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Book ; Online ; Thesis: Expressionshemmung des humanen Onkogens Bcr-Abl durch RNA-Interferenz

Wohlbold, Lara

2005

Author's details	vorgelegt von Lara Wohlbold
Language	German
Size	Online-Ressource
Document type	Book ; Online ; Thesis
Thesis / German Habilitation thesis	Univ., Diss--Stuttgart, 2004
Database	Former special subject collection: coastal and deep sea fishing

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Article ; Online: Behind the wheel and under the hood: functions of cyclin-dependent kinases in response to DNA damage.

Wohlbold, Lara / Fisher, Robert P

DNA repair

2009 Volume 8, Issue 9, Page(s) 1018–1024

Abstract: Cell division and the response to genotoxic stress are intimately connected in eukaryotes, for example, by checkpoint pathways that signal the presence of DNA damage or its ongoing repair to the cell cycle machinery, leading to reversible arrest or ... ...

Abstract	Cell division and the response to genotoxic stress are intimately connected in eukaryotes, for example, by checkpoint pathways that signal the presence of DNA damage or its ongoing repair to the cell cycle machinery, leading to reversible arrest or apoptosis. Recent studies reveal another connection: the cyclin-dependent kinases (CDKs) that govern both DNA synthesis (S) phase and mitosis directly coordinate DNA repair processes with progression through the cell cycle. In both mammalian cells and yeast, the two major modes of double strand break (DSB) repair--homologous recombination (HR) and non-homologous end joining (NHEJ)--are reciprocally regulated during the cell cycle. In yeast, the cell cycle kinase Cdk1 directly promotes DSB repair by HR during the G2 phase. In mammalian cells, loss of Cdk2, which is active throughout S and G2 phases, results in defective DNA damage repair and checkpoint signaling. Here we provide an overview of data that implicate CDKs in the regulation of DNA damage responses in yeast and metazoans. In yeast, CDK activity is required at multiple points in the HR pathway; the precise roles of CDKs in mammalian HR have yet to be determined. Finally, we consider how the two different, and in some cases opposing, roles of CDKs--as targets of negative regulation by checkpoint signaling and as positive effectors of repair pathway selection and function--could be balanced to produce a coordinated and effective response to DNA damage.
MeSH term(s)	Animals ; Cell Cycle ; Cyclin-Dependent Kinases/metabolism ; DNA Damage ; DNA Repair ; Humans ; Recombination, Genetic/genetics ; Telomere/metabolism
Chemical Substances	Cyclin-Dependent Kinases (EC 2.7.11.22)
Language	English
Publishing date	2009-05-22
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2071608-4
ISSN	1568-7856 ; 1568-7864
ISSN (online)	1568-7856
ISSN	1568-7864
DOI	10.1016/j.dnarep.2009.04.009
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Book ; Online ; Thesis: Expressionshemmung des humanen Onkogens Bcr-Abl durch RNA-Interferenz

Wohlbold, Lara [Verfasser]

2005

Author's details	vorgelegt von Lara Wohlbold
Keywords	Medizin, Gesundheit ; Medicine, Health
Subject code	sg610
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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Article ; Online: NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT complex that docks onto the NOT1 N-terminal domain.

Bawankar, Praveen / Loh, Belinda / Wohlbold, Lara / Schmidt, Steffen / Izaurralde, Elisa

RNA biology

2013 Volume 10, Issue 2, Page(s) 228–244

Abstract: The CCR4-NOT complex plays a crucial role in post-transcriptional mRNA regulation in eukaryotes. This complex catalyzes the removal of mRNA poly(A) tails, thereby repressing translation and committing an mRNA to degradation. The conserved core of the ... ...

Abstract	The CCR4-NOT complex plays a crucial role in post-transcriptional mRNA regulation in eukaryotes. This complex catalyzes the removal of mRNA poly(A) tails, thereby repressing translation and committing an mRNA to degradation. The conserved core of the complex is assembled by the interaction of at least two modules: the NOT module, which minimally consists of NOT1, NOT2 and NOT3, and a catalytic module comprising two deadenylases, CCR4 and POP2/CAF1. Additional complex subunits include CAF40 and two newly identified human subunits, NOT10 and C2orf29. The role of the NOT10 and C2orf29 subunits and how they are integrated into the complex are unknown. Here, we show that the Drosophila melanogaster NOT10 and C2orf29 orthologs form a complex that interacts with the N-terminal domain of NOT1 through C2orf29. These interactions are conserved in human cells, indicating that NOT10 and C2orf29 define a conserved module of the CCR4-NOT complex. We further investigated the assembly of the D. melanogaster CCR4-NOT complex, and demonstrate that the conserved armadillo repeat domain of CAF40 interacts with a region of NOT1, comprising a domain of unknown function, DUF3819. Using tethering assays, we show that each subunit of the CCR4-NOT complex causes translational repression of an unadenylated mRNA reporter and deadenylation and degradation of a polyadenylated reporter. Therefore, the recruitment of a single subunit of the complex to an mRNA target induces the assembly of the complete CCR4-NOT complex, resulting in a similar regulatory outcome.
MeSH term(s)	Animals ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Line ; Conserved Sequence ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Humans ; Multiprotein Complexes/genetics ; Multiprotein Complexes/metabolism ; Polyadenylation ; Protein Binding ; Protein Biosynthesis ; Protein Interaction Mapping ; Protein Structure, Tertiary ; RNA Stability ; RNA, Catalytic/genetics ; RNA, Catalytic/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA-Binding Proteins ; Ribonucleases/genetics ; Ribonucleases/metabolism
Chemical Substances	Carrier Proteins ; Drosophila Proteins ; Multiprotein Complexes ; NOT1 protein, Drosophila ; RNA, Catalytic ; RNA, Messenger ; RNA-Binding Proteins ; CCR4 protein, Drosophila (EC 3.1.-) ; Ribonucleases (EC 3.1.-)
Language	English
Publishing date	2013-01-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1555-8584
ISSN (online)	1555-8584
DOI	10.4161/rna.23018
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Article ; Online: HELZ directly interacts with CCR4-NOT and causes decay of bound mRNAs.

Hanet, Aoife / Räsch, Felix / Weber, Ramona / Ruscica, Vincenzo / Fauser, Maria / Raisch, Tobias / Kuzuoğlu-Öztürk, Duygu / Chang, Chung-Te / Bhandari, Dipankar / Igreja, Cátia / Wohlbold, Lara

Life science alliance

2019 Volume 2, Issue 5

Abstract: Eukaryotic superfamily (SF) 1 helicases have been implicated in various aspects of RNA metabolism, including transcription, processing, translation, and degradation. Nevertheless, until now, most human SF1 helicases remain poorly understood. Here, we ... ...

Abstract	Eukaryotic superfamily (SF) 1 helicases have been implicated in various aspects of RNA metabolism, including transcription, processing, translation, and degradation. Nevertheless, until now, most human SF1 helicases remain poorly understood. Here, we have functionally and biochemically characterized the role of a putative SF1 helicase termed "helicase with zinc-finger," or HELZ. We discovered that HELZ associates with various mRNA decay factors, including components of the carbon catabolite repressor 4-negative on TATA box (CCR4-NOT) deadenylase complex in human and
MeSH term(s)	Animals ; Cell Line ; Drosophila melanogaster ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; HEK293 Cells ; Humans ; Nervous System/growth & development ; Nervous System/metabolism ; Protein Binding ; Protein Biosynthesis ; RNA Helicases/genetics ; RNA Helicases/metabolism ; RNA Stability ; Receptors, CCR4/chemistry ; Receptors, CCR4/metabolism ; TATA Box
Chemical Substances	Receptors, CCR4 ; RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2019-09-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2575-1077
ISSN (online)	2575-1077
DOI	10.26508/lsa.201900405
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Article ; Online: GIGYF1/2 proteins use auxiliary sequences to selectively bind to 4EHP and repress target mRNA expression.

Peter, Daniel / Weber, Ramona / Sandmeir, Felix / Wohlbold, Lara / Helms, Sigrun / Bawankar, Praveen / Valkov, Eugene / Igreja, Cátia / Izaurralde, Elisa

Genes & development

2017 Volume 31, Issue 11, Page(s) 1147–1161

Abstract: The eIF4E homologous protein (4EHP) is thought to repress translation by competing with eIF4E for binding to the 5' cap structure of specific mRNAs to which it is recruited through interactions with various proteins, including the GRB10-interacting GYF ( ... ...

Abstract	The eIF4E homologous protein (4EHP) is thought to repress translation by competing with eIF4E for binding to the 5' cap structure of specific mRNAs to which it is recruited through interactions with various proteins, including the GRB10-interacting GYF (glycine-tyrosine-phenylalanine domain) proteins 1 and 2 (GIGYF1/2). Despite its similarity to eIF4E, 4EHP does not interact with eIF4G and therefore fails to initiate translation. In contrast to eIF4G, GIGYF1/2 bind selectively to 4EHP but not eIF4E. Here, we present crystal structures of the 4EHP-binding regions of GIGYF1 and GIGYF2 in complex with 4EHP, which reveal the molecular basis for the selectivity of the GIGYF1/2 proteins for 4EHP. Complementation assays in a GIGYF1/2-null cell line using structure-based mutants indicate that 4EHP requires interactions with GIGYF1/2 to down-regulate target mRNA expression. Our studies provide structural insights into the assembly of 4EHP-GIGYF1/2 repressor complexes and reveal that rather than merely facilitating 4EHP recruitment to transcripts, GIGYF1/2 proteins are required for repressive activity.
MeSH term(s)	Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Line ; Crystallization ; Gene Expression Regulation/genetics ; HEK293 Cells ; Humans ; Models, Molecular ; Mutation ; Protein Binding/genetics ; Protein Stability ; Protein Structure, Quaternary ; RNA Cap-Binding Proteins/chemistry ; RNA Cap-Binding Proteins/metabolism ; RNA, Messenger/genetics
Chemical Substances	Carrier Proteins ; EIF4E2 protein, human ; GIGYF1 protein, human ; GIGYF2 protein, human ; RNA Cap-Binding Proteins ; RNA, Messenger
Language	English
Publishing date	2017-06-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	806684-x
ISSN	1549-5477 ; 0890-9369
ISSN (online)	1549-5477
ISSN	0890-9369
DOI	10.1101/gad.299420.117
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Article ; Online: A low-complexity region in human XRN1 directly recruits deadenylation and decapping factors in 5'-3' messenger RNA decay.

Chang, Chung-Te / Muthukumar, Sowndarya / Weber, Ramona / Levdansky, Yevgen / Chen, Ying / Bhandari, Dipankar / Igreja, Catia / Wohlbold, Lara / Valkov, Eugene / Izaurralde, Elisa

Nucleic acids research

2019 Volume 47, Issue 17, Page(s) 9282–9295

Abstract: XRN1 is the major cytoplasmic exoribonuclease in eukaryotes, which degrades deadenylated and decapped mRNAs in the last step of the 5'-3' mRNA decay pathway. Metazoan XRN1 interacts with decapping factors coupling the final stages of decay. Here, we ... ...

Abstract	XRN1 is the major cytoplasmic exoribonuclease in eukaryotes, which degrades deadenylated and decapped mRNAs in the last step of the 5'-3' mRNA decay pathway. Metazoan XRN1 interacts with decapping factors coupling the final stages of decay. Here, we reveal a direct interaction between XRN1 and the CCR4-NOT deadenylase complex mediated by a low-complexity region in XRN1, which we term the 'C-terminal interacting region' or CIR. The CIR represses reporter mRNA deadenylation in human cells when overexpressed and inhibits CCR4-NOT and isolated CAF1 deadenylase activity in vitro. Through complementation studies in an XRN1-null cell line, we dissect the specific contributions of XRN1 domains and regions toward decay of an mRNA reporter. We observe that XRN1 binding to the decapping activator EDC4 counteracts the dominant negative effect of CIR overexpression on decay. Another decapping activator PatL1 directly interacts with CIR and alleviates the CIR-mediated inhibition of CCR4-NOT activity in vitro. Ribosome profiling revealed that XRN1 loss impacts not only on mRNA levels but also on the translational efficiency of many cellular transcripts likely as a consequence of incomplete decay. Our findings reveal an additional layer of direct interactions in a tightly integrated network of factors mediating deadenylation, decapping and 5'-3' exonucleolytic decay.
MeSH term(s)	DNA-Binding Proteins/genetics ; Endoribonucleases/genetics ; Exoribonucleases/genetics ; Humans ; Microtubule-Associated Proteins/genetics ; Multiprotein Complexes/genetics ; Nuclear Receptor Subfamily 4, Group A, Member 2/genetics ; Proteins/genetics ; RNA Caps/genetics ; RNA Stability/genetics ; RNA, Messenger/chemistry ; RNA, Messenger/genetics ; Receptors, CCR4/genetics ; Repressor Proteins/genetics ; Trans-Activators/genetics ; Transcription Factors/genetics
Chemical Substances	CCR4 protein, human ; CIR1 protein, human ; CNOT8 protein, human ; DNA-Binding Proteins ; EDC4 protein, human ; Microtubule-Associated Proteins ; Multiprotein Complexes ; NR4A2 protein, human ; Nuclear Receptor Subfamily 4, Group A, Member 2 ; PATL1 protein, human ; Proteins ; RNA Caps ; RNA, Messenger ; Receptors, CCR4 ; Repressor Proteins ; Trans-Activators ; Transcription Factors ; mRNA decapping enzymes ; Endoribonucleases (EC 3.1.-) ; Exoribonucleases (EC 3.1.-) ; XRN1 protein, human (EC 3.1.13.1) ; DCP1A protein, human (EC 3.1.27.-)
Language	English
Publishing date	2019-07-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkz633
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Article ; Online: The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation.

Grüner, Stefan / Peter, Daniel / Weber, Ramona / Wohlbold, Lara / Chung, Min-Yi / Weichenrieder, Oliver / Valkov, Eugene / Igreja, Cátia / Izaurralde, Elisa

Molecular cell

2016 Volume 64, Issue 3, Page(s) 467–479

Abstract: Eukaryotic initiation factor 4G (eIF4G) plays a central role in translation initiation through its interactions with the cap-binding protein eIF4E. This interaction is a major drug target for repressing translation and is naturally regulated by 4E- ... ...

Abstract	Eukaryotic initiation factor 4G (eIF4G) plays a central role in translation initiation through its interactions with the cap-binding protein eIF4E. This interaction is a major drug target for repressing translation and is naturally regulated by 4E-binding proteins (4E-BPs). 4E-BPs and eIF4G compete for binding to the eIF4E dorsal surface via a shared canonical 4E-binding motif, but also contain auxiliary eIF4E-binding sequences, which were assumed to contact non-overlapping eIF4E surfaces. However, it is unknown how metazoan eIF4G auxiliary sequences bind eIF4E. Here, we describe crystal structures of human and Drosophila melanogaster eIF4E-eIF4G complexes, which unexpectedly reveal that the eIF4G auxiliary sequences bind to the lateral surface of eIF4E, using a similar mode to that of 4E-BPs. Our studies provide a molecular model of the eIF4E-eIF4G complex, shed light on the competition mechanism of 4E-BPs, and enable the rational design of selective eIF4G inhibitors to dampen dysregulated translation in disease.
MeSH term(s)	Amino Acid Sequence ; Animals ; Binding Sites ; Cloning, Molecular ; Crystallography, X-Ray ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Eukaryotic Initiation Factor-4E/chemistry ; Eukaryotic Initiation Factor-4E/genetics ; Eukaryotic Initiation Factor-4E/metabolism ; Eukaryotic Initiation Factor-4G/chemistry ; Eukaryotic Initiation Factor-4G/genetics ; Eukaryotic Initiation Factor-4G/metabolism ; Gene Expression ; Humans ; Kinetics ; Models, Molecular ; Mutation ; Peptide Chain Initiation, Translational ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Thermodynamics
Chemical Substances	Eukaryotic Initiation Factor-4E ; Eukaryotic Initiation Factor-4G ; Recombinant Proteins
Language	English
Publishing date	2016-10-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2016.09.020
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Article ; Online: Molecular architecture of 4E-BP translational inhibitors bound to eIF4E.

Peter, Daniel / Igreja, Cátia / Weber, Ramona / Wohlbold, Lara / Weiler, Catrin / Ebertsch, Linda / Weichenrieder, Oliver / Izaurralde, Elisa

Molecular cell

2015 Volume 57, Issue 6, Page(s) 1074–1087

Abstract: The eIF4E-binding proteins (4E-BPs) represent a diverse class of translation inhibitors that are often deregulated in cancer cells. 4E-BPs inhibit translation by competing with eIF4G for binding to eIF4E through an interface that consists of canonical ... ...

Abstract	The eIF4E-binding proteins (4E-BPs) represent a diverse class of translation inhibitors that are often deregulated in cancer cells. 4E-BPs inhibit translation by competing with eIF4G for binding to eIF4E through an interface that consists of canonical and non-canonical eIF4E-binding motifs connected by a linker. The lack of high-resolution structures including the linkers, which contain phosphorylation sites, limits our understanding of how phosphorylation inhibits complex formation. Furthermore, the binding mechanism of the non-canonical motifs is poorly understood. Here, we present structures of human eIF4E bound to 4E-BP1 and fly eIF4E bound to Thor, 4E-T, and eIF4G. These structures reveal architectural elements that are unique to 4E-BPs and provide insight into the consequences of phosphorylation. Guided by these structures, we designed and crystallized a 4E-BP mimic that shows increased repressive activity. Our studies pave the way for the rational design of 4E-BP mimics as therapeutic tools to decrease translation during oncogenic transformation.
MeSH term(s)	Adaptor Proteins, Signal Transducing/chemistry ; Adaptor Proteins, Signal Transducing/metabolism ; Amino Acid Motifs ; Animals ; Binding Sites ; Binding, Competitive ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Crystallography, X-Ray ; Drosophila Proteins/chemistry ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Eukaryotic Initiation Factor-4E/chemistry ; Eukaryotic Initiation Factor-4E/metabolism ; Eukaryotic Initiation Factor-4G/chemistry ; Eukaryotic Initiation Factor-4G/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins/chemistry ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Models, Molecular ; Molecular Mimicry ; Peptide Initiation Factors/chemistry ; Peptide Initiation Factors/genetics ; Peptide Initiation Factors/metabolism ; Phosphoproteins/chemistry ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Conformation ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Carrier Proteins ; Drosophila Proteins ; EIF4EBP1 protein, human ; EIF4EBP3 protein, human ; Eukaryotic Initiation Factor-4E ; Eukaryotic Initiation Factor-4G ; Intracellular Signaling Peptides and Proteins ; Peptide Initiation Factors ; Phosphoproteins ; Recombinant Proteins ; Thor protein, Drosophila ; eIF4G2 protein, Drosophila
Language	English
Publishing date	2015-02-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2015.01.017
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Article ; Online: The interactions of GW182 proteins with PABP and deadenylases are required for both translational repression and degradation of miRNA targets.

Huntzinger, Eric / Kuzuoglu-Öztürk, Duygu / Braun, Joerg E / Eulalio, Ana / Wohlbold, Lara / Izaurralde, Elisa

Nucleic acids research

2012 Volume 41, Issue 2, Page(s) 978–994

Abstract: Animal miRNAs silence the expression of mRNA targets through translational repression, deadenylation and subsequent mRNA degradation. Silencing requires association of miRNAs with an Argonaute protein and a GW182 family protein. In turn, GW182 proteins ... ...

Abstract	Animal miRNAs silence the expression of mRNA targets through translational repression, deadenylation and subsequent mRNA degradation. Silencing requires association of miRNAs with an Argonaute protein and a GW182 family protein. In turn, GW182 proteins interact with poly(A)-binding protein (PABP) and the PAN2-PAN3 and CCR4-NOT deadenylase complexes. These interactions are required for the deadenylation and decay of miRNA targets. Recent studies have indicated that miRNAs repress translation before inducing target deadenylation and decay; however, whether translational repression and deadenylation are coupled or represent independent repressive mechanisms is unclear. Another remaining question is whether translational repression also requires GW182 proteins to interact with both PABP and deadenylases. To address these questions, we characterized the interaction of Drosophila melanogaster GW182 with deadenylases and defined the minimal requirements for a functional GW182 protein. Functional assays in D. melanogaster and human cells indicate that miRNA-mediated translational repression and degradation are mechanistically linked and are triggered through the interactions of GW182 proteins with PABP and deadenylases.
MeSH term(s)	Animals ; Carrier Proteins/metabolism ; Drosophila Proteins/chemistry ; Drosophila Proteins/metabolism ; Drosophila melanogaster/enzymology ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; HeLa Cells ; Humans ; MicroRNAs/metabolism ; Poly(A)-Binding Proteins/metabolism ; Protein Biosynthesis ; Protein Interaction Domains and Motifs ; RNA Interference ; RNA Stability ; RNA, Messenger/metabolism ; RNA-Binding Proteins/chemistry ; Ribonucleases/metabolism ; Transcription Factors/chemistry
Chemical Substances	CNOT1 protein, human ; Carrier Proteins ; Drosophila Proteins ; Gw protein, Drosophila ; MicroRNAs ; NOT1 protein, Drosophila ; Poly(A)-Binding Proteins ; RNA, Messenger ; RNA-Binding Proteins ; TNRC6C protein, human ; Transcription Factors ; Ribonucleases (EC 3.1.-) ; mRNA deadenylase (EC 3.1.-)
Language	English
Publishing date	2012-11-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gks1078
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