Results 171 to 180 of about 4,434,687 (184)

GTP‐BINDING PROTEINS G_sα, G_iα, AND RAN IDENTIFIED IN MITOCHONDRIA OF HUMAN PLACENTA

Cell Biology International, 2002
GTP‐binding proteins (GTPases) have been detected in the mitochondria of human placenta. It has been proposed that porin interacts with GTPases in the mitochondrion to modulate contact site function, however, their identity and location is not known. In this study, we investigated the location of GTPases in mitochondria from term placentae as well as ...
Ileana Kuyznierewicz, Murray Thomson
openaire   +1 more source

Phenotype of the fission yeast cell cycle regulatory mutant pim1‐46 is suppressed by a tobacco cDNA encoding a small, Ran‐like GTP‐binding protein

The Plant Journal, 1994
Mutations in which the onset of mitosis is uncoupled from the completion of DNA replication has recently been described. Characterization of these mutants led to the identification of Pim1/Spi1 in fission yeast and RCC1/Ran proteins in mammalian cells.
Merkle, Thomas, Haizel, T., Matsumoto, T., Harter, K., Dallmann, G., Nagy, F.   +5 more
openaire   +3 more sources

Cloning of cDNAs encoding a cell-cycle-regulatory GTP-binding low-Mr (GBLM) protein, Ran/TC4, from micronucleated Tetrahymena thermophila and amicronucleated Tetrahymena pyriformis

Gene, 1994
Using PCR we have isolated two novel, closely related cDNA clones coding for a GTP-binding low-M(r) protein from Tetrahymena cells. The two clones from T. thermophila and T. pyriformis have open reading frames encoding proteins of 225 amino acids (aa) with a calculated M(r) of 25,648, and of 223 aa with a calculated M(r) of 25,421, respectively.
K, Nagata, T, Takemasa, S, Alam, T, Hattori, Y, Watanabe, Y, Nozawa   +5 more
openaire   +2 more sources

GTP-binding proteins G(salpha), G(ialpha), and Ran identified in mitochondria of human placenta.

Cell biology international, 2002
GTP-binding proteins (GTPases) have been detected in the mitochondria of human placenta. It has been proposed that porin interacts with GTPases in the mitochondrion to modulate contact site function, however, their identity and location is not known. In this study, we investigated the location of GTPases in mitochondria from term placentae as well as ...
Ileana, Kuyznierewicz, Murray, Thomson
openaire   +1 more source

Comparative genomics of prokaryotic GTP-binding proteins (the Era, Obg, EngA, ThdF (TrmE), YchF and YihA families) and their relationship to eukaryotic GTP-binding proteins (the DRG, ARF, RAB, RAN, RAS and RHO families).

Journal of molecular microbiology and biotechnology, 2001
Several GTP-binding proteins with poorly defined functions were previously identified in Escherichia coli (i.e. Era, ThdF (TrmE)), Bacillus subtilis (i.e. Obg) and Neisseria gonorrhoeae (i.e. EngA). In these species, every individual protein is encoded by an essential gene.
openaire   +1 more source

Identification of GTP Binding Nuclear Protein Ran as an Upregulation Target in Acetoin Glucoside Mediated Plant Growth Enhancement

The Natural Products Journal, 2017
Jyoti Tripathi, Vanshika Adiani, Sukhendu B. Ghosh, Thumballi R. Ganapathi, Ajoy K. Bauri, Suchandra Chatterjee, Vishwas M. Kulkarni, Prasad S. Variyar, Arun Sharma   +8 more
openaire   +1 more source

An Arabidopsis Ran-binding protein, AtRanBP1c, is a co-activator of Ran GTPase-activating protein and requires the C-terminus for its cytoplasmic localization

Planta, 2003
Stanley Roux
exaly  

Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport

Nature, 1999
Alfred Wittinghofer, Takeharu Nishimoto, Jürgen Kuhlmann   +2 more
exaly  

Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta.

Proceedings of the National Academy of Sciences of the United States of America, 1996
Günter Blobel, A Radu
exaly  

Tyr39 of Ran Preserves the Ran·GTP Gradient by Inhibiting GTP Hydrolysis

Journal of Molecular Biology, 2010
Klaus Gerwert, Carsten Kötting
exaly