Results 171 to 180 of about 29,147 (185)

The GTP-binding protein Ran/TC4 is required for protein import into the nucleus

Nature, 1993
Two cytosolic fractions (A and B) from Xenopus oocytes are sufficient to support protein import into the nuclei of digitonin-permeabilized cells. Fraction A recognizes the nuclear localization sequence (NLS) and binds the import substrate to the nuclear envelope, whereas fraction B mediates the subsequent passage of the bound substrate into the nucleus.
M S, Moore, G, Blobel
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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.
P, Dupree, V M, Olkkonen, P, Chavrier
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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).
C, Klebe, F R, Bischoff, H, Ponstingl, A, Wittinghofer   +3 more
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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.
G, Saalbach, V, Christov
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Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation

Biochemical and Biophysical Research Communications, 2006
Polo-like kinase functions are essential for the establishment of a normal bipolar mitotic spindle, although precisely how Plk1 regulates the spindle is uncertain. In this study, we report that the small GTP/GDP-binding protein Ran is associated with Plk1.
Yang, Feng, Jin Hui, Yuan, Sharon C, Maloid, Rebecca, Fisher, Terry D, Copeland, Dan L, Longo, Thomas P, Conrads, Timothy D, Veenstra, Andrea, Ferris, Steve, Hughes, Dimiter S, Dimitrov, Douglass K, Ferris   +11 more
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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
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Conformational States of the Nuclear GTP-Binding Protein Ran and Its Complexes with the Exchange Factor RCC1 and the Effector Protein RanBP1

Biochemistry, 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., Assheuer, R., Klebe, C., Kuhlmann, J., Becker, J., Wittinghofer, A., Kalbitzer, H.   +6 more
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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
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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, Mara, Gil, Eugene, Rivkin, Laura L, Tres   +3 more
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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
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