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Volumn 18, Issue 7, 2016, Pages 803-813

PTP1B controls non-mitochondrial oxygen consumption by regulating RNF213 to promote tumour survival during hypoxia

(25)  Banh, Robert S a,b,c   Iorio, Caterina b   Marcotte, Richard b   Xu, Yang a,b,c   Cojocari, Dan a,b   Rahman, Anas Abdel d,e   Pawling, Judy d   Zhang, Wei a   Sinha, Ankit a,b   Rose, Christopher M f   Isasa, Marta f   Zhang, Shuang c   Wu, Ronald a,b   Virtanen, Carl b   Hitomi, Toshiaki g   Habu, Toshiyuki g   Sidhu, Sachdev S a   Koizumi, Akio g   Wilkins, Sarah E h   Kislinger, Thomas a,b   more..


Author keywords

[No Author keywords available]

Indexed keywords

ALPHA KGDD PROTEIN; DIOXYGENASE; EPIDERMAL GROWTH FACTOR RECEPTOR 2; PROTEIN TYROSINE PHOSPHATASE 1B; RNF213 PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATASE; ALPHA KETOGLUTARATE DEPENDENT DIOXYGENASE FTO; PTPN1 PROTEIN, HUMAN; PTPN1 PROTEIN, MOUSE; RNF213 PROTEIN, HUMAN; RNF213 PROTEIN, MOUSE; UBIQUITIN PROTEIN LIGASE;

EID: 84975318750     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb3376     Document Type: Article
Times cited : (102)

References (62)
  • 1
    • 57149142495 scopus 로고    scopus 로고
    • The impact of O2 availability on human cancer
    • Bertout J. A, Patel S. A, & Simon M. C. The impact of O2 availability on human cancer. Nat. Rev. Cancer 8, 967-975 (2008).
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 967-975
    • Bertout, J.A.1    Patel, S.A.2    Simon, M.C.3
  • 2
    • 33644622570 scopus 로고    scopus 로고
    • HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
    • Papandreou I, Cairns R. A, Fontana L, Lim A. L, & Denko N. C. HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. Cell Metab. 3, 187-197 (2006).
    • (2006) Cell Metab , vol.3 , pp. 187-197
    • Papandreou, I.1    Cairns, R.A.2    Fontana, L.3    Lim, A.L.4    Denko, N.C.5
  • 3
    • 67349217986 scopus 로고    scopus 로고
    • Molecular mechanisms of mTOR-mediated translational control
    • Ma X. M, & Blenis J. Molecular mechanisms of mTOR-mediated translational control. Nat. Rev. 10, 307-318 (2009).
    • (2009) Nat. Rev , vol.10 , pp. 307-318
    • Ma, X.M.1    Blenis, J.2
  • 4
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • Laplante M, & Sabatini D. M. mTOR signaling in growth control and disease. Cell 149, 274-293 (2012).
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 5
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, & Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519-529 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 6
    • 39349105090 scopus 로고    scopus 로고
    • Expanding chemical biology of 2-oxoglutarate oxygenases
    • Loenarz C, & Schofield C. J. Expanding chemical biology of 2-oxoglutarate oxygenases. Nat. Chem. Biol. 4, 152-156 (2008).
    • (2008) Nat. Chem. Biol , vol.4 , pp. 152-156
    • Loenarz, C.1    Schofield, C.J.2
  • 7
    • 2342644926 scopus 로고    scopus 로고
    • Oxygen sensing by HIF hydroxylases
    • Schofield C. J, & Ratcliffe P. J. Oxygen sensing by HIF hydroxylases. Nat. Rev. 5, 343-354 (2004).
    • (2004) Nat. Rev , vol.5 , pp. 343-354
    • Schofield, C.J.1    Ratcliffe, P.J.2
  • 8
    • 20744448379 scopus 로고    scopus 로고
    • Oxidation by 2-oxoglutarate oxygenases: Non-haem iron systems in catalysis and signalling
    • discussion 1035-1040
    • Hewitson K. S, Granatino N, Welford R. W, McDonough M. A, & Schofield C. J. Oxidation by 2-oxoglutarate oxygenases: non-haem iron systems in catalysis and signalling. Phil. Transact. A 363, 807-828 (2005), discussion 1035-1040.
    • (2005) Phil. Transact. A , vol.363 , pp. 807-828
    • Hewitson, K.S.1    Granatino, N.2    Welford, R.W.3    McDonough, M.A.4    Schofield, C.J.5
  • 9
    • 0032760945 scopus 로고    scopus 로고
    • Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
    • Schofield C. J, & Zhang Z. Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes. Curr. Opin. Struct. Biol. 9, 722-731 (1999).
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 722-731
    • Schofield, C.J.1    Zhang, Z.2
  • 10
    • 84915763059 scopus 로고    scopus 로고
    • Ascorbate as a co-factor for Fe-and 2-oxoglutarate dependent dioxygenases: Physiological activity in tumor growth and progression
    • Kuiper C, & Vissers M. C. Ascorbate as a co-factor for Fe-and 2-oxoglutarate dependent dioxygenases: physiological activity in tumor growth and progression. Front Oncol. 4, 359 (2014).
    • (2014) Front Oncol , vol.4 , pp. 359
    • Kuiper, C.1    Vissers, M.C.2
  • 11
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene
    • Elchebly M, et al. Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science 283, 1544-1548 (1999).
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1
  • 12
    • 18344379861 scopus 로고    scopus 로고
    • PTP1B regulates leptin signal transduction in vivo
    • Zabolotny J. M, et al. PTP1B regulates leptin signal transduction in vivo. Dev. Cell 2, 489-495 (2002).
    • (2002) Dev. Cell , vol.2 , pp. 489-495
    • Zabolotny, J.M.1
  • 13
    • 0033942614 scopus 로고    scopus 로고
    • Increased energy expenditure, decreased adiposity, and tissuespecific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice
    • Klaman L. D, et al. Increased energy expenditure, decreased adiposity, and tissuespecific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol. Cell. Biol. 20, 5479-5489 (2000).
    • (2000) Mol. Cell. Biol , vol.20 , pp. 5479-5489
    • Klaman, L.D.1
  • 14
    • 84879040174 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B regulates pyruvate kinase M2 tyrosine phosphorylation
    • Bettaieb A, et al. Protein tyrosine phosphatase 1B regulates pyruvate kinase M2 tyrosine phosphorylation. J. Biol. Chem. 288, 17360-17371 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 17360-17371
    • Bettaieb, A.1
  • 15
    • 83655165310 scopus 로고    scopus 로고
    • H2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response
    • ra86
    • Krishnan N, Fu C, Pappin D. J, & Tonks N. K. H2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response. Sci. Signal. 4, ra86 (2011).
    • (2011) Sci Signal , vol.4
    • Krishnan, N.1    Fu, C.2    Pappin, D.J.3    Tonks, N.K.4
  • 16
    • 43049126784 scopus 로고    scopus 로고
    • PTP1B and TC-PTP: Regulators of transformation and tumorigenesis
    • Stuible M, Doody K. M, & Tremblay M. L. PTP1B and TC-PTP: regulators of transformation and tumorigenesis. Cancer Metastasis Rev. 27, 215-230 (2008).
    • (2008) Cancer Metastasis Rev , vol.27 , pp. 215-230
    • Stuible, M.1    Doody, K.M.2    Tremblay, M.L.3
  • 17
    • 84877028141 scopus 로고    scopus 로고
    • Comprehensive molecular portraits of human breast tumours
    • Comprehensive molecular portraits of human breast tumours Nature 490 61-70 (2012).
    • (2012) Nature , vol.490 , pp. 61-70
  • 18
    • 0028327324 scopus 로고
    • Overexpression of the protein tyrosine phosphatase PTP1B in human breast cancer: Association with p185c-ERBB-2 protein expression
    • Wiener J. R, et al. Overexpression of the protein tyrosine phosphatase PTP1B in human breast cancer: association with p185c-erbB-2 protein expression. J. Natl Cancer Inst. 86, 372-378 (1994).
    • (1994) J. Natl Cancer Inst , vol.86 , pp. 372-378
    • Wiener, J.R.1
  • 19
    • 33847375227 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B is required for HER2/Neu-induced breast cancer
    • Bentires-Alj M, & Neel B. G. Protein-tyrosine phosphatase 1B is required for HER2/Neu-induced breast cancer. Cancer Res. 67, 2420-2424 (2007).
    • (2007) Cancer Res , vol.67 , pp. 2420-2424
    • Bentires-Alj, M.1    Neel, B.G.2
  • 20
    • 33847202286 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B deficiency or inhibition delays ErbB2-induced mammary tumorigenesis and protects from lung metastasis
    • Julien S. G, et al. Protein tyrosine phosphatase 1B deficiency or inhibition delays ErbB2-induced mammary tumorigenesis and protects from lung metastasis. Nat. Genet. 39, 338-346 (2007).
    • (2007) Nat. Genet , vol.39 , pp. 338-346
    • Julien, S.G.1
  • 21
    • 84969423577 scopus 로고    scopus 로고
    • Moyamoya disease: Epidemiology, clinical features, and diagnosis
    • Kim J. S. Moyamoya disease: epidemiology, clinical features, and diagnosis. J. Stroke 18, 2-11 (2016).
    • (2016) J. Stroke , vol.18 , pp. 2-11
    • Kim, J.S.1
  • 22
    • 84902852963 scopus 로고    scopus 로고
    • Targeting the disordered C terminus of PTP1B with an allosteric inhibitor
    • Krishnan N, et al. Targeting the disordered C terminus of PTP1B with an allosteric inhibitor. Nat. Chem. Biol. 10, 558-566 (2014).
    • (2014) Nat. Chem. Biol , vol.10 , pp. 558-566
    • Krishnan, N.1
  • 23
    • 80054715291 scopus 로고    scopus 로고
    • Epithelial protein-tyrosine phosphatase 1B contributes to the induction of mammary tumors by HER2/Neu but is not essential for tumor maintenance
    • Balavenkatraman K. K, et al. Epithelial protein-tyrosine phosphatase 1B contributes to the induction of mammary tumors by HER2/Neu but is not essential for tumor maintenance. Mol. Cancer Res. 9, 1377-1384 (2011).
    • (2011) Mol. Cancer Res , vol.9 , pp. 1377-1384
    • Balavenkatraman, K.K.1
  • 24
    • 3543017313 scopus 로고    scopus 로고
    • Allosteric inhibition of protein tyrosine phosphatase 1B
    • Wiesmann C, et al. Allosteric inhibition of protein tyrosine phosphatase 1B. Nat. Struct. Mol. Biol. 11, 730-737 (2004).
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 730-737
    • Wiesmann, C.1
  • 25
    • 84893852306 scopus 로고    scopus 로고
    • Metabolic changes in cancer cells upon suppression of MYC
    • Anso E, et al. Metabolic changes in cancer cells upon suppression of MYC. Cancer Metab. 1, 7 (2013).
    • (2013) Cancer Metab , vol.1 , pp. 7
    • Anso, E.1
  • 26
    • 19744373474 scopus 로고    scopus 로고
    • Selective inhibition of factor inhibiting hypoxia-inducible factor
    • McDonough M. A, et al. Selective inhibition of factor inhibiting hypoxia-inducible factor. J. Am. Chem. Soc. 127, 7680-7681 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 7680-7681
    • McDonough, M.A.1
  • 27
    • 84880534866 scopus 로고    scopus 로고
    • Selective small molecule probes for the hypoxia inducible factor (HIF) prolyl hydroxylases
    • Chowdhury R, et al. Selective small molecule probes for the hypoxia inducible factor (HIF) prolyl hydroxylases. ACS Chem. Biol. 8, 1488-1496 (2013).
    • (2013) ACS Chem. Biol , vol.8 , pp. 1488-1496
    • Chowdhury, R.1
  • 28
    • 77955790529 scopus 로고    scopus 로고
    • Prolyl hydroxylase domain-containing protein inhibitors as stabilizers of hypoxia-inducible factor: Small molecule-based therapeutics for anemia
    • Yan L, Colandrea V. J, & Hale J. J. Prolyl hydroxylase domain-containing protein inhibitors as stabilizers of hypoxia-inducible factor: small molecule-based therapeutics for anemia. Expert Opin. Ther. Pat. 20, 1219-1245 (2010).
    • (2010) Expert Opin. Ther. Pat , vol.20 , pp. 1219-1245
    • Yan, L.1    Colandrea, V.J.2    Hale, J.J.3
  • 29
    • 33846945811 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase function: The substrate perspective
    • Tiganis T, & Bennett A. M. Protein tyrosine phosphatase function: the substrate perspective. Biochem. J. 402, 1-15 (2007).
    • (2007) Biochem. J. , vol.402 , pp. 1-15
    • Tiganis, T.1    Bennett, A.M.2
  • 30
    • 0031055324 scopus 로고    scopus 로고
    • Development of substratetrapping mutants to identify physiological substrates of protein tyrosine phosphatases
    • Flint A. J, Tiganis T, Barford D, & Tonks N. K. Development of substratetrapping mutants to identify physiological substrates of protein tyrosine phosphatases. Proc. Natl Acad. Sci. USA 94, 1680-1685 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1680-1685
    • Flint, A.J.1    Tiganis, T.2    Barford, D.3    Tonks, N.K.4
  • 31
    • 52149083055 scopus 로고    scopus 로고
    • Met-driven invasive growth involves transcriptional regulation of Arhgap12
    • Gentile A, et al. Met-driven invasive growth involves transcriptional regulation of Arhgap12. Oncogene 27, 5590-5598 (2008).
    • (2008) Oncogene , vol.27 , pp. 5590-5598
    • Gentile, A.1
  • 32
    • 52649120850 scopus 로고    scopus 로고
    • Investigation of protein-tyrosine phosphatase 1B function by quantitative proteomics
    • Mertins P, et al. Investigation of protein-tyrosine phosphatase 1B function by quantitative proteomics. Mol. Cell. Proteomics 7, 1763-1777 (2008).
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1763-1777
    • Mertins, P.1
  • 33
    • 79960608326 scopus 로고    scopus 로고
    • Identification of RNF213 as a susceptibility gene for moyamoya disease and its possible role in vascular development
    • Liu W, et al. Identification of RNF213 as a susceptibility gene for moyamoya disease and its possible role in vascular development. PLoS ONE 6, e22542 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e22542
    • Liu, W.1
  • 34
    • 82455179484 scopus 로고    scopus 로고
    • Systematic and quantitative assessment of the ubiquitin-modified proteome
    • Kim W, et al. Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol. Cell 44, 325-340 (2011).
    • (2011) Mol. Cell , vol.44 , pp. 325-340
    • Kim, W.1
  • 35
    • 79958781143 scopus 로고    scopus 로고
    • Moyamoya disease: A review of histopathology, biochemistry, and genetics
    • Weinberg D. G, et al. Moyamoya disease: a review of histopathology, biochemistry, and genetics. Neurosurg. Focus 30, E20 (2011).
    • (2011) Neurosurg. Focus , vol.30 , pp. E20
    • Weinberg, D.G.1
  • 36
    • 0031965006 scopus 로고    scopus 로고
    • Moyamoya syndrome associated with congenital heart disease
    • Lutterman J, Scott M, Nass R, & Geva T. Moyamoya syndrome associated with congenital heart disease. Pediatrics 101, 57-60 (1998).
    • (1998) Pediatrics , vol.101 , pp. 57-60
    • Lutterman, J.1    Scott, M.2    Nass, R.3    Geva, T.4
  • 37
    • 84863922124 scopus 로고    scopus 로고
    • Comprehensive molecular characterization of human colon and rectal cancer
    • Comprehensive molecular characterization of human colon and rectal cancer Nature 487 330-337 (2012).
    • (2012) Nature , vol.487 , pp. 330-337
  • 38
    • 3543017313 scopus 로고    scopus 로고
    • Allosteric inhibition of protein tyrosine phosphatase 1B
    • Wiesmann C, et al. Allosteric inhibition of protein tyrosine phosphatase 1B. Nat. Struct. Mol. Biol. 11, 730-737 (2004).
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 730-737
    • Wiesmann, C.1
  • 39
    • 79960608326 scopus 로고    scopus 로고
    • Identification of RNF213 as a susceptibility gene for moyamoya disease and its possible role in vascular development
    • Liu W, et al. Identification of RNF213 as a susceptibility gene for moyamoya disease and its possible role in vascular development. PLoS ONE 6, e22542 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e22542
    • Liu, W.1
  • 40
    • 0025204095 scopus 로고
    • Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumour growth
    • Ingber D, et al. Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumour growth. Nature 348, 555-557 (1990).
    • (1990) Nature , vol.348 , pp. 555-557
    • Ingber, D.1
  • 41
    • 33847375227 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B is required for HER2/Neu-induced breast cancer
    • Bentires-Alj M, & Neel B. G. Protein-tyrosine phosphatase 1B is required for HER2/Neu-induced breast cancer. Cancer Res. 67, 2420-2424 (2007).
    • (2007) Cancer Res , vol.67 , pp. 2420-2424
    • Bentires-Alj, M.1    Neel, B.G.2
  • 42
    • 84887010498 scopus 로고    scopus 로고
    • Genome engineering using the CRISPR-Cas9 system
    • Ran F. A, et al. Genome engineering using the CRISPR-Cas9 system. Nat. Protocols 8, 2281-2308 (2013).
    • (2013) Nat. Protocols , vol.8 , pp. 2281-2308
    • Ran, F.A.1
  • 43
    • 69949124669 scopus 로고    scopus 로고
    • Hypoxia-induced expression of carbonic anhydrase 9 is dependent on the unfolded protein response
    • van den Beucken T, et al. Hypoxia-induced expression of carbonic anhydrase 9 is dependent on the unfolded protein response. J. Biol. Chem. 284, 24204-24212 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 24204-24212
    • Van Den Beucken, T.1
  • 44
    • 84884639800 scopus 로고    scopus 로고
    • Probing the hexosamine biosynthetic pathway in human tumor cells by multitargeted tandem mass spectrometry
    • Abdel Rahman A. M, Ryczko M, Pawling J, & Dennis J. W. Probing the hexosamine biosynthetic pathway in human tumor cells by multitargeted tandem mass spectrometry. ACS Chem. Biol. 8, 2053-2062 (2013).
    • (2013) ACS Chem. Biol , vol.8 , pp. 2053-2062
    • Abdel Rahman, A.M.1    Ryczko, M.2    Pawling, J.3    Dennis, J.W.4
  • 45
    • 84941137578 scopus 로고    scopus 로고
    • Golgi N-glycan branching Nacetylglucosaminyltransferases I, v and VI promote nutrient uptake and metabolism
    • Abdel Rahman A. M, et al. Golgi N-glycan branching Nacetylglucosaminyltransferases I, V and VI promote nutrient uptake and metabolism. Glycobiology 25, 225-240 (2015).
    • (2015) Glycobiology , vol.25 , pp. 225-240
    • Abdel Rahman, A.M.1
  • 46
    • 84908545013 scopus 로고    scopus 로고
    • Targeted metabolomics in cultured cells and tissues by mass spectrometry: Method development and validation
    • Abdel Rahman A. M, Pawling J, Ryczko M, Caudy A. A, & Dennis J. W. Targeted metabolomics in cultured cells and tissues by mass spectrometry: method development and validation. Anal. Chim. Acta 845, 53-61 (2014).
    • (2014) Anal. Chim. Acta , vol.845 , pp. 53-61
    • Abdel Rahman, A.M.1    Pawling, J.2    Ryczko, M.3    Caudy, A.A.4    Dennis, J.W.5
  • 47
    • 84868713216 scopus 로고    scopus 로고
    • Increased BRAF heterodimerization is the common pathogenic mechanism for noonan syndrome-Associated RAF1 mutants
    • Wu X, et al. Increased BRAF heterodimerization is the common pathogenic mechanism for noonan syndrome-Associated RAF1 mutants. Mol. Cell. Biol. 32, 3872-3890 (2012).
    • (2012) Mol. Cell. Biol , vol.32 , pp. 3872-3890
    • Wu, X.1
  • 48
    • 77149134353 scopus 로고    scopus 로고
    • Cancer-Associated metabolite 2-hydroxyglutarate accumulates in acute myelogenous leukemia with isocitrate dehydrogenase 1 and 2 mutations
    • Gross S, et al. Cancer-Associated metabolite 2-hydroxyglutarate accumulates in acute myelogenous leukemia with isocitrate dehydrogenase 1 and 2 mutations. J. Exp. Med. 207, 339-344 (2010).
    • (2010) J. Exp. Med , vol.207 , pp. 339-344
    • Gross, S.1
  • 49
    • 77649305610 scopus 로고    scopus 로고
    • The common feature of leukemia-Associated IDH1 and IDH2 mutations is a neomorphic enzyme activity converting -ketoglutarate to 2-hydroxyglutarate
    • Ward P. S, et al. The common feature of leukemia-Associated IDH1 and IDH2 mutations is a neomorphic enzyme activity converting -ketoglutarate to 2-hydroxyglutarate. Cancer Cell 17, 225-234 (2010).
    • (2010) Cancer Cell , vol.17 , pp. 225-234
    • Ward, P.S.1
  • 50
    • 84897370572 scopus 로고    scopus 로고
    • Indepth proteomic analyses of ovarian cancer cell line exosomes reveals differential enrichment of functional categories compared to the NCI 60 proteome
    • Sinha A, Ignatchenko V, Ignatchenko A, Mejia-Guerrero S, & Kislinger T. Indepth proteomic analyses of ovarian cancer cell line exosomes reveals differential enrichment of functional categories compared to the NCI 60 proteome. Biochem. Biophys. Res. Commun. 445, 694-701 (2014).
    • (2014) Biochem. Biophys. Res. Commun , vol.445 , pp. 694-701
    • Sinha, A.1    Ignatchenko, V.2    Ignatchenko, A.3    Mejia-Guerrero, S.4    Kislinger, T.5
  • 51
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized ppb-range mass accuracies and proteome-wide protein quantification
    • Cox J, & Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372 (2008).
    • (2008) Nat. Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 52
    • 84861151032 scopus 로고    scopus 로고
    • Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition
    • Udeshi N. D, et al. Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition. Mol. Cell. Proteomics 11, 148-159 (2012).
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 148-159
    • Udeshi, N.D.1
  • 53
    • 12444345515 scopus 로고    scopus 로고
    • Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • Thompson A, et al. Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS. Anal. Chem. 75, 1895-1904 (2003).
    • (2003) Anal. Chem , vol.75 , pp. 1895-1904
    • Thompson, A.1
  • 54
    • 84890470098 scopus 로고    scopus 로고
    • Novel parallelized quadrupole/linear ion trap/Orbitrap tribrid mass spectrometer improving proteome coverage and peptide identification rates
    • Senko M. W, et al. Novel parallelized quadrupole/linear ion trap/Orbitrap tribrid mass spectrometer improving proteome coverage and peptide identification rates. Anal. Chem. 85, 11710-11714 (2013).
    • (2013) Anal. Chem , vol.85 , pp. 11710-11714
    • Senko, M.W.1
  • 55
    • 80155124832 scopus 로고    scopus 로고
    • MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics
    • Ting L, Rad R, Gygi S. P, & Haas W. MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics. Nat. Methods 8, 937-940 (2011).
    • (2011) Nat. Methods , vol.8 , pp. 937-940
    • Ting, L.1    Rad, R.2    Gygi, S.P.3    Haas, W.4
  • 56
    • 84904325891 scopus 로고    scopus 로고
    • MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes
    • McAlister G. C, et al. MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes. Anal. Chem. 86, 7150-7158 (2014).
    • (2014) Anal. Chem , vol.86 , pp. 7150-7158
    • McAlister, G.C.1
  • 57
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng J. K, McCormack A. L, & Yates J. R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989 (1994).
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 58
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias J. E, & Gygi S. P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4, 207-214 (2007).
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 59
    • 78650466243 scopus 로고    scopus 로고
    • A tissue-specific atlas of mouse protein phosphorylation and expression
    • Huttlin E. L, et al. A tissue-specific atlas of mouse protein phosphorylation and expression. Cell 143 1174-1189 (2010).
    • (2010) Cell , vol.143 , pp. 1174-1189
    • Huttlin, E.L.1
  • 60
    • 0242490780 scopus 로고    scopus 로고
    • Cytoscape: A software environment for integrated models of biomolecular interaction networks
    • Shannon P, et al. Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res. 13, 2498-2504 (2003).
    • (2003) Genome Res , vol.13 , pp. 2498-2504
    • Shannon, P.1
  • 61
    • 24044440971 scopus 로고    scopus 로고
    • BiNGO: A Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks
    • Maere S, Heymans K, & Kuiper M. BiNGO: a Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks. Bioinformatics 21, 3448-3449 (2005).
    • (2005) Bioinformatics , vol.21 , pp. 3448-3449
    • Maere, S.1    Heymans, K.2    Kuiper, M.3
  • 62
    • 38049148026 scopus 로고    scopus 로고
    • DAVID Knowledgebase: A gene-centered database integrating heterogeneous gene annotation resources to facilitate high-throughput gene functional analysis
    • Sherman B. T, et al. DAVID Knowledgebase: a gene-centered database integrating heterogeneous gene annotation resources to facilitate high-throughput gene functional analysis. BMC Bioinformatics 8, 426 (2007).
    • (2007) BMC Bioinformatics , vol.8 , pp. 426
    • Sherman, B.T.1


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