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Article: Caulobacter chromosome segregation is an ordered multistep process

Shebelut, Conrad W / Guberman, Jonathan M / van Teeffelen, Sven / Yakhnina, Anastasiya A / Gitai, Zemer

Proceedings of the National Academy of Sciences of the United States of America. 2010 Aug. 10, v. 107, no. 32

2010

Abstract: Despite its fundamental nature, bacterial chromosome segregation remains poorly understood. Viewing segregation as a single process caused multiple proposed mechanisms to appear in conflict and failed to explain how asymmetrically dividing bacteria break ...

Abstract	Despite its fundamental nature, bacterial chromosome segregation remains poorly understood. Viewing segregation as a single process caused multiple proposed mechanisms to appear in conflict and failed to explain how asymmetrically dividing bacteria break symmetry to move only one of their chromosomes. Here, we demonstrate that the ParA ATPase extends from one cell pole and pulls the chromosome by retracting upon association with the ParB DNA-binding protein. Surprisingly, ParA disruption has a specific effect on chromosome segregation that only perturbs the latter stages of this process. Using quantitative high-resolution imaging, we demonstrate that this specificity results from the multistep nature of chromosome translocation. We propose that Caulobacter chromosome segregation follows an ordered pathway of events with distinct functions and mechanisms. Initiation releases polar tethering of the origin of replication, distinction spatially differentiates the two chromosomes, and commitment irreversibly translocates the distal centromeric locus. Thus, much as eukaryotic mitosis involves a sequence of distinct subprocesses, Caulobacter cells also segregate their chromosomes through an orchestrated series of steps. We discuss how the multistep view of bacterial chromosome segregation can help to explain and reconcile outstanding puzzles and frame future investigation.
Keywords	Caulobacter ; DNA-binding proteins ; adenosinetriphosphatase ; bacteria ; chromosome segregation ; chromosome translocation ; image analysis ; loci ; mitosis ; replication origin
Language	English
Dates of publication	2010-0810
Size	p. 14194-14198.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1005274107
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Caulobacter chromosome segregation is an ordered multistep process.

Shebelut, Conrad W / Guberman, Jonathan M / van Teeffelen, Sven / Yakhnina, Anastasiya A / Gitai, Zemer

Proceedings of the National Academy of Sciences of the United States of America

2010 Volume 107, Issue 32, Page(s) 14194–14198

Abstract	Despite its fundamental nature, bacterial chromosome segregation remains poorly understood. Viewing segregation as a single process caused multiple proposed mechanisms to appear in conflict and failed to explain how asymmetrically dividing bacteria break symmetry to move only one of their chromosomes. Here, we demonstrate that the ParA ATPase extends from one cell pole and pulls the chromosome by retracting upon association with the ParB DNA-binding protein. Surprisingly, ParA disruption has a specific effect on chromosome segregation that only perturbs the latter stages of this process. Using quantitative high-resolution imaging, we demonstrate that this specificity results from the multistep nature of chromosome translocation. We propose that Caulobacter chromosome segregation follows an ordered pathway of events with distinct functions and mechanisms. Initiation releases polar tethering of the origin of replication, distinction spatially differentiates the two chromosomes, and commitment irreversibly translocates the distal centromeric locus. Thus, much as eukaryotic mitosis involves a sequence of distinct subprocesses, Caulobacter cells also segregate their chromosomes through an orchestrated series of steps. We discuss how the multistep view of bacterial chromosome segregation can help to explain and reconcile outstanding puzzles and frame future investigation.
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Adenosine Triphosphatases/physiology ; Bacterial Proteins ; Caulobacter/genetics ; Chromosome Segregation ; Chromosomes, Bacterial ; DNA-Binding Proteins/metabolism ; DNA-Binding Proteins/physiology
Chemical Substances	Bacterial Proteins ; DNA-Binding Proteins ; Adenosine Triphosphatases (EC 3.6.1.-)
Language	English
Publishing date	2010-07-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1005274107
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Article: Quantitative genome-scale analysis of protein localization in an asymmetric bacterium

Werner, John N / Chen, Eric Y / Guberman, Jonathan M / Zippilli, Angela R / Irgon, Joseph J / Gitai, Zemer

Proceedings of the National Academy of Sciences of the United States of America. 2009 May 12, v. 106, no. 19

2009

Abstract: Despite the importance of subcellular localization for cellular activities, the lack of high-throughput, high-resolution imaging and quantitation methodologies has limited genomic localization analysis to a small number of archival studies focused on C- ... ...

Abstract	Despite the importance of subcellular localization for cellular activities, the lack of high-throughput, high-resolution imaging and quantitation methodologies has limited genomic localization analysis to a small number of archival studies focused on C-terminal fluorescent protein fusions. Here, we develop a high-throughput pipeline for generating, imaging, and quantitating fluorescent protein fusions that we use for the quantitative genomic assessment of the distributions of both N- and C-terminal fluorescent protein fusions. We identify nearly 300 localized Caulobacter crescentus proteins, up to 10-fold more than were previously characterized. The localized proteins tend to be involved in spatially or temporally dynamic processes and proteins that function together and often localize together as well. The distributions of the localized proteins were quantitated by using our recently described projected system of internal coordinates from interpolated contours (PSICIC) image analysis toolkit, leading to the identification of cellular regions that are over- or under-enriched in localized proteins and of potential differences in the mechanisms that target proteins to different subcellular destinations. The Caulobacter localizome data thus represent a resource for studying both global properties of protein localization and specific protein functions, whereas the localization analysis pipeline is a methodological resource that can be readily applied to other systems.
Keywords	Caulobacter crescentus ; bacteria ; fluorescent proteins ; image analysis
Language	English
Dates of publication	2009-0512
Size	p. 7858-7863.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0901781106
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: PSICIC: noise and asymmetry in bacterial division revealed by computational image analysis at sub-pixel resolution.

Guberman, Jonathan M / Fay, Allison / Dworkin, Jonathan / Wingreen, Ned S / Gitai, Zemer

PLoS computational biology

2008 Volume 4, Issue 11, Page(s) e1000233

Abstract: Live-cell imaging by light microscopy has demonstrated that all cells are spatially and temporally organized. Quantitative, computational image analysis is an important part of cellular imaging, providing both enriched information about individual cell ... ...

Abstract	Live-cell imaging by light microscopy has demonstrated that all cells are spatially and temporally organized. Quantitative, computational image analysis is an important part of cellular imaging, providing both enriched information about individual cell properties and the ability to analyze large datasets. However, such studies are often limited by the small size and variable shape of objects of interest. Here, we address two outstanding problems in bacterial cell division by developing a generally applicable, standardized, and modular software suite termed Projected System of Internal Coordinates from Interpolated Contours (PSICIC) that solves common problems in image quantitation. PSICIC implements interpolated-contour analysis for accurate and precise determination of cell borders and automatically generates internal coordinate systems that are superimposable regardless of cell geometry. We have used PSICIC to establish that the cell-fate determinant, SpoIIE, is asymmetrically localized during Bacillus subtilis sporulation, thereby demonstrating the ability of PSICIC to discern protein localization features at sub-pixel scales. We also used PSICIC to examine the accuracy of cell division in Esherichia coli and found a new role for the Min system in regulating division-site placement throughout the cell length, but only prior to the initiation of cell constriction. These results extend our understanding of the regulation of both asymmetry and accuracy in bacterial division while demonstrating the general applicability of PSICIC as a computational approach for quantitative, high-throughput analysis of cellular images.
MeSH term(s)	Algorithms ; Bacillus subtilis/cytology ; Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Bacteria/cytology ; Bacteria/metabolism ; Cell Division ; Escherichia coli/cytology ; Image Processing, Computer-Assisted/methods ; Microscopy/methods ; Molecular Sequence Data ; Software
Language	English
Publishing date	2008-11-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2193340-6
ISSN	1553-7358 ; 1553-734X
ISSN (online)	1553-7358
ISSN	1553-734X
DOI	10.1371/journal.pcbi.1000233
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: BioMart: a data federation framework for large collaborative projects.

Zhang, Junjun / Haider, Syed / Baran, Joachim / Cros, Anthony / Guberman, Jonathan M / Hsu, Jack / Liang, Yong / Yao, Long / Kasprzyk, Arek

Database : the journal of biological databases and curation

2011 Volume 2011, Page(s) bar038

Abstract: BioMart is a freely available, open source, federated database system that provides a unified access to disparate, geographically distributed data sources. It is designed to be data agnostic and platform independent, such that existing databases can ... ...

Abstract	BioMart is a freely available, open source, federated database system that provides a unified access to disparate, geographically distributed data sources. It is designed to be data agnostic and platform independent, such that existing databases can easily be incorporated into the BioMart framework. BioMart allows databases hosted on different servers to be presented seamlessly to users, facilitating collaborative projects between different research groups. BioMart contains several levels of query optimization to efficiently manage large data sets and offers a diverse selection of graphical user interfaces and application programming interfaces to ensure that queries can be performed in whatever manner is most convenient for the user. The software has now been adopted by a large number of different biological databases spanning a wide range of data types and providing a rich source of annotation available to bioinformaticians and biologists alike.
MeSH term(s)	Computational Biology ; Cooperative Behavior ; Database Management Systems ; Databases, Factual ; International Cooperation ; Internet ; User-Computer Interface
Language	English
Publishing date	2011-09-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2496706-3
ISSN	1758-0463 ; 1758-0463
ISSN (online)	1758-0463
ISSN	1758-0463
DOI	10.1093/database/bar038
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Article ; Online: A distance-weighted interaction map reveals a previously uncharacterized layer of the Bacillus subtilis spore coat.

McKenney, Peter T / Driks, Adam / Eskandarian, Haig A / Grabowski, Paul / Guberman, Jonathan / Wang, Katherine H / Gitai, Zemer / Eichenberger, Patrick

Current biology : CB

2010 Volume 20, Issue 10, Page(s) 934–938

Abstract: Bacillus subtilis spores are encased in a protein assembly called the spore coat that is made up of at least 70 different proteins. Conventional electron microscopy shows the coat to be organized into two distinct layers. Because the coat is about as ... ...

Abstract	Bacillus subtilis spores are encased in a protein assembly called the spore coat that is made up of at least 70 different proteins. Conventional electron microscopy shows the coat to be organized into two distinct layers. Because the coat is about as wide as the theoretical limit of light microscopy, quantitatively measuring the localization of individual coat proteins within the coat is challenging. We used fusions of coat proteins to green fluorescent protein to map genetic dependencies for coat assembly and to define three independent subnetworks of coat proteins. To complement the genetic data, we measured coat protein localization at subpixel resolution and integrated these two data sets to produce a distance-weighted genetic interaction map. Using these data, we predict that the coat comprises at least four spatially distinct layers, including a previously uncharacterized glycoprotein outermost layer that we name the spore crust. We found that crust assembly depends on proteins we predicted to localize to the crust. The crust may be conserved in all Bacillus spores and may play critical functions in the environment.
MeSH term(s)	Bacillus subtilis/chemistry ; Bacillus subtilis/metabolism ; Bacillus subtilis/ultrastructure ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Gene Regulatory Networks ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Spores, Bacterial/chemistry ; Spores, Bacterial/ultrastructure
Chemical Substances	Bacterial Proteins ; Recombinant Fusion Proteins
Language	English
Publishing date	2010-05-06
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2010.03.060
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Quantitative genome-scale analysis of protein localization in an asymmetric bacterium.

Werner, John N / Chen, Eric Y / Guberman, Jonathan M / Zippilli, Angela R / Irgon, Joseph J / Gitai, Zemer

Proceedings of the National Academy of Sciences of the United States of America

2009 Volume 106, Issue 19, Page(s) 7858–7863

Abstract	Despite the importance of subcellular localization for cellular activities, the lack of high-throughput, high-resolution imaging and quantitation methodologies has limited genomic localization analysis to a small number of archival studies focused on C-terminal fluorescent protein fusions. Here, we develop a high-throughput pipeline for generating, imaging, and quantitating fluorescent protein fusions that we use for the quantitative genomic assessment of the distributions of both N- and C-terminal fluorescent protein fusions. We identify nearly 300 localized Caulobacter crescentus proteins, up to 10-fold more than were previously characterized. The localized proteins tend to be involved in spatially or temporally dynamic processes and proteins that function together and often localize together as well. The distributions of the localized proteins were quantitated by using our recently described projected system of internal coordinates from interpolated contours (PSICIC) image analysis toolkit, leading to the identification of cellular regions that are over- or under-enriched in localized proteins and of potential differences in the mechanisms that target proteins to different subcellular destinations. The Caulobacter localizome data thus represent a resource for studying both global properties of protein localization and specific protein functions, whereas the localization analysis pipeline is a methodological resource that can be readily applied to other systems.
MeSH term(s)	Bacterial Proteins/genetics ; Caulobacter crescentus/metabolism ; Computational Biology/methods ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Genome, Bacterial ; Genomics/methods ; Image Processing, Computer-Assisted ; Luminescent Proteins/chemistry ; Open Reading Frames ; Protein Structure, Tertiary
Chemical Substances	Bacterial Proteins ; Luminescent Proteins
Language	English
Publishing date	2009-04-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0901781106
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: International Cancer Genome Consortium Data Portal--a one-stop shop for cancer genomics data.

Zhang, Junjun / Baran, Joachim / Cros, A / Guberman, Jonathan M / Haider, Syed / Hsu, Jack / Liang, Yong / Rivkin, Elena / Wang, Jianxin / Whitty, Brett / Wong-Erasmus, Marie / Yao, Long / Kasprzyk, Arek

Database : the journal of biological databases and curation

2011 Volume 2011, Page(s) bar026

Abstract: The International Cancer Genome Consortium (ICGC) is a collaborative effort to characterize genomic abnormalities in 50 different cancer types. To make this data available, the ICGC has created the ICGC Data Portal. Powered by the BioMart software, the ... ...

Abstract	The International Cancer Genome Consortium (ICGC) is a collaborative effort to characterize genomic abnormalities in 50 different cancer types. To make this data available, the ICGC has created the ICGC Data Portal. Powered by the BioMart software, the Data Portal allows each ICGC member institution to manage and maintain its own databases locally, while seamlessly presenting all the data in a single access point for users. The Data Portal currently contains data from 24 cancer projects, including ICGC, The Cancer Genome Atlas (TCGA), Johns Hopkins University, and the Tumor Sequencing Project. It consists of 3478 genomes and 13 cancer types and subtypes. Available open access data types include simple somatic mutations, copy number alterations, structural rearrangements, gene expression, microRNAs, DNA methylation and exon junctions. Additionally, simple germline variations are available as controlled access data. The Data Portal uses a web-based graphical user interface (GUI) to offer researchers multiple ways to quickly and easily search and analyze the available data. The web interface can assist in constructing complicated queries across multiple data sets. Several application programming interfaces are also available for programmatic access. Here we describe the organization, functionality, and capabilities of the ICGC Data Portal.
MeSH term(s)	Database Management Systems ; Databases, Factual ; Gene Expression Profiling ; Genetic Variation ; Genomics ; Humans ; International Cooperation ; Internet ; Neoplasms/genetics ; Societies ; User-Computer Interface
Language	English
Publishing date	2011-09-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2496706-3
ISSN	1758-0463 ; 1758-0463
ISSN (online)	1758-0463
ISSN	1758-0463
DOI	10.1093/database/bar026
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: BioMart Central Portal: an open database network for the biological community.

Guberman, Jonathan M / Ai, J / Arnaiz, O / Baran, Joachim / Blake, Andrew / Baldock, Richard / Chelala, Claude / Croft, David / Cros, Anthony / Cutts, Rosalind J / Di Génova, A / Forbes, Simon / Fujisawa, T / Gadaleta, E / Goodstein, D M / Gundem, Gunes / Haggarty, Bernard / Haider, Syed / Hall, Matthew /

Harris, Todd / Haw, Robin / Hu, S / Hubbard, Simon / Hsu, Jack / Iyer, Vivek / Jones, Philip / Katayama, Toshiaki / Kinsella, R / Kong, Lei / Lawson, Daniel / Liang, Yong / Lopez-Bigas, Nuria / Luo, J / Lush, Michael / Mason, Jeremy / Moreews, Francois / Ndegwa, Nelson / Oakley, Darren / Perez-Llamas, Christian / Primig, Michael / Rivkin, Elena / Rosanoff, S / Shepherd, Rebecca / Simon, Reinhard / Skarnes, B / Smedley, Damian / Sperling, Linda / Spooner, William / Stevenson, Peter / Stone, Kevin / Teague, J / Wang, Jun / Wang, Jianxin / Whitty, Brett / Wong, D T / Wong-Erasmus, Marie / Yao, L / Youens-Clark, Ken / Yung, Christina / Zhang, Junjun / Kasprzyk, Arek

Database : the journal of biological databases and curation

2011 Volume 2011, Page(s) bar041

Abstract: BioMart Central Portal is a first of its kind, community-driven effort to provide unified access to dozens of biological databases spanning genomics, proteomics, model organisms, cancer data, ontology information and more. Anybody can contribute an ... ...

Abstract	BioMart Central Portal is a first of its kind, community-driven effort to provide unified access to dozens of biological databases spanning genomics, proteomics, model organisms, cancer data, ontology information and more. Anybody can contribute an independently maintained resource to the Central Portal, allowing it to be exposed to and shared with the research community, and linking it with the other resources in the portal. Users can take advantage of the common interface to quickly utilize different sources without learning a new system for each. The system also simplifies cross-database searches that might otherwise require several complicated steps. Several integrated tools streamline common tasks, such as converting between ID formats and retrieving sequences. The combination of a wide variety of databases, an easy-to-use interface, robust programmatic access and the array of tools make Central Portal a one-stop shop for biological data querying. Here, we describe the structure of Central Portal and show example queries to demonstrate its capabilities.
MeSH term(s)	Animals ; Bacteria ; Biomedical Research ; Database Management Systems ; Databases, Factual ; Fungi ; Genome ; Humans ; International Cooperation ; Internet ; User-Computer Interface ; Viruses
Language	English
Publishing date	2011-09-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2496706-3
ISSN	1758-0463 ; 1758-0463
ISSN (online)	1758-0463
ISSN	1758-0463
DOI	10.1093/database/bar041
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: International network of cancer genome projects.

Hudson, Thomas J / Anderson, Warwick / Artez, Axel / Barker, Anna D / Bell, Cindy / Bernabé, Rosa R / Bhan, M K / Calvo, Fabien / Eerola, Iiro / Gerhard, Daniela S / Guttmacher, Alan / Guyer, Mark / Hemsley, Fiona M / Jennings, Jennifer L / Kerr, David / Klatt, Peter / Kolar, Patrik / Kusada, Jun / Lane, David P /

Laplace, Frank / Youyong, Lu / Nettekoven, Gerd / Ozenberger, Brad / Peterson, Jane / Rao, T S / Remacle, Jacques / Schafer, Alan J / Shibata, Tatsuhiro / Stratton, Michael R / Vockley, Joseph G / Watanabe, Koichi / Yang, Huanming / Yuen, Matthew M F / Knoppers, Bartha M / Bobrow, Martin / Cambon-Thomsen, Anne / Dressler, Lynn G / Dyke, Stephanie O M / Joly, Yann / Kato, Kazuto / Kennedy, Karen L / Nicolás, Pilar / Parker, Michael J / Rial-Sebbag, Emmanuelle / Romeo-Casabona, Carlos M / Shaw, Kenna M / Wallace, Susan / Wiesner, Georgia L / Zeps, Nikolajs / Lichter, Peter / Biankin, Andrew V / Chabannon, Christian / Chin, Lynda / Clément, Bruno / de Alava, Enrique / Degos, Françoise / Ferguson, Martin L / Geary, Peter / Hayes, D Neil / Johns, Amber L / Kasprzyk, Arek / Nakagawa, Hidewaki / Penny, Robert / Piris, Miguel A / Sarin, Rajiv / Scarpa, Aldo / van de Vijver, Marc / Futreal, P Andrew / Aburatani, Hiroyuki / Bayés, Mónica / Botwell, David D L / Campbell, Peter J / Estivill, Xavier / Grimmond, Sean M / Gut, Ivo / Hirst, Martin / López-Otín, Carlos / Majumder, Partha / Marra, Marco / McPherson, John D / Ning, Zemin / Puente, Xose S / Ruan, Yijun / Stunnenberg, Hendrik G / Swerdlow, Harold / Velculescu, Victor E / Wilson, Richard K / Xue, Hong H / Yang, Liu / Spellman, Paul T / Bader, Gary D / Boutros, Paul C / Flicek, Paul / Getz, Gad / Guigó, Roderic / Guo, Guangwu / Haussler, David / Heath, Simon / Hubbard, Tim J / Jiang, Tao / Jones, Steven M / Li, Qibin / López-Bigas, Nuria / Luo, Ruibang / Muthuswamy, Lakshmi / Ouellette, B F Francis / Pearson, John V / Quesada, Victor / Raphael, Benjamin J / Sander, Chris / Speed, Terence P / Stein, Lincoln D / Stuart, Joshua M / Teague, Jon W / Totoki, Yasushi / Tsunoda, Tatsuhiko / Valencia, Alfonso / Wheeler, David A / Wu, Honglong / Zhao, Shancen / Zhou, Guangyu / Lathrop, Mark / Thomas, Gilles / Yoshida, Teruhiko / Axton, Myles / Gunter, Chris / Miller, Linda J / Zhang, Junjun / Haider, Syed A / Wang, Jianxin / Yung, Christina K / Cros, Anthony / Cross, Anthony / Liang, Yong / Gnaneshan, Saravanamuttu / Guberman, Jonathan / Hsu, Jack / Chalmers, Don R C / Hasel, Karl W / Kaan, Terry S H / Lowrance, William W / Masui, Tohru / Rodriguez, Laura Lyman / Vergely, Catherine / Bowtell, David D L / Cloonan, Nicole / deFazio, Anna / Eshleman, James R / Etemadmoghadam, Dariush / Gardiner, Brooke B / Gardiner, Brooke A / Kench, James G / Sutherland, Robert L / Tempero, Margaret A / Waddell, Nicola J / Wilson, Peter J / Gallinger, Steve / Tsao, Ming-Sound / Shaw, Patricia A / Petersen, Gloria M / Mukhopadhyay, Debabrata / DePinho, Ronald A / Thayer, Sarah / Shazand, Kamran / Beck, Timothy / Sam, Michelle / Timms, Lee / Ballin, Vanessa / Lu, Youyong / Ji, Jiafu / Zhang, Xiuqing / Chen, Feng / Hu, Xueda / Yang, Qi / Tian, Geng / Zhang, Lianhai / Xing, Xiaofang / Li, Xianghong / Zhu, Zhenggang / Yu, Yingyan / Yu, Jun / Tost, Jörg / Brennan, Paul / Holcatova, Ivana / Zaridze, David / Brazma, Alvis / Egevard, Lars / Prokhortchouk, Egor / Banks, Rosamonde Elizabeth / Uhlén, Mathias / Viksna, Juris / Ponten, Fredrik / Skryabin, Konstantin / Birney, Ewan / Borg, Ake / Børresen-Dale, Anne-Lise / Caldas, Carlos / Foekens, John A / Martin, Sancha / Reis-Filho, Jorge S / Richardson, Andrea L / Sotiriou, Christos / Thoms, Giles / van't Veer, Laura / Birnbaum, Daniel / Blanche, Hélène / Boucher, Pascal / Boyault, Sandrine / Masson-Jacquemier, Jocelyne D / Pauporté, Iris / Pivot, Xavier / Vincent-Salomon, Anne / Tabone, Eric / Theillet, Charles / Treilleux, Isabelle / Bioulac-Sage, Paulette / Decaens, Thomas / Franco, Dominique / Gut, Marta / Samuel, Didier / Zucman-Rossi, Jessica / Eils, Roland / Brors, Benedikt / Korbel, Jan O / Korshunov, Andrey / Landgraf, Pablo / Lehrach, Hans / Pfister, Stefan / Radlwimmer, Bernhard / Reifenberger, Guido / Taylor, Michael D / von Kalle, Christof / Majumder, Partha P / Pederzoli, Paolo / Lawlor, Rita A / Delledonne, Massimo / Bardelli, Alberto / Gress, Thomas / Klimstra, David / Zamboni, Giuseppe / Nakamura, Yusuke / Miyano, Satoru / Fujimoto, Akihiro / Campo, Elias / de Sanjosé, Silvia / Montserrat, Emili / González-Díaz, Marcos / Jares, Pedro / Himmelbauer, Heinz / Himmelbaue, Heinz / Bea, Silvia / Aparicio, Samuel / Easton, Douglas F / Collins, Francis S / Compton, Carolyn C / Lander, Eric S / Burke, Wylie / Green, Anthony R / Hamilton, Stanley R / Kallioniemi, Olli P / Ley, Timothy J / Liu, Edison T / Wainwright, Brandon J

Nature

2010 Volume 464, Issue 7291, Page(s) 993–998

Abstract: The International Cancer Genome Consortium (ICGC) was launched to coordinate large-scale cancer genome studies in tumours from 50 different cancer types and/or subtypes that are of clinical and societal importance across the globe. Systematic studies of ... ...

Abstract	The International Cancer Genome Consortium (ICGC) was launched to coordinate large-scale cancer genome studies in tumours from 50 different cancer types and/or subtypes that are of clinical and societal importance across the globe. Systematic studies of more than 25,000 cancer genomes at the genomic, epigenomic and transcriptomic levels will reveal the repertoire of oncogenic mutations, uncover traces of the mutagenic influences, define clinically relevant subtypes for prognosis and therapeutic management, and enable the development of new cancer therapies.
MeSH term(s)	DNA Methylation ; DNA Mutational Analysis/trends ; Databases, Genetic ; Genes, Neoplasm/genetics ; Genetics, Medical/organization & administration ; Genetics, Medical/trends ; Genome, Human/genetics ; Genomics/organization & administration ; Genomics/trends ; Humans ; Intellectual Property ; International Cooperation ; Mutation ; Neoplasms/classification ; Neoplasms/genetics ; Neoplasms/pathology ; Neoplasms/therapy
Language	English
Publishing date	2010-02-24
Publishing country	England
Document type	Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/nature08987
Database	MEDical Literature Analysis and Retrieval System OnLINE

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