosine triphosphate- (GTP-) binding proteins act as molecular switches: active in GTP-bound form and inactivated when bound GTP is hydrolyzed. Switching on these proteins initiates a wide range of cellular responses and is controlled by multiple factors.
Anna Koffer, Richard Sullivan
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GTP-Binding Proteins: Structures, interactions and relationships

Current Biology, 1994
Recently available crystal structures show that some, though not all, GTP-binding proteins have a common 'G-domain' topology, variations on which confer distinct functional properties.
Alfred Wittinghofer, Thomas Schweins
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Dynamin: A microtubule-associated GTP-binding protein

Journal of Cell Science, 1991
ABSTRACT We recently identified dynamin as a third nucleotide-sensitive microtubule-associated protein in brain tissue, in addition to kinesin and cytoplasmic dynein. Molecular cloning analysis has revealed that dynamin contains the three consensus elements characteristic of GTP-binding proteins, and biochemical results support a role ...
Robert A. Obar, Richard B. Vallee, Howard S. Shpetner   +2 more
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Unconventional GTP-Binding Proteins in Plants

2009
G proteins, including monomeric G proteins and heterotrimeric G proteins composed of Gα, Gβ, and Gγ subunits, are molecular switches in cellular signaling. In addition to these classic G proteins, plants have several types of unconventional G proteins, such as extra-large G proteins (XLGs), developmentally regulated G proteins (DRGs), and GPCR-type G ...
Timothy E. Gookin, Sarah M. Assmann, Lei Ding   +2 more
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Small GTP-binding protein-coupled receptors

Biochemical Society Transactions, 2004
Heterotrimeric GPCRs (G-protein-coupled receptors) form the largest group of integral membrane receptor proteins and mediate diverse physiological processes. In addition to signalling via heterotrimeric G-proteins, GPCRs can also signal by interacting with various small G-proteins to regulate downstream effector pathways.
Andy V. Babwah, Andy V. Babwah, Moshmi Bhattacharya, Moshmi Bhattacharya, Stephen S. G. Ferguson, Stephen S. G. Ferguson   +5 more
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Partial characterization of GTP-binding proteins in Neurospora

Biochemical and Biophysical Research Communications, 1987
Six fractions of GTP-binding proteins separated by gel filtration of a mycelial extract containing membrane components of Neurospora crassa were partially characterized. [35S]GTP gamma S bound to GTP-binding protein was assayed by repeated treatments with a Norit solution and centrifugation.
Yukie Miyamoto-Shinohara, Kazuhiko Furukawa, Kohji Hasunuma   +2 more
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Regulatory Role for GTP-Binding Proteins in Endocytosis

Science, 1989
Guanosine 5′-triphosphate (GTP)-binding proteins have been implicated in the transport of newly synthesized proteins along the secretory pathway of yeast and mammalian cells. Early vesicle fusion events that follow receptor-mediated endocytosis as measured by three in vitro assays were blocked by guanosine 5′- O -(3-
Philip D. Stahl, R Diaz, Luis S. Mayorga
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The Cellular Functions of Small GTP-Binding Proteins

Science, 1990
A substantial number of novel guanine nucleotide binding regulatory proteins have been identified over the last few years but the function of many of them is largely unknown. This article will discuss a particular family of these proteins, structurally related to the Ras oncoprotein.
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Signal transducing gtp-binding proteins in olfaction

Comparative Biochemistry and Physiology Part A: Physiology, 1990
1. Several members of the family of heterotrimeric signal transducing GTP-binding proteins have been identified in the olfactory epithelium of vertebrates by biochemical and molecular cloning techniques. 2. Biochemical and electrophysiological evidence indicates that one or more GTP-binding proteins mediate many olfactory responses by coupling stimulus
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Small GTP-binding proteins as compartmental markers

Seminars in Cell Biology, 1992
Each intracellular compartment involved in the biosynthetic/secretory pathway of eukaryotic cells bears at its surface at least one small GTP-binding protein. Most of them belong to a distinct branch of the p21ras superfamily, the Sec4/Ypt1/rab family. Other proteins are members of the ARF family.
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