Research Topics
Genomes and Genes | H PonstinglSummaryAffiliation: German Cancer Research Center Country: Germany Publications
| Collaborators
|
Detail Information
Publications
Human RanBP3, a group of nuclear RanGTP binding proteinsL Mueller
Division for Molecular Biology of Mitosis, German Cancer Research Center, Heidelberg
FEBS Lett 427:330-6. 1998..These proteins are localized in the nucleus, preferentially bind RanGTP and may be nuclear effectors of the Ran pathway...- Localization of the gene encoding the Ran-binding protein RanBP2 to human chromosome 2q11-q13 by fluorescence in situ hybridizationH Krebber
Division for Molecular Biology of Mitosis, German Cancer Research Center, Heidelberg
Genomics 43:247-8. 1997 
Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1F R Bischoff
Division for Molecular Biology of Mitosis, German Cancer Research Center, Heidelberg
EMBO J 14:705-15. 1995..RanBP1 is the first member of a new class of proteins regulating the binding and hydrolysis of GTP by Ras-related proteins...- RanGAP1 induces GTPase activity of nuclear Ras-related RanF R Bischoff
Division for Molecular Biology of Mitosis, German Cancer Research Center, Heidelberg, Federal Republic of Germany
Proc Natl Acad Sci U S A 91:2587-91. 1994..It was purified from HeLa cell lysates and induces GTPase activity of Ran, but not Ras, by more than 3 orders of magnitude. The Ran mutant Q69L, modeled after RasQ61L, which is unable to hydrolyze bound GTP, is insensitive to RanGAP1... - DelGEF, an RCC1-related protein encoded by a gene on chromosome 11p14 critical for two forms of hereditary deafnessJ Uhlmann
Division for Molecular Biology of Mitosis, German Cancer Research Center, Heidelberg
FEBS Lett 460:153-60. 1999..In addition, we have identified a murine homologue, mDelGEF. The ubiquitously expressed soluble protein hDelGEF1 is found both in the cyytoplasm and in the nucleus. Overexpressed hDelGEF2 colocalizes with mitochondria... - Assignment of the human serine/threonine protein phosphatase 4 gene (PPP4C) to chromosome 16p11-p12 by fluorescence in situ hybridizationH Bastians
Division of Molecular Biology of Mitosis, German Cancer Research Center, Heidelberg, Germany
Genomics 42:181-2. 1997 - Ubiquitous expression and testis-specific alternative polyadenylation of mRNA for the human Ran GTPase activator RanGAP1H Krebber
Division for Molecular Biology of Mitosis, German Cancer Research Center, Heidelberg, Germany
Gene 180:7-11. 1996..Taking the 3' UTR of RanGAP1, which lies downstream of the first polyadenylation signal, as a probe in Northern blot analysis, we confirmed that this second transcript found in testis results from a distinct 3' UTR... - Human Supt5h protein, a putative modulator of chromatin structure, is reversibly phosphorylated in mitosisA A Stachora
Deutsches Krebsforschungszentrum, Division for Molecular Biology of Mitosis, Heidelberg, Germany
FEBS Lett 409:74-8. 1997..One of them, with the consensus sequence P-T/S-P-S-P-Q/A-S/G-Y, is similar to the C-terminal domain in the largest subunit of RNA polymerase II... - Localization of the novel serine/threonine protein phosphatase 6 gene (PPP6C) to human chromosome Xq22.3H Bastians
Division for Molecular Biology of Mitosis, German Cancer Research Center, Heidelberg, Germany
Genomics 41:296-7. 1997 - The novel human protein serine/threonine phosphatase 6 is a functional homologue of budding yeast Sit4p and fission yeast ppe1, which are involved in cell cycle regulationH Bastians
Deutsches Krebsforschungszentrum, Division for Molecular Biology of Mitosis, Heidelberg, Germany
J Cell Sci 109:2865-74. 1996..These data indicate that human PP6 is a functional homologue of budding yeast Sit4p and fission yeast ppe1, implying a function of PP6 in cell cycle regulation... - Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transportF R Bischoff
Division of Molecular Biology of Mitosis, German Cancer Research Center, Heidelberg
Proc Natl Acad Sci U S A 92:1749-53. 1995..Thus, a defect in either of the two antagonistic regulators of Ran would result in a shutdown of Ran-dependent transport processes, in agreement with the almost identical phenotypes described for such defects in budding yeast... - Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1F R Bischoff
Deutsches Krebsforschungszentrum, Heidelberg, Germany
Nature 354:80-2. 1991..Here we show that RCC1 specifically catalyses the exchange of guanine nucleotides on the Ran protein but not on the protein c-Ha-ras p21 (p21ras)... - Mitotic regulator protein RCC1 is complexed with a nuclear ras-related polypeptideF R Bischoff
Project Molecular Biology of Mitosis, Deutsches Krebsforschungszentrum, Heidelberg, Federal Republic of Germany
Proc Natl Acad Sci U S A 88:10830-4. 1991..We designate this polypeptide Ran, for ras-related nuclear protein... - Yrb4p, a yeast ran-GTP-binding protein involved in import of ribosomal protein L25 into the nucleusG Schlenstedt
Medizinische Biochemie, Universit at des Saarlandes, D 66421 Homburg, Germany
EMBO J 16:6237-49. 1997..L25 binds to Yrb4p and Pse1p and is released by Gsp1p-GTP. Consistent with its putative role as an import receptor for L25-like proteins, Yrb4p localizes to the cytoplasm, the nucleoplasm and the NPC... - Ran-binding protein 5 (RanBP5) is related to the nuclear transport factor importin-beta but interacts differently with RanBP1R Deane
Abteilung Molekulare Biologie der Mitose, Deutsches Krebsforschungszentrum, Heidelberg, Germany
Mol Cell Biol 17:5087-96. 1997..We propose that RanBP5 is a mediator of a nucleocytoplasmic transport pathway that is distinct from the importin-alpha-dependent import of proteins with a classical NLS... - A 47-kDa human nuclear protein recognized by antikinetochore autoimmune sera is homologous with the protein encoded by RCC1, a gene implicated in onset of chromosome condensationF R Bischoff
Institute of Cell and Tumor Biology, Deutsches Krebsforschungszentrum, Heidelberg, Federal Republic of Germany
Proc Natl Acad Sci U S A 87:8617-21. 1990..This sequence is highly homologous with the translated reading frame of RCC1, a gene reportedly involved in regulating onset of mammalian chromosome condensation... - The human gene ZFP161 on 18p11.21-pter encodes a putative c-myc repressor and is homologous to murine Zfp161 (Chr 17) and Zfp161-rs1 (X Chr)I Sobek-Klocke
Faculty of Biology, Genetechnology Microbiology Unit, University of Bielefeld, Germany
Genomics 43:156-64. 1997..Mapping of Zfp161 confirms and extends a region of homology between distal mouse chromosome 17 and human 18p... - RNA1 encodes a GTPase-activating protein specific for Gsp1p, the Ran/TC4 homologue of Saccharomyces cerevisiaeJ Becker
Max Planck Institut fur molekulare Physiologie, Abteilung Strukturelle Biologie, Dortmund, Germany
J Biol Chem 270:11860-5. 1995..The GTP hydrolysis of Ran is induced by RanGAP1 and rna1p but not by Rna1p. Implications for the suggested functions of Ran/TC4/Gsp1p in nuclear transport and mitotic control are discussed... - Structure of the pleckstrin homology domain from beta-spectrinM J Macias
European Molecular Biology Laboratory, Heidelberg, Germany
Nature 369:675-7. 1994..There is a distant relationship to the peptidyl-prolyl-cis-trans-isomerase FKBP in which this pocket is involved in the binding of the macrocyclic compound FK506 (refs 8-11)... - NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxinH Ponstingl
Karolinska Institute, Department of Medical Biochemistry and Biophysics, Stockholm, Sweden
Eur J Biochem 244:384-99. 1997..One of these water molecules mediates hydrogen bonds between the protein backbone and the ribityl chain of the FMN cofactor... - Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysisF Aslund
Department of Medical Biochemistry and Biophysics, Karolinska Institute, S 171 77 Stockholm, Sweden
J Biol Chem 271:6736-45. 1996..Thus, despite an identical active site disulfide motif and a similar secondary structure and tertiary fold, Grx3 and Grx1 display large functional differences in in vitro protein disulfide oxido-reduction reactions...