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Article: Novel

Kusada, Hiroyuki / Zhang, Yu / Tamaki, Hideyuki / Kimura, Nobutada / Kamagata, Yoichi

2019 Volume 10, Page(s) 455

Abstract: ... ...

Abstract	N
Language	English
Publishing date	2019-03-14
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2019.00455
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Article ; Online: Prediction Error of Intraocular Lens Power Calculation in Very Elderly Patients over 90 Years Old.

Koga, Yusuke / Kojima, Kentaro / Yoshii, Kengo / Kusada, Natsuki / Kagitani, Yu / Aoki, Takanori / Horiuchi, Noriko / Kitazawa, Koji / Sotozono, Chie

Current eye research

2020 Volume 46, Issue 8, Page(s) 1148–1153

Abstract: Background: To investigate the influence of age on prediction error (PE) after cataract surgery in very elderly (VE) patients aged more than 90 years.: Methods: We retrospectively analyzed 66 eyes of patients aged ≥90 years (VE group) who underwent ... ...

Abstract	Background: To investigate the influence of age on prediction error (PE) after cataract surgery in very elderly (VE) patients aged more than 90 years. Methods: We retrospectively analyzed 66 eyes of patients aged ≥90 years (VE group) who underwent phacoemulsification and intraocular lens (IOL) implantation. As the control group (CG), we investigated 121 eyes of patients aged 70-89 years who underwent the same surgery. PE was calculated 1 month post-surgery as the actual postoperative spherical equivalent minus the target diopter, which was calculated using the Sanders-Retzlaff-Kraff/T formula. The absolute and arithmetic PE were compared between the two groups. The factors affecting absolute PE outside ±0.5 diopter (D) and ±1.0 D were determined through logistic regression analysis with the variables age, sex, axial length (AL), average corneal power, preoperative best-corrected visual acuity, target diopter, and coexisting pseudoexfoliation syndrome. Results: The absolute PE was significantly larger in the VE group than that in the CG (0.60 ± 0.52 D and 0.34 ± 0.25 D, respectively; Conclusions: Absolute PE tended to increase in the cataract surgery of VE patients.
MeSH term(s)	Age Factors ; Aged ; Aged, 80 and over ; Axial Length, Eye ; Biometry ; Female ; Humans ; Lens Implantation, Intraocular ; Lenses, Intraocular ; Male ; Optics and Photonics ; Phacoemulsification ; Pseudophakia/physiopathology ; Retrospective Studies ; Visual Acuity/physiology
Language	English
Publishing date	2020-12-26
Publishing country	England
Document type	Comparative Study ; Journal Article
ZDB-ID	82079-9
ISSN	1460-2202 ; 0271-3683
ISSN (online)	1460-2202
ISSN	0271-3683
DOI	10.1080/02713683.2020.1858486
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Article ; Online: Affinity of anti-insulin-like growth factor Ι receptor antibody binding to the receptor altered by plant lectins.

Kusada, Yu / Fujita-Yamaguchi, Yoko

Bioscience trends

2011 Volume 5, Issue 3, Page(s) 93–98

Abstract: The binding ability of anti-insulin-like growth factor Ι receptor (IGF-ΙR) single-chain variable fragments (scFvs) to IGF-IR was measured in the presence of plant lectins. Combinations of concanavalin A (Con A), wheat germ agglutinin (WGA), or peanut ... ...

Abstract	The binding ability of anti-insulin-like growth factor Ι receptor (IGF-ΙR) single-chain variable fragments (scFvs) to IGF-IR was measured in the presence of plant lectins. Combinations of concanavalin A (Con A), wheat germ agglutinin (WGA), or peanut agglutinin (PNA) and 1H7 or 3B7 anti-IGF-ΙR scFv/phage antibodies that were previously produced and characterized were used. WGA inhibited binding of both scFvs proteins to the receptor. PNA slightly enhanced the binding of 1H7 scFv and phage antibody to the receptor. Con A led to enhancement of 3B7 scFv-binding but had no effect in a test of phage antibodies and determination of kinetic parameters. The effect of lectins differed for scFvs and phage antibodies, implying that affinity altered by lectins is dependent upon the molecular structure of the antibodies. Results indicated that animal lectins may affect the affinity of therapeutic antibodies targeting cell membrane receptors in vivo.
MeSH term(s)	Antibodies/immunology ; Antibodies/metabolism ; Concanavalin A/pharmacology ; Enzyme-Linked Immunosorbent Assay ; Humans ; Kinetics ; Peanut Agglutinin/pharmacology ; Plant Lectins/pharmacology ; Protein Binding/drug effects ; Receptor, IGF Type 1/immunology ; Receptor, IGF Type 1/metabolism ; Single-Chain Antibodies/immunology ; Single-Chain Antibodies/metabolism ; Wheat Germ Agglutinins/pharmacology
Chemical Substances	Antibodies ; Peanut Agglutinin ; Plant Lectins ; Single-Chain Antibodies ; Wheat Germ Agglutinins ; Concanavalin A (11028-71-0) ; Receptor, IGF Type 1 (EC 2.7.10.1)
Language	English
Publishing date	2011-07-15
Publishing country	Japan
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2543899-2
ISSN	1881-7823 ; 1881-7815
ISSN (online)	1881-7823
ISSN	1881-7815
DOI	10.5582/bst.2011.v5.3.93
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Article ; Online: An overview of currently available anti-insulin-like growth factor I receptor antibodies.

Kusada, Yu / Fujita-Yamaguchi, Yoko

Bioscience trends

2007 Volume 1, Issue 3, Page(s) 128–133

Abstract: A number of studies during the last two decades revealed that the insulin-like growth factor I receptor (IGFIR) is an attractive target for cancer molecular therapy. Different molecular strategies have been developed and evaluated in experimental systems, ...

Abstract	A number of studies during the last two decades revealed that the insulin-like growth factor I receptor (IGFIR) is an attractive target for cancer molecular therapy. Different molecular strategies have been developed and evaluated in experimental systems, and one such strategy involves anti-IGFIR antibodies, which have been rigorously tested for their therapeutic potential over the last 5-6 years. This mini-review thus introduces currently available IGFIR antibodies with a particular emphasis on epitope mapping and anti-IGFIR antibody-induced cancer growth inhibition.
MeSH term(s)	Animals ; Antibodies/immunology ; Antibodies/therapeutic use ; Epitope Mapping/methods ; Humans ; Models, Biological ; Neoplasms/therapy ; Receptor, IGF Type 1/immunology
Chemical Substances	Antibodies ; Receptor, IGF Type 1 (EC 2.7.10.1)
Language	English
Publishing date	2007-12
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	2543899-2
ISSN	1881-7823 ; 1881-7815
ISSN (online)	1881-7823
ISSN	1881-7815
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Article: Construction and Characterization of Single-chain Antibodies Against Human Insulin-like Growth Factor-I Receptor from Hybridomas Producing 1H7 or 3B7 Monoclonal Antibody

Kusada, Yu / Morizono, Toru / Matsumoto-Takasaki, Ayano / Sakai, Keiko / Sato, Shuma / Asanuma, Hideki / Takayanagi, Atsushi / Fujita-Yamaguchi, Yoko

Journal of biochemistry. 2008 Jan., v. 143, no. 1

2008

Abstract: Recombinant antibody consisting of the single-chain variable fragment (scFv) of 1H7 monoclonal antibody against insulin-like growth factor-I receptor (IGF-IR) and human IgG₁ Fc domain, scFv-Fc, has been found to exhibit inhibitory effects on breast ... ...

Abstract	Recombinant antibody consisting of the single-chain variable fragment (scFv) of 1H7 monoclonal antibody against insulin-like growth factor-I receptor (IGF-IR) and human IgG₁ Fc domain, scFv-Fc, has been found to exhibit inhibitory effects on breast cancer growth in vitro and in vivo [Li et al. (2000) Cancer Immunol. Immunother. 49, 243; Sachdev et al. (2003) Cancer Res. 63, 627]. Various types of scFvs from hybridomas producing 1H7 or 3B7 mAb were constructed using conventional phage display technology to further characterize the specificity and affinity of anti-IGF-IR mAbs. Binding studies performed using either phage antibodies or soluble scFv proteins to IGF-IR or insulin receptor (IR) and IGF-IR pre-incubated with mAbs suggested that (i) 1H7 and 3B7 bind to IGF-IR but do not bind to its structurally related IR, (ii) either the VL-VH or VH-VL sequence order does not apparently affect specificity for IGF-IR and (iii) 1H7 and 3B7 bind the independent epitopes, located in or near the N-terminal (440-514) and C-terminal (62-184) domains of the α subunit, respectively. This study not only revealed new information on binding regions for two anti-IGF-IR mAbs, but also provided the scFv genes as tools for further manipulation of the affinity or development of new IGF-IR-targeted cancer therapeutics.
Language	English
Dates of publication	2008-01
Size	p. 9-19.
Publishing place	Japanese Biochemical Society
Document type	Article
ZDB-ID	218073-x
ISSN	1756-2651 ; 0021-924X
ISSN (online)	1756-2651
ISSN	0021-924X
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Influenza PR8 HA-specific Fab fragments produced by phage display methods.

Asanuma, Hideki / Matsumoto-Takasaki, Ayano / Suzuki, Yujiro / Tamura, Shin-Ichi / Sata, Tetsutaro / Kusada, Yu / Matsushita, Misao / Fujita-Yamaguchi, Yoko

Biochemical and biophysical research communications

2008 Volume 366, Issue 2, Page(s) 445–449

Abstract: Anti-influenza hemagglutinin (HA) Fabs were isolated from a phage display library using purified HA of influenza virus A/Puerto Rico/8/34 (PR8; H1N1) as an antigen. Four Fab clones displaying a 25-50-fold higher binding signal to PR8 HA than the control ... ...

Abstract	Anti-influenza hemagglutinin (HA) Fabs were isolated from a phage display library using purified HA of influenza virus A/Puerto Rico/8/34 (PR8; H1N1) as an antigen. Four Fab clones displaying a 25-50-fold higher binding signal to PR8 HA than the control were selected for further analysis and comparison with anti-PR8 monoclonal antibody (mAb). All four Fabs and mAb recognized the PR8 HA under non-reducing conditions but rarely bound to reduced PR8 HA. Inhibition of influenza virus infection on MDCK cells was observed with Fab1 and mAb in a dose-dependent manner while Fab3 and 4 exhibited only a partial inhibitory effect. Moreover, Fab1 clone and mAb exhibited cross-reactivity with the A/Peking/262/95 (A/Peking; H1N1) strain. The inhibitory effects of mAb on both influenza strains were more potent than Fab1, which is likely attributed to its higher affinity for the antigen. SPR analyses, in fact, revealed that Fab1 and mAb have K(D) of 1.5 x 10(-8) and 3.2 x 10(-9)M, respectively. These results strongly suggest that phage library-derived Fabs can be readily prepared and that such HA-specific Fabs with inhibitory action on influenza infection may be used to treat influenza patients.
MeSH term(s)	Animals ; Hemagglutinins, Viral/immunology ; Hemagglutinins, Viral/isolation & purification ; Immunoglobulin Fab Fragments/immunology ; Immunoglobulin Fab Fragments/isolation & purification ; Influenza A Virus, H1N1 Subtype/immunology ; Mice ; Mice, Inbred BALB C ; Orthomyxoviridae/immunology ; Peptide Library
Chemical Substances	Hemagglutinins, Viral ; Immunoglobulin Fab Fragments ; Peptide Library
Language	English
Publishing date	2008-02-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2007.11.135
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Article: Construction and characterization of single-chain antibodies against human insulin-like growth factor-I receptor from hybridomas producing 1H7 or 3B7 monoclonal antibody.

Kusada, Yu / Morizono, Toru / Matsumoto-Takasaki, Ayano / Sakai, Keiko / Sato, Shuma / Asanuma, Hideki / Takayanagi, Atsushi / Fujita-Yamaguchi, Yoko

Journal of biochemistry

2008 Volume 143, Issue 1, Page(s) 9–19

Abstract: Recombinant antibody consisting of the single-chain variable fragment (scFv) of 1H7 monoclonal antibody against insulin-like growth factor-I receptor (IGF-IR) and human IgG(1) Fc domain, scFv-Fc, has been found to exhibit inhibitory effects on breast ... ...

Abstract	Recombinant antibody consisting of the single-chain variable fragment (scFv) of 1H7 monoclonal antibody against insulin-like growth factor-I receptor (IGF-IR) and human IgG(1) Fc domain, scFv-Fc, has been found to exhibit inhibitory effects on breast cancer growth in vitro and in vivo [Li et al. (2000) Cancer Immunol. Immunother. 49, 243; Sachdev et al. (2003) Cancer Res. 63, 627]. Various types of scFvs from hybridomas producing 1H7 or 3B7 mAb were constructed using conventional phage display technology to further characterize the specificity and affinity of anti-IGF-IR mAbs. Binding studies performed using either phage antibodies or soluble scFv proteins to IGF-IR or insulin receptor (IR) and IGF-IR pre-incubated with mAbs suggested that (i) 1H7 and 3B7 bind to IGF-IR but do not bind to its structurally related IR, (ii) either the VL-VH or VH-VL sequence order does not apparently affect specificity for IGF-IR and (iii) 1H7 and 3B7 bind the independent epitopes, located in or near the N-terminal (440-514) and C-terminal (62-184) domains of the alpha subunit, respectively. This study not only revealed new information on binding regions for two anti-IGF-IR mAbs, but also provided the scFv genes as tools for further manipulation of the affinity or development of new IGF-IR-targeted cancer therapeutics.
MeSH term(s)	Antibodies, Monoclonal/biosynthesis ; Antibodies, Monoclonal/immunology ; Antibody Specificity ; Epitopes/immunology ; Humans ; Hybridomas/immunology ; Immunoglobulin Variable Region/genetics ; Immunoglobulin Variable Region/immunology ; Immunoglobulin Variable Region/metabolism ; Peptide Library ; Receptor, IGF Type 1/chemistry ; Receptor, IGF Type 1/immunology
Chemical Substances	Antibodies, Monoclonal ; Epitopes ; Immunoglobulin Variable Region ; Peptide Library ; Receptor, IGF Type 1 (EC 2.7.10.1)
Language	English
Publishing date	2008-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218073-x
ISSN	1756-2651 ; 0021-924X
ISSN (online)	1756-2651
ISSN	0021-924X
DOI	10.1093/jb/mvm192
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Article: Isolation and characterization of phage-displayed single chain antibodies recognizing nonreducing terminal mannose residues. 2. Expression, purification, and characterization of recombinant single chain antibodies.

Zhang, Wei / Matsumoto-Takasaki, Ayano / Kusada, Yu / Sakaue, Hiroyuki / Sakai, Keiko / Nakata, Munehiro / Fujita-Yamaguchi, Yoko

Biochemistry

2007 Volume 46, Issue 1, Page(s) 263–270

Abstract: Since phage-display technology is probably the best available strategy to produce antibodies directed against various carbohydrate moieties, we employed phage-display technology to generate human single chain antibodies (scFvs) using neoglycolipids as ... ...

Abstract	Since phage-display technology is probably the best available strategy to produce antibodies directed against various carbohydrate moieties, we employed phage-display technology to generate human single chain antibodies (scFvs) using neoglycolipids as carbohydrate antigens. An accompanying paper in this issue describes how phage-displayed antibodies (phage Abs) that recognized nonreducing terminal mannose residues were isolated and characterized. In this study, four independent scFv genes, isolated by a mannotriose (Man3)-bearing lipid as an antigen as previously described, were used to construct expression vectors to produce soluble scFv proteins in quantity. Both bacterial and mammalian expression systems were used to produce glutathione S-transferase-scFv fusion proteins and scFv-human IgG1 Fc conjugates, respectively. The expressed scFv fusion proteins were purified to apparent homogeneity with yields of approximately 1 and 48 mg, from 1 L of bacterial culture and myeloma cell media, respectively. Surface plasmon resonance and ELISA analyses confirmed that purified scFv proteins showed Man3 specificity. The humanized antibody in scFv-Fc form, derived from clone 5A3, was a disulfide-liked dimer with a molecular mass of 108 kDa. According to a bivalent model, the kinetics parameters of its binding to Man3 were determined to be ka = 4.03 x 104 M-1 s-1, kd = 5.77 x 10-4 s-1, KA = 6.98 x 107 M-1, and KD = 1.43 x 10-8 M. This study thus established the foundation for isolation of carbohydrate-specific scFv genes and eventual production of humanized scFv-Fc type antibodies.
MeSH term(s)	Antibody Specificity ; Cells, Cultured ; Dimerization ; Enzyme-Linked Immunosorbent Assay ; Humans ; Immunoglobulin Variable Region/genetics ; Immunoglobulin Variable Region/immunology ; Immunoglobulin Variable Region/isolation & purification ; Mannose/immunology ; Molecular Weight ; Peptide Library ; Recombinant Fusion Proteins/biosynthesis ; Recombinant Fusion Proteins/immunology ; Recombinant Fusion Proteins/isolation & purification ; Surface Plasmon Resonance
Chemical Substances	Immunoglobulin Variable Region ; Peptide Library ; Recombinant Fusion Proteins ; Mannose (PHA4727WTP)
Language	English
Publishing date	2007-01-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi0618767
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Article: Isolation and characterization of phage-displayed single chain antibodies recognizing nonreducing terminal mannose residues. 1. A new strategy for generation of anti-carbohydrate antibodies.

Sakai, Keiko / Shimizu, Yoshitaka / Chiba, Tomoki / Matsumoto-Takasaki, Ayano / Kusada, Yu / Zhang, Wei / Nakata, Munehiro / Kojima, Naoya / Toma, Kazunori / Takayanagi, Atsushi / Shimizu, Nobuyoshi / Fujita-Yamaguchi, Yoko

Biochemistry

2007 Volume 46, Issue 1, Page(s) 253–262

Abstract: Phage-display technology is probably the best available strategy to produce antibodies directed against various carbohydrate moieties since conventional hybridoma technologies have yielded mostly low-affinity antibodies against a limited number of ... ...

Abstract	Phage-display technology is probably the best available strategy to produce antibodies directed against various carbohydrate moieties since conventional hybridoma technologies have yielded mostly low-affinity antibodies against a limited number of carbohydrate antigens. Because of difficulties in immobilization of carbohydrate antigens onto plastic plates, however, the same procedures used for protein antigens cannot be readily applied. We adapted phage-display technology to generate human single chain antibodies (scFvs) using neoglycolipids as antigens. This study describes the isolation and characterization of phage-displayed antibodies (phage Abs) that recognized nonreducing terminal mannose residues. We first constructed a phage Ab library with a large repertoire using CDR shuffling and VL/VH shuffling methods with unique vector constructs. The library was subjected to four rounds of panning against neoglycolipids synthesized from mannotriose (Man3) and dipalmitoylphosphatidylethanolamine (DPPE) by reductive amination. Of 672 clones screened by enzyme-linked immunosorbent assay (ELISA) using Man3-DPPE as an antigen, 25 positive clones encoding scFvs with unique amino acid sequences were isolated as candidates for phage Abs against Man3 residues. TLC-overlay assays and surface plasmon resonance analyses revealed that selected phage Abs bound to neoglycolipids bearing mannose residues at nonreducing termini. In addition, binding of the phage Ab to RNase B carrying high mannose type oligosaccharides but not to fetuin carrying complex type and O-linked oligosaccharides was confirmed. Furthermore, first round characterization of scFvs expressed from respective phages indicated good affinity and specificity for nonreducing terminal mannose residues. These results demonstrated the usefulness of this strategy in constructing human scFv against various carbohydrate antigens. Further studies on the purification and characterization of these scFvs are presented in an accompanying paper in this issue.
MeSH term(s)	Antibody Affinity ; Antibody Specificity ; Carbohydrate Conformation ; Carbohydrates/immunology ; DNA, Complementary/metabolism ; Enzyme-Linked Immunosorbent Assay ; Humans ; Immunoglobulin Variable Region/genetics ; Immunoglobulin Variable Region/immunology ; Immunoglobulin Variable Region/isolation & purification ; Mannose/immunology ; Peptide Library
Chemical Substances	Carbohydrates ; DNA, Complementary ; Immunoglobulin Variable Region ; Peptide Library ; Mannose (PHA4727WTP)
Language	English
Publishing date	2007-01-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi061875e
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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 / Kusada, Jun / 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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