نتایج جستجو برای: ژن parc

تعداد نتایج: 18098  

2012
Susana Ochoa Judith Usall Jesús Cobo Javier Labad Jayashri Kulkarni

1Research and Development Unit of Parc Sanitari Sant Joan de Déu/CIBERSAM, 08330 Sant Boi de Llobregat, Spain 2Grup de Treball i Recerca en Dona i Salut Mental (GTRDSM), Catalonia, Spain 3 Salut Mental Parc Tauĺı, Fundació Parc Tauĺı Institut Universitari UAB, Corporació Sanitària Parc Tauĺı, 08208 Sabadell, Spain 4 IISPV, Hospital Psiquiàtric Universitari Institut de Psiquiatria Pere Mata/Univ...

2008
Zaher Nahlé Michael Hsieh Terri Pietka Chris T. Coburn Paul A. Grimaldi Michael Q. Zhang Nada A. Abumrad

Zaher Nahlé, Michael Hsieh, Terri Pietka, Chris T. Coburn, Paul A. Grimaldi, Michael Q. Zhang , Debopriya Das**, and Nada A. Abumrad From the Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, the Department of Biology, Western Carolina University, Cullowhee, North Carolina 28723, Inserm U636, Université de Nice-Sophia Antipolis, Centre de Biochimie, Pa...

Journal: :Cell 2003
Anatoly Y. Nikolaev Muyang Li Norbert Puskas Jun Qin Wei Gu

Nuclear localization of p53 is essential for its tumor suppressor function. Here, we have identified Parc, a Parkin-like ubiquitin ligase, as a cytoplasmic anchor protein in p53-associated protein complexes. Parc directly interacts and forms a approximately 1 MDa complex with p53 in the cytoplasm of unstressed cells. In the absence of stress, inactivation of Parc induces nuclear localization of...

Journal: :Cell 2003

Journal: :Ecological Informatics 2013
Edwige Bellier Philipp Neubauer Pascal Monestiez Yves Letourneur Laurence Ledireach Patrick Bonhomme Frédéric Bachet

a INRA, UR 546 Biostatistics and Spatial Processes, (BioSP), F-84914 Avignon, France b Mediterranean Institute of Oceanology, University of Aix-Marseille II, Parc Scientifique et Technologique de Luminy, Case 901, 13288 Marseille Cedex 9, France c Institute of Marine and Coastal Sciences, Rutgers University, 71 Dudley Rd, New Brunswick, NJ, USA d Université de la Nouvelle-Calédonie, Laboratoire...

Journal: :PLoS ONE 2007
Ivan Laponogov Dennis A. Veselkov Maninder K. Sohi Xiao-Su Pan Aniruddha Achari Cheng Yang Joseph D. Ferrara L. Mark Fisher Mark R. Sanderson

The 2.7 A crystal structure of the 55-kDa N-terminal breakage-reunion domain of topoisomerase (topo) IV subunit A (ParC) from Streptococcus pneumoniae, the first for the quinolone targets from a gram-positive bacterium, has been solved and reveals a 'closed' dimer similar in fold to Escherichia coli DNA gyrase subunit A (GyrA), but distinct from the 'open' gate structure of Escherichia coli Par...

Background: Emergence Klebsiella pneumoniae resistant to quinolone antibiotics due to mutations in gyrA and parC genes created problem for treatment of patients in different hospitals in Iran. The objective of this study was to determine the amino acid substitutions of GyrA and ParC proteins in certain clonal lineages of the K. pneumoniae conferring high level quinolone resistance. Methods: One...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1998
R B Jensen R Lurz K Gerdes

Prokaryotic chromosomes and plasmids encode partitioning systems that are required for DNA segregation at cell division. The systems are thought to be functionally analogous to eukaryotic centromeres and to play a general role in DNA segregation. The parA system of plasmid R1 encodes two proteins ParM and ParR, and a cis-acting centromere-like site denoted parC. The ParR protein binds to parC i...

2002
Yuan Qi Jimin Pei Nick V. Grishin

Two different type II topoisomerases are known in bacteria. DNA gyrase (Gyr) introduces negative supercoils into DNA. Topoisomerase IV (Par) relaxes DNA supercoils. GyrA and ParC subunits of bacterial type II topoisomerases are involved in breakage and reunion of DNA. The spatial structure of the C-terminal fragment in GyrA/ ParC is not available. We infer homology between the C-terminal domain...

2008
C. Hoischen M. Bussiek J. Langowski S. Diekmann

The Escherichia coli low-copy-number plasmid R1 contains a segregation machinery composed of parC, ParR and parM. The R1 centromere-like site parC contains two separate sets of repeats. By atomic force microscopy (AFM) we show here that ParR molecules bind to each of the 5-fold repeated iterons separately with the intervening sequence unbound by ParR. The two ParR protein complexes on parC do n...

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