Results 171 to 180 of about 13,129 (191)

Conformational States of the Nuclear GTP-Binding Protein Ran and Its Complexes with the Exchange Factor RCC1 and the Effector Protein RanBP1 [PDF]

open access: yesBiochemistry, 1999
It has been shown before by (31)P NMR that Ras bound to the nonhydrolyzable GTP analogue guanosine 5'-O-(beta, gamma-imidotriphosphate) (GppNHp) exists in two conformations which are rapidly interconverting with a rate constant of 3200 s-1 at 30 degrees C [Geyer, M., et al. (1996) Biochemistry 35, 10308-10320].
Geyer, M.   +6 more
openaire   +4 more sources

Interaction of the Nuclear GTP-Binding Protein Ran with Its Regulatory Proteins RCC1 and RanGAP1

Biochemistry, 1995
The guanine nucleotide dissociation and GTPase reactions of Ran, a Ras-related nuclear protein, have been investigated using different fluorescence techniques to determine how these reactions are stimulated by the guanine nucleotide exchange factor RCC1 and the other regulatory protein, RanGAP1 (GTPase-activating protein).
H Ponstingl   +2 more
exaly   +3 more sources

Sequence of a canine cDNA clone encoding a Ran/TC4 GTP-binding protein

Gene, 1992
We report the isolation and characterization of a canine cDNA encoding a 216-amino acid GTP-binding protein of the Ras superfamily. The protein is almost identical to the human TC4 [Drivas et al., Mol. Cell. Biol. 10 (1990) 1793-1798] and Ran [Bischoff and Ponstingl, Proc. Natl. Acad. Sci.
Vesa Olkkonen   +2 more
exaly   +3 more sources

Sequence of a plant cDNA from Vicia faba encoding a novel Ran-related GTP-binding protein

Plant Molecular Biology, 1994
A clone obtained from a broad bean (Vicia faba) developing cotyledon cDNA library contained the complete coding sequence of a polypeptide with very high homology to the small GTP-binding proteins Ran from human cells and Spi1 from yeast. These proteins belong to the ras superfamily of proteins involved in different basic cellular processes.
Gerhard Saalbach
exaly   +3 more sources

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 [PDF]

open access: yesThe 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   +5 more
openaire   +4 more sources

Isolation and characterization of Ras-related GTP-binding protein (Ran) from Lepidium latifolium L. reveals its potential role in regulating abiotic stress tolerance

Acta Physiologiae Plantarum, 2014
Lepidium latifolium L., a weed distributed in the Ladakh region of Himalayan range, belongs to Brassicaceae family and reported to withstand low temperature stress
Vimlendu Bhushan Sinha   +2 more
exaly   +2 more sources

Cloning and Expression of a cDNA-Encoding the Homologue of Ran/TC4 GTP-Binding Protein from Plasmodium falciparum

Biochemical and Biophysical Research Communications, 1994
In our effort to identify and study proteins that are important for the progression of the malaria parasite, Plasmodium falciparum, through the cell cycle, we have cloned and sequenced the homologue of Ras-related nuclear protein Ran/TC4 (PfRan). The predicted peptide sequence of PfRan is 214 amino acids long and contains consensus motifs of the Ras ...
F F, Dontfraid, D, Chakrabarti
openaire   +2 more sources

Ran, a GTP‐binding protein involved in nucleocytoplasmic transport and microtubule nucleation, relocates from the manchette to the centrosome region during rat spermiogenesis

Molecular Reproduction and Development, 2002
AbstractRan, a Ras‐related GTPase, is required for transporting proteins in and out of the nucleus during interphase and for regulating the assembly of microtubules. cDNA cloning shows that rat testis, like mouse testis, expresses both somatic and testis‐specific forms of Ran–GTPase.
Abraham L, Kierszenbaum   +3 more
openaire   +2 more sources

GTP‐BINDING PROTEINS G, G, 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

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   +5 more
openaire   +2 more sources

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