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Article: Non-radioactive LATS

Hong, Audrey W / Guan, Kun-Liang

2017 Volume 7, Issue 14

Abstract: This protocol describes a method to directly measure LATS activity by ... ...

Abstract	This protocol describes a method to directly measure LATS activity by an
Language	English
Publishing date	2017-11-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	2833269-6
ISSN	2331-8325
ISSN	2331-8325
DOI	10.21769/BioProtoc.2391
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Article ; Online: Critical roles of phosphoinositides and NF2 in Hippo pathway regulation.

Hong, Audrey W / Meng, Zhipeng / Plouffe, Steven W / Lin, Zhijie / Zhang, Mingjie / Guan, Kun-Liang

Genes & development

2020 Volume 34, Issue 7-8, Page(s) 511–525

Abstract: The Hippo pathway is a master regulator of tissue homeostasis and organ size. NF2 is a well-established tumor suppressor, and loss of NF2 severely compromises Hippo pathway activity. However, the precise mechanism of how NF2 mediates upstream signals to ... ...

Abstract	The Hippo pathway is a master regulator of tissue homeostasis and organ size. NF2 is a well-established tumor suppressor, and loss of NF2 severely compromises Hippo pathway activity. However, the precise mechanism of how NF2 mediates upstream signals to regulate the Hippo pathway is not clear. Here we report that, in mammalian cells, NF2's lipid-binding ability is critical for its function in activating the Hippo pathway in response to osmotic stress. Mechanistically, osmotic stress induces PI(4,5)P
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Cycle Proteins/metabolism ; Cell Line ; Hippo Signaling Pathway ; Homeostasis/physiology ; Humans ; Mice ; Neurofibromin 2/genetics ; Neurofibromin 2/metabolism ; Osmotic Pressure/physiology ; Phosphatidylinositols/metabolism ; Phosphorylation ; Protein Serine-Threonine Kinases/metabolism ; Signal Transduction/genetics ; YAP-Signaling Proteins
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cell Cycle Proteins ; Neurofibromin 2 ; Phosphatidylinositols ; YAP-Signaling Proteins ; Yap1 protein, mouse ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2020-02-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	806684-x
ISSN	1549-5477 ; 0890-9369
ISSN (online)	1549-5477
ISSN	0890-9369
DOI	10.1101/gad.333435.119
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Zs.A 2292: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: The Hippo pathway in intestinal regeneration and disease.

Hong, Audrey W / Meng, Zhipeng / Guan, Kun-Liang

Nature reviews. Gastroenterology & hepatology

2016 Volume 13, Issue 6, Page(s) 324–337

Abstract: The Hippo pathway is a signalling cascade conserved from Drosophila melanogaster to mammals. The mammalian core kinase components comprise MST1 and MST2, SAV1, LATS1 and LATS2 and MOB1A and MOB1B. The transcriptional co-activators YAP1 and TAZ are the ... ...

Abstract	The Hippo pathway is a signalling cascade conserved from Drosophila melanogaster to mammals. The mammalian core kinase components comprise MST1 and MST2, SAV1, LATS1 and LATS2 and MOB1A and MOB1B. The transcriptional co-activators YAP1 and TAZ are the downstream effectors of the Hippo pathway and regulate target gene expression. Hippo signalling has crucial roles in the control of organ size, tissue homeostasis and regeneration, and dysregulation of the Hippo pathway can lead to uncontrolled cell growth and malignant transformation. Mammalian intestine consists of a stem cell compartment as well as differentiated cells, and its ability to regenerate rapidly after injury makes it an excellent model system to study tissue homeostasis, regeneration and tumorigenesis. Several studies have established the important role of the Hippo pathway in these processes. In addition, crosstalk between Hippo and other signalling pathways provides tight, yet versatile, regulation of tissue homeostasis. In this Review, we summarize studies on the role of the Hippo pathway in the intestine on these physiological processes and the underlying mechanisms responsible, and discuss future research directions and potential therapeutic strategies targeting Hippo signalling in intestinal disease.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Bone Morphogenetic Proteins/metabolism ; Carcinogenesis/metabolism ; Cell Adhesion/physiology ; Colonic Neoplasms/physiopathology ; Drosophila melanogaster ; Hedgehog Proteins/metabolism ; Homeostasis/physiology ; Humans ; Intestine, Large/physiology ; Intestine, Small/physiology ; Irritable Bowel Syndrome/physiopathology ; Liver Neoplasms/physiopathology ; Mammals ; Organ Size ; Phosphoproteins/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, G-Protein-Coupled/physiology ; Receptors, Notch/metabolism ; Regeneration/physiology ; Signal Transduction/physiology ; Stress, Physiological/physiology ; Transcription Factors/metabolism ; Wnt Signaling Pathway/physiology
Chemical Substances	Adaptor Proteins, Signal Transducing ; Bone Morphogenetic Proteins ; Hedgehog Proteins ; Phosphoproteins ; Receptors, G-Protein-Coupled ; Receptors, Notch ; Transcription Factors ; YAP1 protein, human ; TAFAZZIN protein, human (EC 2.3.1.-) ; Hippo protein, human (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2016-05-05
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2493722-8
ISSN	1759-5053 ; 1759-5045
ISSN (online)	1759-5053
ISSN	1759-5045
DOI	10.1038/nrgastro.2016.59
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Zs.MG 97: Show issues

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Article ; Online: Disease implications of the Hippo/YAP pathway.

Plouffe, Steven W / Hong, Audrey W / Guan, Kun-Liang

Trends in molecular medicine

2015 Volume 21, Issue 4, Page(s) 212–222

Abstract: The Hippo signaling pathway is important for controlling organ size and tissue homeostasis. Originally identified in Drosophila melanogaster, the core components of the Hippo pathway are highly conserved in mammals. The Hippo pathway can be modulated by ... ...

Abstract	The Hippo signaling pathway is important for controlling organ size and tissue homeostasis. Originally identified in Drosophila melanogaster, the core components of the Hippo pathway are highly conserved in mammals. The Hippo pathway can be modulated by a wide range of stimuli, including G protein-coupled receptor (GPCR) signaling, changes in the actin cytoskeleton, cell-cell contact, and cell polarity. When activated, the Hippo pathway functions as a tumor suppressor to limit cell growth. However, dysregulation by genetic inactivation of core pathway components or amplification or gene fusion of its downstream effectors results in increased cell proliferation and decreased apoptosis and differentiation. Unsurprisingly, this can lead to tissue overgrowth, tumorigenesis, and many other diseases.
MeSH term(s)	Animals ; Apoptosis ; Carcinogenesis ; Cell Proliferation ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Gene Expression Regulation, Developmental ; Gene Expression Regulation, Neoplastic ; Hippo Signaling Pathway ; Homeostasis ; Humans ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Mammals ; Neoplasms/genetics ; Neoplasms/pathology ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Organ Size ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Receptors, G-Protein-Coupled/genetics ; Receptors, G-Protein-Coupled/metabolism ; Signal Transduction ; Trans-Activators/genetics ; Trans-Activators/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism ; YAP-Signaling Proteins
Chemical Substances	Drosophila Proteins ; Intracellular Signaling Peptides and Proteins ; Nuclear Proteins ; Receptors, G-Protein-Coupled ; Trans-Activators ; Transcription Factors ; YAP-Signaling Proteins ; Yki protein, Drosophila ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; hpo protein, Drosophila (EC 2.7.11.1)
Language	English
Publishing date	2015-02-18
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2036490-8
ISSN	1471-499X ; 1471-4914
ISSN (online)	1471-499X
ISSN	1471-4914
DOI	10.1016/j.molmed.2015.01.003
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Article ; Online: Integrative analyses highlight functional regulatory variants associated with neuropsychiatric diseases.

Guo, Margaret G / Reynolds, David L / Ang, Cheen E / Liu, Yingfei / Zhao, Yang / Donohue, Laura K H / Siprashvili, Zurab / Yang, Xue / Yoo, Yongjin / Mondal, Smarajit / Hong, Audrey / Kain, Jessica / Meservey, Lindsey / Fabo, Tania / Elfaki, Ibtihal / Kellman, Laura N / Abell, Nathan S / Pershad, Yash / Bayat, Vafa /

Etminani, Payam / Holodniy, Mark / Geschwind, Daniel H / Montgomery, Stephen B / Duncan, Laramie E / Urban, Alexander E / Altman, Russ B / Wernig, Marius / Khavari, Paul A

Nature genetics

2023 Volume 55, Issue 11, Page(s) 1876–1891

Abstract: Noncoding variants of presumed regulatory function contribute to the heritability of neuropsychiatric disease. A total of 2,221 noncoding variants connected to risk for ten neuropsychiatric disorders, including autism spectrum disorder, attention deficit ...

Abstract	Noncoding variants of presumed regulatory function contribute to the heritability of neuropsychiatric disease. A total of 2,221 noncoding variants connected to risk for ten neuropsychiatric disorders, including autism spectrum disorder, attention deficit hyperactivity disorder, bipolar disorder, borderline personality disorder, major depression, generalized anxiety disorder, panic disorder, post-traumatic stress disorder, obsessive-compulsive disorder and schizophrenia, were studied in developing human neural cells. Integrating epigenomic and transcriptomic data with massively parallel reporter assays identified differentially-active single-nucleotide variants (daSNVs) in specific neural cell types. Expression-gene mapping, network analyses and chromatin looping nominated candidate disease-relevant target genes modulated by these daSNVs. Follow-up integration of daSNV gene editing with clinical cohort analyses suggested that magnesium transport dysfunction may increase neuropsychiatric disease risk and indicated that common genetic pathomechanisms may mediate specific symptoms that are shared across multiple neuropsychiatric diseases.
MeSH term(s)	Humans ; Autism Spectrum Disorder/genetics ; Bipolar Disorder/genetics ; Schizophrenia/genetics ; Obsessive-Compulsive Disorder/genetics ; Obsessive-Compulsive Disorder/psychology ; Depressive Disorder, Major/genetics ; Attention Deficit Disorder with Hyperactivity/genetics
Language	English
Publishing date	2023-10-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	1108734-1
ISSN	1546-1718 ; 1061-4036
ISSN (online)	1546-1718
ISSN	1061-4036
DOI	10.1038/s41588-023-01533-5
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Zs.A 3613: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: GPCR signaling inhibits mTORC1 via PKA phosphorylation of Raptor.

Jewell, Jenna L / Fu, Vivian / Hong, Audrey W / Yu, Fa-Xing / Meng, Delong / Melick, Chase H / Wang, Huanyu / Lam, Wai-Ling Macrina / Yuan, Hai-Xin / Taylor, Susan S / Guan, Kun-Liang

eLife

2019 Volume 8

Abstract: The mammalian target of rapamycin complex 1 (mTORC1) regulates cell growth, metabolism, and autophagy. Extensive research has focused on pathways that activate mTORC1 like growth factors and amino acids; however, much less is known about signaling cues ... ...

Abstract	The mammalian target of rapamycin complex 1 (mTORC1) regulates cell growth, metabolism, and autophagy. Extensive research has focused on pathways that activate mTORC1 like growth factors and amino acids; however, much less is known about signaling cues that directly inhibit mTORC1 activity. Here, we report that G-protein coupled receptors (GPCRs) paired to Gα
MeSH term(s)	Animals ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Humans ; Mechanistic Target of Rapamycin Complex 1/antagonists & inhibitors ; Phosphorylation ; Protein Processing, Post-Translational ; Receptors, G-Protein-Coupled/metabolism ; Regulatory-Associated Protein of mTOR/metabolism ; Signal Transduction
Chemical Substances	RPTOR protein, human ; Receptors, G-Protein-Coupled ; Regulatory-Associated Protein of mTOR ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11)
Language	English
Publishing date	2019-05-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.43038
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Article ; Online: BRCA1/BARD1-dependent ubiquitination of NF2 regulates Hippo-YAP1 signaling.

Verma, Sachin / Yeddula, Narayana / Soda, Yasushi / Zhu, Quan / Pao, Gerald / Moresco, James / Diedrich, Jolene K / Hong, Audrey / Plouffe, Steve / Moroishi, Toshiro / Guan, Kun-Liang / Verma, Inder M

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

2019 Volume 116, Issue 15, Page(s) 7363–7370

Abstract: Coordination of growth and genomic stability is critical for normal cell physiology. Although the E3 ubiquitin ligase BRCA1 is a key player in maintenance of genomic stability, its role in growth signaling remains elusive. Here, we show that BRCA1 ... ...

Abstract	Coordination of growth and genomic stability is critical for normal cell physiology. Although the E3 ubiquitin ligase BRCA1 is a key player in maintenance of genomic stability, its role in growth signaling remains elusive. Here, we show that BRCA1 facilitates stabilization of YAP1 protein and turning "off" the Hippo pathway through ubiquitination of NF2. In BRCA1-deficient cells Hippo pathway is "turned On." Phosphorylation of YAP1 is crucial for this signaling process because a YAP1 mutant harboring alanine substitutions (Mt-YAP5SA) in LATS1 kinase recognition sites not only resists degradation but also rescues YAP1 transcriptional activity in BRCA1-deficient cells. Furthermore, an ectopic expression of the active Mt-YAP5SA, but not inactive Mt-YAP6SA, promotes EGF-independent proliferation and tumorigenesis in BRCA1
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Amino Acid Substitution ; BRCA1 Protein/genetics ; BRCA1 Protein/metabolism ; Breast Neoplasms/genetics ; Breast Neoplasms/metabolism ; Breast Neoplasms/pathology ; Cell Line, Tumor ; Cell Proliferation ; Female ; HEK293 Cells ; Humans ; Mutation, Missense ; Neurofibromin 2/genetics ; Neurofibromin 2/metabolism ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Signal Transduction ; Transcription Factors ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
Chemical Substances	Adaptor Proteins, Signal Transducing ; BRCA1 Protein ; BRCA1 protein, human ; Neurofibromin 2 ; Phosphoproteins ; Transcription Factors ; Tumor Suppressor Proteins ; YAP1 protein, human ; BARD1 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; LATS1 protein, human (EC 2.7.1.-) ; Hippo protein, human (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2019-03-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1822155116
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Article ; Online: Characterization of Hippo Pathway Components by Gene Inactivation.

Plouffe, Steven W / Meng, Zhipeng / Lin, Kimberly C / Lin, Brian / Hong, Audrey W / Chun, Justin V / Guan, Kun-Liang

Molecular cell

2016 Volume 64, Issue 5, Page(s) 993–1008

Abstract: The Hippo pathway is important for regulating tissue homeostasis, and its dysregulation has been implicated in human cancer. However, it is not well understood how the Hippo pathway becomes dysregulated because few mutations in core Hippo pathway ... ...

Abstract	The Hippo pathway is important for regulating tissue homeostasis, and its dysregulation has been implicated in human cancer. However, it is not well understood how the Hippo pathway becomes dysregulated because few mutations in core Hippo pathway components have been identified. Therefore, much work in the Hippo field has focused on identifying upstream regulators, and a complex Hippo interactome has been identified. Nevertheless, it is not always clear which components are the most physiologically relevant in regulating YAP/TAZ. To provide an overview of important Hippo pathway components, we created knockout cell lines for many of these components and compared their relative contributions to YAP/TAZ regulation in response to a wide range of physiological signals. By this approach, we provide an overview of the functional importance of many Hippo pathway components and demonstrate NF2 and RHOA as important regulators of YAP/TAZ and TAOK1/3 as direct kinases for LATS1/2.
MeSH term(s)	Acyltransferases ; Cell Cycle Proteins ; Clustered Regularly Interspaced Short Palindromic Repeats ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation/physiology ; Gene Knockdown Techniques ; HEK293 Cells ; Hippo Signaling Pathway ; Humans ; Neurofibromin 2 ; Nuclear Proteins ; Phosphorylation ; Protein Serine-Threonine Kinases ; Signal Transduction/genetics ; Transcription Factors ; Tumor Suppressor Proteins ; rhoA GTP-Binding Protein
Chemical Substances	Cell Cycle Proteins ; DNA-Binding Proteins ; Neurofibromin 2 ; Nuclear Proteins ; Transcription Factors ; Tumor Suppressor Proteins ; YY1AP1 protein, human ; Acyltransferases (EC 2.3.-) ; TAFAZZIN protein, human (EC 2.3.1.-) ; LATS1 protein, human (EC 2.7.1.-) ; LATS2 protein, human (EC 2.7.1.11) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; TAO1 protein kinase (EC 2.7.11.1) ; rhoA GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2016-11-17
Publishing country	United States
Document type	Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2016.10.034
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Article ; Online: Osmotic stress-induced phosphorylation by NLK at Ser128 activates YAP.

Hong, Audrey W / Meng, Zhipeng / Yuan, Hai-Xin / Plouffe, Steven W / Moon, Sungho / Kim, Wantae / Jho, Eek-Hoon / Guan, Kun-Liang

EMBO reports

2016 Volume 18, Issue 1, Page(s) 72–86

Abstract: YAP is the major downstream effector of the Hippo pathway, which controls cell growth, tissue homeostasis, and organ size. Aberrant YAP activation, resulting from dysregulation of the Hippo pathway, is frequently observed in human cancers. YAP is a ... ...

Abstract	YAP is the major downstream effector of the Hippo pathway, which controls cell growth, tissue homeostasis, and organ size. Aberrant YAP activation, resulting from dysregulation of the Hippo pathway, is frequently observed in human cancers. YAP is a transcription co-activator, and the key mechanism of YAP regulation is its nuclear and cytoplasmic translocation. The Hippo pathway component, LATS, inhibits YAP by phosphorylating YAP at Ser127, leading to 14-3-3 binding and cytoplasmic retention of YAP Here, we report that osmotic stress stimulates transient YAP nuclear localization and increases YAP activity even when YAP Ser127 is phosphorylated. Osmotic stress acts via the NLK kinase to induce YAP Ser128 phosphorylation. Phosphorylation of YAP at Ser128 interferes with its ability to bind to 14-3-3, resulting in YAP nuclear accumulation and induction of downstream target gene expression. This osmotic stress-induced YAP activation enhances cellular stress adaptation. Our findings reveal a critical role for NLK-mediated Ser128 phosphorylation in YAP regulation and a crosstalk between osmotic stress and the Hippo pathway.
MeSH term(s)	Cell Cycle ; Cell Cycle Proteins ; Cell Nucleolus ; Cytoplasm/metabolism ; Enzyme Activation ; HEK293 Cells ; Humans ; Intracellular Signaling Peptides and Proteins/chemistry ; Intracellular Signaling Peptides and Proteins/metabolism ; Nuclear Proteins/metabolism ; Osmotic Pressure ; Phosphorylation ; Protein Binding ; Protein Transport ; Protein-Serine-Threonine Kinases/chemistry ; Protein-Serine-Threonine Kinases/metabolism ; Serine/chemistry ; Serine/metabolism ; Signal Transduction ; Transcription Factors/metabolism
Chemical Substances	Cell Cycle Proteins ; Intracellular Signaling Peptides and Proteins ; Nuclear Proteins ; Transcription Factors ; YY1AP1 protein, human ; Serine (452VLY9402) ; NLK protein, human (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2016-12-15
Publishing country	England
Document type	Journal Article
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.201642681
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Article ; Online: Opposing roles of conventional and novel PKC isoforms in Hippo-YAP pathway regulation.

Gong, Rui / Hong, Audrey W / Plouffe, Steven W / Zhao, Bin / Liu, Guangbo / Yu, Fa-Xing / Xu, Yanhui / Guan, Kun-Liang

Cell research

2015 Volume 25, Issue 8, Page(s) 985–988

MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Diglycerides/chemistry ; Diglycerides/pharmacology ; Enzyme Activation/drug effects ; HEK293 Cells ; Humans ; Phosphoproteins/metabolism ; Protein Isoforms ; Protein Kinase C/chemistry ; Protein Kinase C/physiology ; Signal Transduction ; Transcription Factors
Chemical Substances	Adaptor Proteins, Signal Transducing ; Diglycerides ; Phosphoproteins ; Protein Isoforms ; Transcription Factors ; YAP1 protein, human ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2015-07-24
Publishing country	England
Document type	Letter ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1319303-x
ISSN	1748-7838 ; 1001-0602
ISSN (online)	1748-7838
ISSN	1001-0602
DOI	10.1038/cr.2015.88
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