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487 results on '"Hübscher U"'

11. Control of DNA polymerase lambda stability by phosphorylation and ubiquitination during the cell cycle

Author

Wimmer, U, Ferrari, E, Hunziker, P, Hübscher, U, University of Zurich, and Hübscher, U

Subjects
1303 Biochemistry, 1311 Genetics, 1312 Molecular Biology, Genetics, 570 Life sciences, biology, 610 Medicine & health, 10071 Functional Genomics Center Zurich, U7 Systems Biology / Functional Genomics, 10226 Department of Molecular Mechanisms of Disease, Biochemistry, Molecular Biology
Published
2008
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16. Acoordinated interplay: proteins with multiple functions in DNA replication, DNA repair, cell cycle/checkpoint control, and transcription

Author

Stucki, M, Stagljar, I, Jónsson, Z O, Hübscher, U, University of Zurich, and Hübscher, U

Subjects
1312 Molecular Biology, 570 Life sciences, biology, 10226 Department of Molecular Mechanisms of Disease
Abstract

In eukaryotic cells, DNA transactions such as replication, repair, and transcription require a large set of proteins. In all of these events, complexes of more than 30 polypeptides appear to function in highly organized and structurally well-defined machines. We have learned in the past few years that the three essential macromolecular events, replication, repair, and transcription, have common functional entities and are coordinated by complex regulatory mechanisms. This can be documented for replication and repair, for replication and checkpoint control, and for replication and cell cycle control, as well as for replication and transcription. In this review we cover the three different protein classes: DNA polymerases, DNA polymerase accessory proteins, and selected transcription factors. The "common enzyme-different pathway strategy" is fascinating from several points of view: first, it might guarantee that these events are coordinated ; second, it can be viewed from and evolutionary angle ; and third, this strategy might provide cells with backup mechanisms for essential physiological tasks.

Published
2000

17. Biologically Active Molecules: Chemical Research, Development and Scale-up

Author

ANDREY, Dmytrenko, HÜBSCHER, U., ZHANG, Ling Yan, and Andrey, Dmytrenko

Subjects
drug-like compounds, building blocks, fluorescent dyes, [INFO.INFO-BT] Computer Science [cs]/Biotechnology, kinase-related products, target-focused libraries, services for pharmaceutical, selective inhibitors, biologically active substances, tangible compounds, combinatorial synthesis, [SDV.BIO] Life Sciences [q-bio]/Biotechnology
Abstract

The increasing demand for different biologically active molecules has posed challenges to the scientists to get the desired substances in large amounts either from natural sources or to produce synthetically through efficient and economically viable routes. Our company, OTAVA Ltd., provides a wide range of biologically active compounds modulating activity of distinct targets. Protein kinases are popular targets in oncology drug development. These proteins are upregulated in tumor cells making them ideal targets for selective tumor therapy. Currently kinase inhibitors are among the most preferred drugs in development by many pharmaceutical companies. Our company offers a variety of inhibitors including CDK4, DNA-PK, EGFR, CK2, CDK2, IKK-ε, GSK-3 and JNK3 inhibitors. We also propose sets of compounds that inhibit Histone Deacetylase (HDAC), Cyclooxygenase-1, CFTR Chloride Channel, Hypoxia-Inducible Factor-1, STAT3 Transcription Factor, NAD-Dependent Deacetylases SIRT1 and SIRT2. Protein-protein interactions have a key role in most biological processes and offer attractive opportunities for therapeutic intervention. Developing small molecules that modulate protein-protein interactions is difficult. There has been important progress in this endeavour in recent years. A recently developed inhibitior of interaction between the translation initiation factors eIF4E and eIF4G is commercially available from our company. In addition to these highly valuable products, OTAVA offers compounds which were evaluated in vitro on 60 human tumor cell lines. Our biologically active compounds can also be used in experimental biology for understanding the functions of biological molecules in vivo and some compounds could further be used in drug design.

Published
2011

20. Methylation of DNA polymerase beta by protein arginine methyltransferase 1 regulates its binding to proliferating cell nuclear antigen

Author

El-Andaloussi, N, Valovka, T, Toueille, M, Hassa, P O, Gehrig, P, Covic, M, Hübscher, U, Hottiger, M O, University of Zurich, and Hottiger, M O

Subjects
1303 Biochemistry, 1311 Genetics, 1305 Biotechnology, 1312 Molecular Biology, 570 Life sciences, biology, 610 Medicine & health, 10071 Functional Genomics Center Zurich, U7 Systems Biology / Functional Genomics
Published
2007

21. Structural determinants of HIV-1 reverse transcriptase stereoselectivity towards (beta)-L-deoxy- and dideoxy-pyrimidine nucleoside triphosphates: molecular basis for the combination of L-dideoxynucleoside analogs with non-nucleoside inhibitors in anti HIV chemotherapy

Author

Maga, G, Amacker, M, Hübscher, U, Gosselin, G, Imbach, J L, Mathé, C, Faraj, A, Sommadossi, J P, Spadari, S, University of Zurich, and Maga, G

Subjects
1303 Biochemistry, 1311 Genetics, 570 Life sciences, biology, 10226 Department of Molecular Mechanisms of Disease
Published
2006

22. Arginine methylation regulates DNA polymerase beta

Author

El-Andaloussi, N, Valovka, T, Toueille, M, Steinacher, R, Focke, F, Gehrig, P, Covic, M, Hassa, P O, Schär, P, Hübscher, U, Hottiger, M O, University of Zurich, and Hottiger, M O

Subjects
1307 Cell Biology, 1312 Molecular Biology, 570 Life sciences, biology, 610 Medicine & health, 10071 Functional Genomics Center Zurich, U7 Systems Biology / Functional Genomics, 10226 Department of Molecular Mechanisms of Disease
Published
2006

24. Modulation of cellular response to cisplatin by a novel inhibitor of DNA polymerase beta

Author

Boudsocq, F, Benaim, P, Canitrot, Y, Knibiehler, M, Ausseil, F, Capp, J P, Bieth, A, Long, C, David, B, Shevelev, I, Frierich-Heinecken, E, Hübscher, U, Amalric, F, Massiot, G, Hoffmann, J S, Cazaux, C, University of Zurich, and Cazaux, C

Subjects
3004 Pharmacology, 1313 Molecular Medicine, 570 Life sciences, biology, 10226 Department of Molecular Mechanisms of Disease
Published
2005

25. Incorporation of non-nucleoside triphosphate analogues opposite to an abasic site by human DNA polymerases beta and lambda

Author

Crespan, E, Zanoli, S, Khandazhinskaya, A, Shevelev, I, Jasko, M, Alexandrova, L, Kukhanova, M, Blanca, G, Villani, G, Hübscher, U, Spadari, S, Maga, G, Institut de pharmacologie et de biologie structurale (IPBS), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, University of Zurich, and Maga, G

Subjects
1311 Genetics, 570 Life sciences, biology, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, 10226 Department of Molecular Mechanisms of Disease
Published
2005

26. Diketo hexenoic acid (DKHA) derivatives are novel selective non nucleoside inhibitors of mammalian terminal deoxynucleotidyl transferases, with potent cytotoxic effect against leukemic cells

Author

G.A., Locatelli, Santo R., Di, Crespan, E., Costi, R., Roux, A., Hübscher, U., Shevelev, I., Blanca, G., Villani, G., Spadari, S., Maga, G., Institut de pharmacologie et de biologie structurale (IPBS), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), and Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées

Subjects
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [SDV.CAN]Life Sciences [q-bio]/Cancer
Published
2005

29. The 3' 5' exonucleases

Author

Shevelev, I V, Hübscher, U, and University of Zurich

Subjects
1307 Cell Biology, 1312 Molecular Biology, 570 Life sciences, biology, 10226 Department of Molecular Mechanisms of Disease
Published
2002

32. Anti-HIV-1 activity in vitro of ceftazidime degradation products

Author

Hobi, R, Hübscher, U, Neftel, K, Alteri, E, Poncioni, B, Walker, M R, Woods-Cook, K, Schneider, P, Lazdins, J K, University of Zurich, and Hobi, R

Subjects
3004 Pharmacology, 3002 Drug Discovery, 2406 Virology, 570 Life sciences, biology, 10226 Department of Molecular Mechanisms of Disease
Published
2001

33. Potentiation of inhibition of wild-type and mutant human immunodeficiency virus type 1 reverse transcriptases by combinations of nonnucleoside inhibitors and d- and L-(beta)-dideoxynucleoside triphosphate analogs

Author

Maga, G, Hübscher, U, Pregnolato, M, Ubiali, D, Gosselin, G, Spadari, S, University of Zurich, and Maga, G

Subjects
3004 Pharmacology, 570 Life sciences, biology, 2736 Pharmacology (medical), 2725 Infectious Diseases, 10226 Department of Molecular Mechanisms of Disease
Published
2001
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34. Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA replication through a conserved p21(Cip1)-like PCNA-binding motif present in the third subunit of human DNA polymerase delta

Author

Ducoux, M, Urbach, S, Baldacci, G, Hübscher, U, Koundrioukoff, S, Christensen, J, Hughes, P, University of Zurich, and Hughes, P

Subjects
1307 Cell Biology, 1303 Biochemistry, 1312 Molecular Biology, 570 Life sciences, biology, 10226 Department of Molecular Mechanisms of Disease
Published
2001
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36. Eukaryotic DNA polymerases, a growing family

Author

Hübscher, U, Nasheuer, H P, Syväoja, J E, and University of Zurich

Subjects
1303 Biochemistry, 1312 Molecular Biology, 570 Life sciences, biology, 10226 Department of Molecular Mechanisms of Disease
Published
2000

40. A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures

Author

Georlette, D, Jónsson, Z O, Van Petegem, F, Chessa, J, Van Beeumen, J, Hübscher, U, Gerday, C, University of Zurich, and Gerday, C

Subjects
1303 Biochemistry, 570 Life sciences, biology, 10226 Department of Molecular Mechanisms of Disease
Abstract

The cloning, overexpression and characterization of a cold-adapted DNA ligase from the Antarctic sea water bacterium Pseudoalteromonas haloplanktis are described. Protein sequence analysis revealed that the cold-adapted Ph DNA ligase shows a significant level of sequence similarity to other NAD+-dependent DNA ligases and contains several previously described sequence motifs. Also, a decreased level of arginine and proline residues in Ph DNA ligase could be involved in the cold-adaptation strategy. Moreover, 3D modelling of the N-terminal domain of Ph DNA ligase clearly indicates that this domain is destabilized compared with its thermophilic homologue. The recombinant Ph DNA ligase was overexpressed in Escherichia coli and purified to homogeneity. Mass spectroscopy experiments indicated that the purified enzyme is mainly in an adenylated form with a molecular mass of 74593Da. Ph DNA ligase shows similar overall catalytic properties to other NAD+-dependent DNA ligases but is a cold-adapted enzyme as its catalytic efficiency (kcat/Km) at low and moderate temperatures is higher than that of its mesophilic counterpart E.coli DNA ligase. A kinetic comparison of three enzymes adapted to different temperatures (P.haloplanktis, E.coli and Thermus scotoductus DNA ligases) indicated that an increased kcat is the most important adaptive parameter for enzymatic activity at low temperatures, whereas a decreased Km for the nicked DNA substrate seems to allow T.scotoductus DNA ligase to work efficiently at high temperatures. Besides being useful for investigation of the adaptation of enzymes to extreme temperatures, P.haloplanktis DNA ligase, which is very efficient at low temperatures, offers a novel tool for biotechnology.

Published
2000
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42. DNA Replication Fork Proteins

Author

Vengrova, S, Dalgaard, J Z, Vengrova, S ( S ), Dalgaard, J Z ( J Z ), Hübscher, U, Vengrova, S, Dalgaard, J Z, Vengrova, S ( S ), Dalgaard, J Z ( J Z ), and Hübscher, U

Abstract

Since the discovery of DNA structure and throughout the ensuing "DNA era," the field of DNA replication has expanded to cover a vast number of experimental systems. In DNA Replication: Methods and Protocols, expert researchers present a collection of techniques and approaches used to investigate DNA replication with an emphasis on the most recent technological developments. Beginning with several informative introductory review chapters, this extensive volume is organized for clarity while fully encouraging innovation by the mixing of methods to create new techniques. Written in the highly successful Methods in Molecular Biology™ series format, chapters contain brief introductions to the topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and notes on troubleshooting and avoiding known pitfalls. Comprehensive and cutting-edge, DNA Replication: Methods and Protocols provides an excellent tool for both established laboratories and individuals new to this exciting field of research.

Published
2009

43. The Bloom's syndrome helicase (BLM) interacts physically and functionally with p12, the smallest subunit of human DNA polymerase delta

Author

Selak, N, Bachrati, C Z, Shevelev, I, Dietschy, T, van Loon, B, Jacob, A, Hübscher, U, Hoheisel, J D, Hickson, I D, Stagljar, I, Selak, N, Bachrati, C Z, Shevelev, I, Dietschy, T, van Loon, B, Jacob, A, Hübscher, U, Hoheisel, J D, Hickson, I D, and Stagljar, I

Abstract

Bloom's syndrome (BS) is a cancer predisposition disorder caused by mutation of the BLM gene, encoding a member of the RecQ helicase family. Although the phenotype of BS cells is suggestive of a role for BLM in repair of stalled or damaged replication forks, thus far there has been no direct evidence that BLM associates with any of the three human replicative DNA polymerases. Here, we show that BLM interacts specifically in vitro and in vivo with p12, the smallest subunit of human POL {delta} (hPOL {delta}). The hPOL {delta} enzyme, as well as the isolated p12 subunit, stimulates the DNA helicase activity of BLM. Conversely, BLM stimulates hPOL {delta} strand displacement activity. Our results provide the first functional link between BLM and the replicative machinery in human cells, and suggest that BLM might be recruited to sites of disrupted replication through an interaction with hPOL {delta}. Finally, our data also define a novel role for the poorly characterized p12 subunit of hPOL {delta}.

Published
2008

44. Mammalian base excision repair by DNA polymerases delta and epsilon

Author

Stucki, M, Pascucci, B, Parlanti, E, Fortini, P, Wilson, S H, Hübscher, U, Dogliotti, E, University of Zurich, and Dogliotti, E

Subjects
1311 Genetics, 1312 Molecular Biology, 570 Life sciences, biology, 1306 Cancer Research, 10226 Department of Molecular Mechanisms of Disease
Published
1998

46. Newly synthesized L-enantiomers of 3'-fluoro-modified beta-2'-deoxyribonucleoside 5'-triphosphates inhibit hepatitis B DNA polymerases but not the five cellular DNA polymerases alpha, beta, gamma, delta, and epsilon nor HIV-1 reverse transcriptase

Author

von Janta-Lipinski, M, Costisella, B, Ochs, H, Hübscher, U, Hafkemeyer, P, Matthes, E, University of Zurich, and von Janta-Lipinski, M

Subjects
1313 Molecular Medicine, 3002 Drug Discovery, 570 Life sciences, biology, 10226 Department of Molecular Mechanisms of Disease
Published
1998

50. Error-free bypass of 2-hydroxyadenine by human DNA polymerase lambda with Proliferating Cell Nuclear Antigen and Replication Protein A in different sequence contexts

Author

Crespan, E, Hübscher, U, Maga, G, Crespan, E, Hübscher, U, and Maga, G

Abstract

1,2-dihydro-2-oxoadenine (2-OH-A), a common DNA lesion produced by reactive oxygen species, is a strong replicative block for several DNA polymerases (DNA pols). We have previously shown that various bases can be misincorporated opposite the 2-OH-A lesion and the type of mispairs varies with either the sequence context or the type of DNA pol tested. Here, we have analysed the ability of the human pol family X member DNA pol lambda, to bypass the 2-OH-A lesion. DNA pol lambda can perform error-free bypass of 2-OH-A when this lesion is located in a random sequence, whereas in a repeated sequence context, even though bypass was also largely error-free, misincorporation of dGMP could be observed. The fidelity of translesion synthesis of 2-OH-A in a repeated sequence by DNA pol lambda was enhanced by the auxiliary proteins Proliferating Cell Nuclear Antigen (PCNA) and Replication Protein A (RP-A). We also found that the DNA pol lambda active site residue tyrosine 505 determined the nucleotide selectivity opposite 2-OH-A. Our data show, for the first time, that the 2-OH-A lesion can be efficiently and faithfully bypassed by a human DNA pol lambda in combination with PCNA and RP-A.

Published
2007

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