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Article ; Online: UPF1-Mediated RNA Decay-Danse Macabre in a Cloud.

Lavysh, Daria / Neu-Yilik, Gabriele

2020 Volume 10, Issue 7

Abstract: Nonsense-mediated RNA decay (NMD) is the prototype example of a whole family of RNA decay pathways that unfold around a common central effector protein called UPF1. While NMD in yeast appears to be a linear pathway, NMD in higher eukaryotes is a ... ...

Abstract	Nonsense-mediated RNA decay (NMD) is the prototype example of a whole family of RNA decay pathways that unfold around a common central effector protein called UPF1. While NMD in yeast appears to be a linear pathway, NMD in higher eukaryotes is a multifaceted phenomenon with high variability with respect to substrate RNAs, degradation efficiency, effector proteins and decay-triggering RNA features. Despite increasing knowledge of the mechanistic details, it seems ever more difficult to define NMD and to clearly distinguish it from a growing list of other UPF1-mediated RNA decay pathways (UMDs). With a focus on mammalian, we here critically examine the prevailing NMD models and the gaps and inconsistencies in these models. By exploring the minimal requirements for NMD and other UMDs, we try to elucidate whether they are separate and definable pathways, or rather variations of the same phenomenon. Finally, we suggest that the operating principle of the UPF1-mediated decay family could be considered similar to that of a computing cloud providing a flexible infrastructure with rapid elasticity and dynamic access according to specific user needs.
MeSH term(s)	Animals ; Fungal Proteins/metabolism ; Humans ; Nonsense Mediated mRNA Decay ; RNA Helicases/metabolism ; RNA, Messenger/chemistry ; Trans-Activators/metabolism ; Yeasts/metabolism
Chemical Substances	Fungal Proteins ; RNA, Messenger ; Trans-Activators ; RNA Helicases (EC 3.6.4.13) ; UPF1 protein, human (EC 3.6.4.13)
Language	English
Publishing date	2020-07-04
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom10070999
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Article ; Online: NMD inhibition by 5-azacytidine augments presentation of immunogenic frameshift-derived neoepitopes.

Becker, Jonas P / Helm, Dominic / Rettel, Mandy / Stein, Frank / Hernandez-Sanchez, Alejandro / Urban, Katharina / Gebert, Johannes / Kloor, Matthias / Neu-Yilik, Gabriele / von Knebel Doeberitz, Magnus / Hentze, Matthias W / Kulozik, Andreas E

iScience

2021 Volume 24, Issue 4, Page(s) 102389

Abstract: Frameshifted protein sequences elicit tumor-specific T cell-mediated immune responses in microsatellite-unstable (MSI) cancers if presented by HLA class I molecules. However, their expression and presentation are limited by nonsense-mediated RNA decay ( ... ...

Abstract	Frameshifted protein sequences elicit tumor-specific T cell-mediated immune responses in microsatellite-unstable (MSI) cancers if presented by HLA class I molecules. However, their expression and presentation are limited by nonsense-mediated RNA decay (NMD). We employed an unbiased immunopeptidomics workflow to analyze MSI HCT-116 cells and identified >10,000 HLA class I-presented peptides including five frameshift-derived InDel neoepitopes. Notably, pharmacological NMD inhibition with 5-azacytidine stabilizes frameshift-bearing transcripts and increases the HLA class I-mediated presentation of InDel neoepitopes. The frameshift mutation underlying one of the identified InDel neoepitopes is highly recurrent in MSI colorectal cancer cell lines and primary patient samples, and immunization with the corresponding neoepitope induces strong CD8
Language	English
Publishing date	2021-04-01
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2021.102389
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Article ; Online: Blasticidin S inhibits mammalian translation and enhances production of protein encoded by nonsense mRNA.

Powers, Kyle T / Stevenson-Jones, Flint / Yadav, Sathish K N / Amthor, Beate / Bufton, Joshua C / Borucu, Ufuk / Shen, Dakang / Becker, Jonas P / Lavysh, Daria / Hentze, Matthias W / Kulozik, Andreas E / Neu-Yilik, Gabriele / Schaffitzel, Christiane

Nucleic acids research

2021 Volume 49, Issue 13, Page(s) 7665–7679

Abstract: Deciphering translation is of paramount importance for the understanding of many diseases, and antibiotics played a pivotal role in this endeavour. Blasticidin S (BlaS) targets translation by binding to the peptidyl transferase center of the large ... ...

Abstract	Deciphering translation is of paramount importance for the understanding of many diseases, and antibiotics played a pivotal role in this endeavour. Blasticidin S (BlaS) targets translation by binding to the peptidyl transferase center of the large ribosomal subunit. Using biochemical, structural and cellular approaches, we show here that BlaS inhibits both translation elongation and termination in Mammalia. Bound to mammalian terminating ribosomes, BlaS distorts the 3'CCA tail of the P-site tRNA to a larger extent than previously reported for bacterial ribosomes, thus delaying both, peptide bond formation and peptidyl-tRNA hydrolysis. While BlaS does not inhibit stop codon recognition by the eukaryotic release factor 1 (eRF1), it interferes with eRF1's accommodation into the peptidyl transferase center and subsequent peptide release. In human cells, BlaS inhibits nonsense-mediated mRNA decay and, at subinhibitory concentrations, modulates translation dynamics at premature termination codons leading to enhanced protein production.
MeSH term(s)	Cryoelectron Microscopy ; HeLa Cells ; Humans ; Nonsense Mediated mRNA Decay/drug effects ; Nucleosides/chemistry ; Nucleosides/pharmacology ; Peptide Chain Elongation, Translational/drug effects ; Peptide Chain Termination, Translational/drug effects ; Peptide Termination Factors/metabolism ; Peptides/metabolism ; Protein Synthesis Inhibitors/chemistry ; Protein Synthesis Inhibitors/pharmacology ; RNA, Messenger/metabolism ; RNA, Transfer/chemistry ; RNA, Transfer/metabolism ; Ribosome Subunits, Large, Eukaryotic/chemistry ; Ribosome Subunits, Large, Eukaryotic/drug effects ; Ribosome Subunits, Large, Eukaryotic/metabolism ; Ribosomes/metabolism
Chemical Substances	Nucleosides ; Peptide Termination Factors ; Peptides ; Protein Synthesis Inhibitors ; RNA, Messenger ; blasticidin S (83U64J9U23) ; RNA, Transfer (9014-25-9)
Language	English
Publishing date	2021-06-22
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/gkab532
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Article ; Online: NMD inhibition by 5-azacytidine augments presentation of immunogenic frameshift-derived neoepitopes

Jonas P. Becker / Dominic Helm / Mandy Rettel / Frank Stein / Alejandro Hernandez-Sanchez / Katharina Urban / Johannes Gebert / Matthias Kloor / Gabriele Neu-Yilik / Magnus von Knebel Doeberitz / Matthias W. Hentze / Andreas E. Kulozik

iScience, Vol 24, Iss 4, Pp 102389- (2021)

2021

Abstract: Summary: Frameshifted protein sequences elicit tumor-specific T cell-mediated immune responses in microsatellite-unstable (MSI) cancers if presented by HLA class I molecules. However, their expression and presentation are limited by nonsense-mediated RNA ...

Abstract	Summary: Frameshifted protein sequences elicit tumor-specific T cell-mediated immune responses in microsatellite-unstable (MSI) cancers if presented by HLA class I molecules. However, their expression and presentation are limited by nonsense-mediated RNA decay (NMD). We employed an unbiased immunopeptidomics workflow to analyze MSI HCT-116 cells and identified >10,000 HLA class I-presented peptides including five frameshift-derived InDel neoepitopes. Notably, pharmacological NMD inhibition with 5-azacytidine stabilizes frameshift-bearing transcripts and increases the HLA class I-mediated presentation of InDel neoepitopes. The frameshift mutation underlying one of the identified InDel neoepitopes is highly recurrent in MSI colorectal cancer cell lines and primary patient samples, and immunization with the corresponding neoepitope induces strong CD8+ T cell responses in an HLA-A∗02:01 transgenic mouse model. Our data show directly that pharmacological NMD inhibition augments HLA class I-mediated presentation of immunogenic frameshift-derived InDel neoepitopes thus highlighting the clinical potential of NMD inhibition in anti-cancer immunotherapy strategies.
Keywords	Biological Sciences ; Immunology ; Cancer ; Science ; Q
Subject code	616
Language	English
Publishing date	2021-04-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: Plasticity of nuclear and cytoplasmic stress responses of RNA-binding proteins.

Backlund, Michael / Stein, Frank / Rettel, Mandy / Schwarzl, Thomas / Perez-Perri, Joel I / Brosig, Annika / Zhou, Yang / Neu-Yilik, Gabriele / Hentze, Matthias W / Kulozik, Andreas E

Nucleic acids research

2019 Volume 48, Issue 9, Page(s) 4725–4740

Abstract: Cellular stress causes multifaceted reactions to trigger adaptive responses to environmental cues at all levels of the gene expression pathway. RNA-binding proteins (RBP) are key contributors to stress-induced regulation of RNA fate and function. Here, ... ...

Abstract	Cellular stress causes multifaceted reactions to trigger adaptive responses to environmental cues at all levels of the gene expression pathway. RNA-binding proteins (RBP) are key contributors to stress-induced regulation of RNA fate and function. Here, we uncover the plasticity of the RNA interactome in stressed cells, differentiating between responses in the nucleus and in the cytoplasm. We applied enhanced RNA interactome capture (eRIC) analysis preceded by nucleo-cytoplasmic fractionation following arsenite-induced oxidative stress. The data reveal unexpectedly compartmentalized RNA interactomes and their responses to stress, including differential responses of RBPs in the nucleus versus the cytoplasm, which would have been missed by whole cell analyses.
MeSH term(s)	Cell Fractionation ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Humans ; Oxidative Stress ; Protein Biosynthesis ; RNA Stability ; RNA, Messenger/metabolism ; RNA-Binding Proteins/metabolism
Chemical Substances	RNA, Messenger ; RNA-Binding Proteins
Language	English
Publishing date	2019-09-16
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/gkaa256
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Article ; Online: Prexasertib (LY2606368) reduces clonogenic survival by inducing apoptosis in primary patient-derived osteosarcoma cells and synergizes with cisplatin and talazoparib.

Heidler, Christopher L / Roth, Eva K / Thiemann, Markus / Blattmann, Claudia / Perez, Ramon L / Huber, Peter E / Kovac, Michal / Amthor, Beate / Neu-Yilik, Gabriele / Kulozik, Andreas E

International journal of cancer

2019 Volume 147, Issue 4, Page(s) 1059–1070

Abstract: Progress in the systemic control of osteosarcoma has been limited over the past decades thus indicating the urgent clinical need for the development of novel treatment strategies. Therefore, we have recently developed new preclinical models to study ... ...

Abstract	Progress in the systemic control of osteosarcoma has been limited over the past decades thus indicating the urgent clinical need for the development of novel treatment strategies. Therefore, we have recently developed new preclinical models to study promising novel agents for the treatment of pediatric osteosarcoma. The checkpoint kinase (chk) inhibitor prexasertib (LY2606368) and its salt form (LSN2940930) have recently been shown to be active in adult and pediatric malignancies, including sarcoma. We have now tested the potency of prexasertib in clonogenic survival assays in two new lines of primary patient-derived osteosarcoma cells and in two established osteosarcoma cell lines as a single agent and in combination with cisplatin and the poly ADP-ribose polymerase (PARP) inhibitor talazoparib. Prexasertib alone results in strongly reduced clonogenic survival at low nanomolar concentrations and acts by affecting cell cycle progression, induction of apoptosis and induction of double-stranded DNA breakage at concentrations that are well below clinically tolerable and safe plasma concentrations. In combination with cisplatin and talazoparib, prexasertib acts in a synergistic fashion. Chk1 inhibition by prexasertib and its combination with the DNA damaging agent cisplatin and the PARP-inhibitor talazoparib thus emerges as a potential new treatment option for pediatric osteosarcoma which will now have to be tested in preclinical primary patient derived in vivo models and clinical studies.
MeSH term(s)	Animals ; Antineoplastic Agents/pharmacology ; Apoptosis/drug effects ; Cell Line, Tumor ; Cell Survival/drug effects ; Cisplatin/pharmacology ; Clone Cells/drug effects ; Drug Synergism ; Humans ; Mice ; Osteosarcoma/drug therapy ; Osteosarcoma/pathology ; Phthalazines/pharmacology ; Protein Kinase Inhibitors/pharmacology ; Pyrazines/pharmacology ; Pyrazoles/pharmacology ; Xenograft Model Antitumor Assays/methods
Chemical Substances	Antineoplastic Agents ; Phthalazines ; Protein Kinase Inhibitors ; Pyrazines ; Pyrazoles ; prexasertib ; talazoparib (9QHX048FRV) ; Cisplatin (Q20Q21Q62J)
Language	English
Publishing date	2019-12-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	218257-9
ISSN	1097-0215 ; 0020-7136
ISSN (online)	1097-0215
ISSN	0020-7136
DOI	10.1002/ijc.32814
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Zs.A 478: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: (Phospho)proteomic Profiling of Microsatellite Unstable CRC Cells Reveals Alterations in Nuclear Signaling and Cholesterol Metabolism Caused by Frameshift Mutation of NMD Regulator UPF3A.

Michalak, Malwina / Katzenmaier, Eva-Maria / Roeckel, Nina / Woerner, Stefan M / Fuchs, Vera / Warnken, Uwe / Yuan, Yan P / Bork, Peer / Neu-Yilik, Gabriele / Kulozik, Andreas / von Knebel Doeberitz, Magnus / Kloor, Matthias / Kopitz, Jürgen / Gebert, Johannes

International journal of molecular sciences

2020 Volume 21, Issue 15

Abstract: DNA mismatch repair-deficient colorectal cancers (CRCs) accumulate numerous frameshift mutations at repetitive sequences recognized as microsatellite instability (MSI). When coding mononucleotide repeats (cMNRs) are affected, tumors accumulate frameshift ...

Abstract	DNA mismatch repair-deficient colorectal cancers (CRCs) accumulate numerous frameshift mutations at repetitive sequences recognized as microsatellite instability (MSI). When coding mononucleotide repeats (cMNRs) are affected, tumors accumulate frameshift mutations and premature termination codons (PTC) potentially leading to truncated proteins. Nonsense-mediated RNA decay (NMD) can degrade PTC-containing transcripts and protect from such faulty proteins. As it also regulates normal transcripts and cellular physiology, we tested whether NMD genes themselves are targets of MSI frameshift mutations. A high frequency of cMNR frameshift mutations in the
MeSH term(s)	Cell Line, Tumor ; Colorectal Neoplasms/genetics ; Colorectal Neoplasms/metabolism ; Colorectal Neoplasms/pathology ; Frameshift Mutation ; Gene Expression Profiling ; Genomic Instability ; Humans ; Microsatellite Repeats ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Nonsense Mediated mRNA Decay ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Proteomics ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism
Chemical Substances	Neoplasm Proteins ; Phosphoproteins ; RNA-Binding Proteins ; UPF3A protein, human
Language	English
Publishing date	2020-07-23
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21155234
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Article ; Online: The differential expression of alternatively polyadenylated transcripts is a common stress-induced response mechanism that modulates mammalian mRNA expression in a quantitative and qualitative fashion.

Hollerer, Ina / Curk, Tomaz / Haase, Bettina / Benes, Vladimir / Hauer, Christian / Neu-Yilik, Gabriele / Bhuvanagiri, Madhuri / Hentze, Matthias W / Kulozik, Andreas E

RNA (New York, N.Y.)

2016 Volume 22, Issue 9, Page(s) 1441–1453

Abstract: Stress adaptation plays a pivotal role in biological processes and requires tight regulation of gene expression. In this study, we explored the effect of cellular stress on mRNA polyadenylation and investigated the implications of regulated ... ...

Abstract	Stress adaptation plays a pivotal role in biological processes and requires tight regulation of gene expression. In this study, we explored the effect of cellular stress on mRNA polyadenylation and investigated the implications of regulated polyadenylation site usage on mammalian gene expression. High-confidence polyadenylation site mapping combined with global pre-mRNA and mRNA expression profiling revealed that stress induces an accumulation of genes with differentially expressed polyadenylated mRNA isoforms in human cells. Specifically, stress provokes a global trend in polyadenylation site usage toward decreased utilization of promoter-proximal poly(A) sites in introns or ORFs and increased utilization of promoter-distal polyadenylation sites in intergenic regions. This extensively affects gene expression beyond regulating mRNA abundance by changing mRNA length and by altering the configuration of open reading frames. Our study highlights the impact of post-transcriptional mechanisms on stress-dependent gene regulation and reveals the differential expression of alternatively polyadenylated transcripts as a common stress-induced mechanism in mammalian cells.
MeSH term(s)	HEK293 Cells ; Humans ; Introns ; Nucleotide Motifs ; Open Reading Frames ; Polyadenylation ; Promoter Regions, Genetic ; RNA, Messenger/chemistry ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Stress, Physiological
Chemical Substances	RNA, Messenger
Language	English
Publishing date	2016-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	1241540-6
ISSN	1469-9001 ; 1355-8382
ISSN (online)	1469-9001
ISSN	1355-8382
DOI	10.1261/rna.055657.115
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Zs.A 4777: Show issues

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Article ; Online: Proteomic Analysis Reveals Branch-specific Regulation of the Unfolded Protein Response by Nonsense-mediated mRNA Decay.

Sieber, Jana / Hauer, Christian / Bhuvanagiri, Madhuri / Leicht, Stefan / Krijgsveld, Jeroen / Neu-Yilik, Gabriele / Hentze, Matthias W / Kulozik, Andreas E

Molecular & cellular proteomics : MCP

2016 Volume 15, Issue 5, Page(s) 1584–1597

Abstract: Nonsense-mediated mRNA decay (NMD) has originally been described as a surveillance mechanism to inhibit the expression of mRNAs with truncated open reading frames (ORFs) and to contribute to the fidelity of gene expression. It is now recognized that NMD ... ...

Abstract	Nonsense-mediated mRNA decay (NMD) has originally been described as a surveillance mechanism to inhibit the expression of mRNAs with truncated open reading frames (ORFs) and to contribute to the fidelity of gene expression. It is now recognized that NMD also controls the expression of physiological genes with "intact" mRNA. Stress can decrease NMD efficiency and thus increase the mRNA levels of physiological NMD targets. As stress can also inhibit translation, the net outcome for shaping the proteome is difficult to predict. We have thus analyzed de novo protein synthesis in response to NMD inhibition or the induction of mild endoplasmic reticulum (ER) stress by treatment of cells with the reducing agent dithiotreitol (DTT). For this purpose, we combined pulsed azidohomoalanine (AHA) and stable isotope labeling by amino acids in cell culture (SILAC). Labeled proteins were purified by click chemistry-based covalent coupling to agarose beads, trypsinized, fractionated, and analyzed by mass spectrometry (MS). We find that mild ER stress up-regulates the de novo synthesis of components of all three branches of the unfolded protein response (PERK, IRE1 and ATF6) without increasing eIF2α phosphorylation or impairing of protein translation. In contrast, inhibition of NMD induces de novo protein synthesis of downstream targets of the PERK and IRE1 pathways, whereas we could not detect regulation of ATF6-responsive genes. These data thus support a model that implicates a positive feedback loop of ER stress inhibiting NMD efficiency which further promotes the ER stress response in a branch-specific manner.
MeSH term(s)	Alanine/analogs & derivatives ; Alanine/chemistry ; Dithiothreitol/pharmacology ; Endoplasmic Reticulum Stress ; Gene Regulatory Networks/drug effects ; HeLa Cells ; Humans ; Isotope Labeling ; Liquid-Liquid Extraction ; Nonsense Mediated mRNA Decay/drug effects ; Proteomics/methods ; Tandem Mass Spectrometry ; Unfolded Protein Response/drug effects
Chemical Substances	azidohomoalanine ; Alanine (OF5P57N2ZX) ; Dithiothreitol (T8ID5YZU6Y)
Language	English
Publishing date	2016-02-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2075924-1
ISSN	1535-9484 ; 1535-9476
ISSN (online)	1535-9484
ISSN	1535-9476
DOI	10.1074/mcp.M115.054056
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Zs.A 5599: Show issues

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Article: NMD: multitasking between mRNA surveillance and modulation of gene expression.

Neu-Yilik, Gabriele / Kulozik, Andreas E

Advances in genetics

2008 Volume 62, Page(s) 185–243

Abstract: Gene expression is a highly specific and regulated multilayer process with a plethora of interconnections as well as safeguard and feedback mechanisms. Messenger RNA, long neglected as a mere subcarrier of genetic information, is more recently recognized ...

Abstract	Gene expression is a highly specific and regulated multilayer process with a plethora of interconnections as well as safeguard and feedback mechanisms. Messenger RNA, long neglected as a mere subcarrier of genetic information, is more recently recognized as a linchpin of regulation and control of gene expression. Moreover, the awareness of not only proteins but also mRNA as a modulator of genetic disorders has vastly increased in recent years. Nonsense-mediated mRNA decay (NMD) is a posttranscriptional surveillance mechanism that uses an intricate network of nuclear and cytoplasmic processes to eliminate mRNAs, containing premature termination codons. It thus helps limit the synthesis of potentially harmful truncated proteins. However, recent results suggest functions of NMD that go far beyond this role and affect the expression of wild-type genes and the modulation of whole pathways. In both respects--the elimination of faulty transcripts and the regulation of error-free mRNAs--NMD has many medical implications. Therefore, it has earned increasing interest from researchers of all fields of the life sciences. In the following text, we (1) present current knowledge about the NMD mechanism and its targets, (2) define its relevance in the regulation of important biochemical pathways, (3) explore its medical significance and the prospects of therapeutic interventions, and (4) discuss additional functions of NMD effectors, some of which may be networked to NMD. The main focus of this chapter lies on mammalian NMD and resorts to the features and factors of NMD in other organisms if these help to complete or illuminate the picture.
MeSH term(s)	Animals ; Codon, Nonsense/physiology ; Gene Expression Regulation/physiology ; Genomic Instability/genetics ; Genomic Instability/physiology ; Humans ; Models, Biological ; Protein Biosynthesis/genetics ; Protein Biosynthesis/physiology ; RNA Processing, Post-Transcriptional/genetics ; RNA Processing, Post-Transcriptional/physiology ; RNA Stability/genetics ; RNA Stability/physiology ; RNA, Messenger/metabolism ; Signal Transduction/genetics ; Transcription Factors/physiology
Chemical Substances	Codon, Nonsense ; RNA, Messenger ; Transcription Factors
Language	English
Publishing date	2008-11-07
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	148-x
ISSN	0065-2660
ISSN	0065-2660
DOI	10.1016/S0065-2660(08)00604-4
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