메뉴 건너뛰기




Volumn 6, Issue 1, 2016, Pages

Lamina associated polypeptide 1 (LAP1) interactome and its functional features

Author keywords

Cytoscape; Database; GeneMANIA; GO terms enrichment analysis; Ingenuity pathway analysis; Inner nuclear membrane; Interactors; Lamina associated polypeptide; Network; Nuclear envelope

Indexed keywords

CELL MEMBRANES; CHROMOSOMES; DATABASE SYSTEMS; NETWORKS (CIRCUITS); PROTEINS;

EID: 84957541375     PISSN: None     EISSN: 20770375     Source Type: Journal    
DOI: 10.3390/membranes6010008     Document Type: Article
Times cited : (12)

References (91)
  • 1
    • 71549117899 scopus 로고    scopus 로고
    • The Nuclear Envelope as a Signaling Node in Development and Disease
    • [CrossRef] [PubMed]
    • Dauer, W.T.; Worman, H.J. The Nuclear Envelope as a Signaling Node in Development and Disease. Dev. Cell 2009, 17, 626–638. [CrossRef] [PubMed]
    • (2009) Dev. Cell , vol.17 , pp. 626-638
    • Dauer, W.T.1    Worman, H.J.2
  • 3
    • 84902465522 scopus 로고    scopus 로고
    • Functional architecture of the cell’s nucleus in development, aging, and disease
    • [PubMed]
    • Burke, B.; Stewart, C.L.: Functional architecture of the cell’s nucleus in development, aging, and disease. Curr. Top. Dev. Biol. 2014, 109, 1–52. [PubMed]
    • (2014) Curr. Top. Dev. Biol , vol.109 , pp. 1-52
    • Burke, B.1    Stewart, C.L.2
  • 4
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • [CrossRef] [PubMed]
    • Schirmer, E.C.; Florens, L.; Guan, T.; Yates, J.R.; Gerace, L. Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 2003, 301, 1380–1382. [CrossRef] [PubMed]
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates, J.R.4    Gerace, L.5
  • 5
    • 0024263203 scopus 로고
    • Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina
    • [CrossRef] [PubMed]
    • Senior, A.; Gerace, L. Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina. J. Cell Biol. 1988, 107, 2029–2036. [CrossRef] [PubMed]
    • (1988) J. Cell Biol , vol.107 , pp. 2029-2036
    • Senior, A.1    Gerace, L.2
  • 6
    • 0028949732 scopus 로고
    • CDNA cloning and characterization of lamina-associated polypeptide 1C (LAP1C), an integral protein of the inner nuclear membrane
    • [CrossRef] [PubMed]
    • Martin, L.; Crimaudo, C.; Gerace, L. cDNA cloning and characterization of lamina-associated polypeptide 1C (LAP1C), an integral protein of the inner nuclear membrane. J. Biol. Chem. 1995, 270, 8822–8828. [CrossRef] [PubMed]
    • (1995) J. Biol. Chem , vol.270 , pp. 8822-8828
    • Martin, L.1    Crimaudo, C.2    Gerace, L.3
  • 7
    • 0036290031 scopus 로고    scopus 로고
    • Molecular cloning of one isotype of human lamina-associated polypeptide 1s and a topological analysis using its deletion mutants. Biochem. Biophys. Res
    • [CrossRef]
    • Kondo, Y.; Kondoh, J.; Hayashi, D.; Ban, T.; Takagi, M.; Kamei, Y.; Tsuji, L.; Kim, J.; Yoneda, Y. Molecular cloning of one isotype of human lamina-associated polypeptide 1s and a topological analysis using its deletion mutants. Biochem. Biophys. Res. Commun. 2002, 294, 770–778. [CrossRef]
    • (2002) Commun , vol.294 , pp. 770-778
    • Kondo, Y.1    Kondoh, J.2    Hayashi, D.3    Ban, T.4    Takagi, M.5    Kamei, Y.6    Tsuji, L.7    Kim, J.8    Yoneda, Y.9
  • 9
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • [CrossRef]
    • Foisner, R.; Gerace, L. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 1993, 73, 1267–1279. [CrossRef]
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 10
    • 84855830585 scopus 로고    scopus 로고
    • Nuclear lamina at the crossroads of the cytoplasm and nucleus
    • [CrossRef] [PubMed]
    • Gerace, L.; Huber, M.D.: Nuclear lamina at the crossroads of the cytoplasm and nucleus. J. Struct. Biol. 2012, 177, 24–31. [CrossRef] [PubMed]
    • (2012) J. Struct. Biol , vol.177 , pp. 24-31
    • Gerace, L.1    Huber, M.D.2
  • 11
    • 15444374750 scopus 로고    scopus 로고
    • The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein
    • [CrossRef] [PubMed]
    • Goodchild, R.E.; Dauer, W.T. The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein. J. Cell Biol. 2005, 168, 855–862. [CrossRef] [PubMed]
    • (2005) J. Cell Biol , vol.168 , pp. 855-862
    • Goodchild, R.E.1    Dauer, W.T.2
  • 13
    • 1642290757 scopus 로고    scopus 로고
    • Aberrant Cellular Behavior of Mutant TorsinA Implicates Nuclear Envelope Dysfunction in DYT1 Dystonia
    • [CrossRef] [PubMed]
    • Gonzalez-Alegre, P. Aberrant Cellular Behavior of Mutant TorsinA Implicates Nuclear Envelope Dysfunction in DYT1 Dystonia. J. Neurosci. 2004, 24, 2593–2601. [CrossRef] [PubMed]
    • (2004) J. Neurosci , vol.24 , pp. 2593-2601
    • Gonzalez-Alegre, P.1
  • 14
    • 1642433201 scopus 로고    scopus 로고
    • Mislocalization to the nuclear envelope: An effect of the dystonia-causing torsinA mutation
    • [CrossRef] [PubMed]
    • Goodchild, R.E.; Dauer, W.T. Mislocalization to the nuclear envelope: An effect of the dystonia-causing torsinA mutation. Proc. Natl. Acad. Sci. USA 2004, 101, 847–852. [CrossRef] [PubMed]
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 847-852
    • Goodchild, R.E.1    Dauer, W.T.2
  • 15
    • 70350463845 scopus 로고    scopus 로고
    • Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion
    • [CrossRef] [PubMed]
    • Naismith, T.V.; Dalal, S.; Hanson, P.I. Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion. J. Biol. Chem. 2009, 284, 27866–27874. [CrossRef] [PubMed]
    • (2009) J. Biol. Chem , vol.284 , pp. 27866-27874
    • Naismith, T.V.1    Dalal, S.2    Hanson, P.I.3
  • 17
    • 84884729973 scopus 로고    scopus 로고
    • Lamina-associated Polypeptide-1 Interacts with the Muscular Dystrophy Protein Emerin and is Essential for Skeletal Muscle Maintenance
    • [CrossRef] [PubMed]
    • Shin, J.; Méndez-lópez, I.; Wang, Y.; Hays, A.P.; Tanji, K.; Lefkowitch, J.H.; Schulze, P.C.; Worman, H.J.; Dauer, W.T. Lamina-associated Polypeptide-1 Interacts with the Muscular Dystrophy Protein Emerin and is Essential for Skeletal Muscle Maintenance. Dev. Cell 2014, 26, 591–603. [CrossRef] [PubMed]
    • (2014) Dev. Cell , vol.26 , pp. 591-603
    • Shin, J.1    Méndez-López, I.2    Wang, Y.3    Hays, A.P.4    Tanji, K.5    Lefkowitch, J.H.6    Schulze, P.C.7    Worman, H.J.8    Dauer, W.T.9
  • 18
    • 0027985787 scopus 로고
    • Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy
    • [CrossRef] [PubMed]
    • Bione, S.; Maestrini, E.; Rivella, S.; Mancini, M.; Regis, S.; Romeo, G.; Toniolo, D. Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy. Nat. Genet. 1994, 8, 323–327. [CrossRef] [PubMed]
    • (1994) Nat. Genet , vol.8 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, S.3    Mancini, M.4    Regis, S.5    Romeo, G.6    Toniolo, D.7
  • 22
    • 84999410485 scopus 로고    scopus 로고
    • Mutation Research/Reviews in Mutation Research Genetic mutations strengthen functional association of LAP1 with DYT1 dystonia and muscular dystrophy
    • Rebelo, S.; Edgar, F.; Odete, A.B. Mutation Research/Reviews in Mutation Research Genetic mutations strengthen functional association of LAP1 with DYT1 dystonia and muscular dystrophy. Mutat. Res. Mutat. Res. 2015, 2–7.
    • (2015) Mutat. Res. Mutat. Res , pp. 2-7
    • Rebelo, S.1    Edgar, F.2    Odete, A.B.3
  • 23
    • 0242490780 scopus 로고    scopus 로고
    • Cytoscape: A Software Environment for Integrated Models of Biomolecular Interaction Networks
    • [CrossRef] [PubMed]
    • Shannon, P.; Markiel, A.; Ozier, O.; Baliga, N.S.; Wang, J.T.; Ramage, D.; Amin, N.; Schwikowski, B.; Ideker, T. Cytoscape: A Software Environment for Integrated Models of Biomolecular Interaction Networks. Genome Res. 2003, 13, 2498–2504. [CrossRef] [PubMed]
    • (2003) Genome Res , vol.13 , pp. 2498-2504
    • Shannon, P.1    Markiel, A.2    Ozier, O.3    Baliga, N.S.4    Wang, J.T.5    Ramage, D.6    Amin, N.7    Schwikowski, B.8    Ideker, T.9
  • 24
    • 84901601509 scopus 로고    scopus 로고
    • Lamina-associated polypeptide 1: Protein interactions and tissue-selective functions
    • [CrossRef] [PubMed]
    • Shin, J.-Y.; Dauer, W.T.; Worman, H.J. Lamina-associated polypeptide 1: Protein interactions and tissue-selective functions. Semin. Cell Dev. Biol. 2014, 29, 164–168. [CrossRef] [PubMed]
    • (2014) Semin. Cell Dev. Biol , vol.29 , pp. 164-168
    • Shin, J.-Y.1    Dauer, W.T.2    Worman, H.J.3
  • 26
    • 84864754639 scopus 로고    scopus 로고
    • Multiple myeloma-associated chromosomal translocation activates orphan snoRNA ACA11 to suppress oxidative stress
    • [CrossRef] [PubMed]
    • Chu, L.; Su, M.Y.; Maggi, L.B.; Lu, L.; Mullins, C.; Crosby, S.; Huang, G.; Chng, W.J.; Vij, R.; Tomasson, M.H. Multiple myeloma-associated chromosomal translocation activates orphan snoRNA ACA11 to suppress oxidative stress. J. Clin. Invest. 2012, 122, 2793–2806. [CrossRef] [PubMed]
    • (2012) J. Clin. Invest , vol.122 , pp. 2793-2806
    • Chu, L.1    Su, M.Y.2    Maggi, L.B.3    Lu, L.4    Mullins, C.5    Crosby, S.6    Huang, G.7    Chng, W.J.8    Vij, R.9    Tomasson, M.H.10
  • 28
    • 84864390283 scopus 로고    scopus 로고
    • The Interactome of the Human Respiratory Syncytial Virus NS1 Protein Highlights Multiple Effects on Host Cell Biology
    • [CrossRef] [PubMed]
    • Wu, W.; Tran, K.C.; Teng, M.N.; Heesom, K.J.; Matthews, D.A.; Barr, J.N.; Hiscox, J.A. The Interactome of the Human Respiratory Syncytial Virus NS1 Protein Highlights Multiple Effects on Host Cell Biology. J. Virol. 2012, 86, 7777–7789. [CrossRef] [PubMed]
    • (2012) J. Virol , vol.86 , pp. 7777-7789
    • Wu, W.1    Tran, K.C.2    Teng, M.N.3    Heesom, K.J.4    Matthews, D.A.5    Barr, J.N.6    Hiscox, J.A.7
  • 29
    • 0036256243 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 2B (LMP2B) co-localizes with LMP2A in perinuclear regions in transiently transfected cells
    • [CrossRef] [PubMed]
    • Lynch, D.T.; Zimmerman, J.S.; Rowe, D.T. Epstein-Barr virus latent membrane protein 2B (LMP2B) co-localizes with LMP2A in perinuclear regions in transiently transfected cells. J. Gen. Virol. 2002, 83, 1025–1035. [CrossRef] [PubMed]
    • (2002) J. Gen. Virol , vol.83 , pp. 1025-1035
    • Lynch, D.T.1    Zimmerman, J.S.2    Rowe, D.T.3
  • 36
    • 84901327080 scopus 로고    scopus 로고
    • Identifying biological pathways that underlie primordial short stature using network analysis
    • [CrossRef] [PubMed]
    • Hanson, D.; Stevens, A.; Murray, P.G.; Black, G.C.M.; Clayton, P.E. Identifying biological pathways that underlie primordial short stature using network analysis. J. Mol. Endocrinol. 2014, 52, 333–344. [CrossRef] [PubMed]
    • (2014) J. Mol. Endocrinol , vol.52 , pp. 333-344
    • Hanson, D.1    Stevens, A.2    Murray, P.G.3    Black, G.C.M.4    Clayton, P.E.5
  • 37
    • 84904118558 scopus 로고    scopus 로고
    • Proteomic Analysis of the Epidermal Growth Factor Receptor (EGFR) Interactome and Post-translational Modifications Associated with Receptor Endocytosis in Response to EGF and Stress
    • [CrossRef] [PubMed]
    • Tong, J.; Taylor, P.; Moran, M.F. Proteomic Analysis of the Epidermal Growth Factor Receptor (EGFR) Interactome and Post-translational Modifications Associated with Receptor Endocytosis in Response to EGF and Stress. Mol. Cell. Proteomics 2014, 13, 1644–1658. [CrossRef] [PubMed]
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 1644-1658
    • Tong, J.1    Taylor, P.2    Moran, M.F.3
  • 39
    • 78549252392 scopus 로고    scopus 로고
    • Identification of differential protein interactors of lamin A and progerin
    • [CrossRef] [PubMed]
    • Kubben, N.; Voncken, J.W.; Demmers, J.; Calis, C.; van Almen, G.; Pinto, Y.M.; Misteli, T. Identification of differential protein interactors of lamin A and progerin. Nucleus 2010, 1, 513–525. [CrossRef] [PubMed]
    • (2010) Nucleus , vol.1 , pp. 513-525
    • Kubben, N.1    Voncken, J.W.2    Demmers, J.3    Calis, C.4    Van Almen, G.5    Pinto, Y.M.6    Misteli, T.7
  • 40
    • 27744495042 scopus 로고    scopus 로고
    • Novel progerin-interactive partner proteins hnRNP E1, EGF, Mel 18, and UBC9 interact with lamin A/C
    • [CrossRef] [PubMed]
    • Zhong, N.; Radu, G.; Ju, W.; Brown, W.T. Novel progerin-interactive partner proteins hnRNP E1, EGF, Mel 18, and UBC9 interact with lamin A/C. Biochem. Biophys. Res. Commun. 2005, 338, 855–861. [CrossRef] [PubMed]
    • (2005) Biochem. Biophys. Res. Commun , vol.338 , pp. 855-861
    • Zhong, N.1    Radu, G.2    Ju, W.3    Brown, W.T.4
  • 41
    • 84860270506 scopus 로고    scopus 로고
    • A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells
    • [CrossRef] [PubMed]
    • Roux, K.J.; Kim, D.I.; Raida, M.; Burke, B. A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells. J. Cell Biol. 2012, 196, 801–810. [CrossRef] [PubMed]
    • (2012) J. Cell Biol , vol.196 , pp. 801-810
    • Roux, K.J.1    Kim, D.I.2    Raida, M.3    Burke, B.4
  • 42
    • 0030745846 scopus 로고    scopus 로고
    • The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles
    • [CrossRef] [PubMed]
    • Maison, C.; Pyrpasopoulou, A.; Theodoropoulos, P.A.; Georgatos, S.D. The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles. EMBO J. 1997, 16, 4839–4850. [CrossRef] [PubMed]
    • (1997) EMBO J , vol.16 , pp. 4839-4850
    • Maison, C.1    Pyrpasopoulou, A.2    Theodoropoulos, P.A.3    Georgatos, S.D.4
  • 44
    • 84898622052 scopus 로고    scopus 로고
    • Ribosomal protein s15 phosphorylation mediates LRRK2 neurodegeneration in Parkinson’s disease
    • [CrossRef] [PubMed]
    • Martin, I.; Kim, J.W.; Lee, B.D.; Kang, H.C.; Xu, J.-C.; Jia, H.; Stankowski, J.; Kim, M.-S.; Zhong, J.; Kumar, M.; et al. Ribosomal protein s15 phosphorylation mediates LRRK2 neurodegeneration in Parkinson’s disease. Cell 2014, 157, 472–485. [CrossRef] [PubMed]
    • (2014) Cell , vol.157 , pp. 472-485
    • Martin, I.1    Kim, J.W.2    Lee, B.D.3    Kang, H.C.4    Xu, J.-C.5    Jia, H.6    Stankowski, J.7    Kim, M.-S.8    Zhong, J.9    Kumar, M.10
  • 45
    • 84895947285 scopus 로고    scopus 로고
    • Systems wide mass spectrometric based linear motif screen to identify dominant in-vivo interacting proteins for the ubiquitin ligase MDM2
    • [CrossRef] [PubMed]
    • Nicholson, J.; Scherl, A.; Way, L.; Blackburn, E.A.; Walkinshaw, M.D.; Ball, K.L.; Hupp, T.R. A systems wide mass spectrometric based linear motif screen to identify dominant in-vivo interacting proteins for the ubiquitin ligase MDM2. Cell. Signal. 2014, 26, 1243–1257. [CrossRef] [PubMed]
    • (2014) Cell. Signal , vol.26 , pp. 1243-1257
    • Nicholson, J.1    Scherl, A.2    Way, L.3    Blackburn, E.A.4    Walkinshaw, M.D.5    Ball, K.L.6    Hupp, T.7
  • 50
    • 79953212976 scopus 로고    scopus 로고
    • Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells
    • [CrossRef] [PubMed]
    • Lee, O.-H.; Kim, H.; He, Q.; Baek, H.J.; Yang, D.; Chen, L.-Y.; Liang, J.; Chae, H.K.; Safari, A.; Liu, D.; et al. Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells. Mol. Cell. Proteomics 2011, 10, M110.001628. [CrossRef] [PubMed]
    • (2011) Mol. Cell. Proteomics , vol.10
    • Lee, O.-H.1    Kim, H.2    He, Q.3    Baek, H.J.4    Yang, D.5    Chen, L.-Y.6    Liang, J.7    Chae, H.K.8    Safari, A.9    Liu, D.10
  • 51
    • 78549234083 scopus 로고    scopus 로고
    • A unique redox-sensing sensor II motif in TorsinA plays a critical role in nucleotide and partner binding
    • [CrossRef] [PubMed]
    • Zhu, L.; Millen, L.; Mendoza, J.L.; Thomas, P.J. A unique redox-sensing sensor II motif in TorsinA plays a critical role in nucleotide and partner binding. J. Biol. Chem. 2010, 285, 37271–37280. [CrossRef] [PubMed]
    • (2010) J. Biol. Chem , vol.285 , pp. 37271-37280
    • Zhu, L.1    Millen, L.2    Mendoza, J.L.3    Thomas, P.J.4
  • 53
    • 77953090863 scopus 로고    scopus 로고
    • Molecular mechanism underlying the neural-specific defect in torsinA mutant mice
    • [CrossRef] [PubMed]
    • Kim, C.E.; Perez, A.; Perkins, G.; Ellisman, M.H.; Dauer, W.T. A molecular mechanism underlying the neural-specific defect in torsinA mutant mice. Proc. Natl. Acad. Sci. USA 2010, 107, 9861–9866. [CrossRef] [PubMed]
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 9861-9866
    • Kim, C.E.1    Perez, A.2    Perkins, G.3    Ellisman, M.H.4    Dauer, W.5
  • 55
    • 80054033461 scopus 로고    scopus 로고
    • Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles
    • [CrossRef] [PubMed]
    • Wagner, S.A.; Beli, P.; Weinert, B.T.; Nielsen, M.L.; Cox, J.; Mann, M.; Choudhary, C. A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles. Mol. Cell. Proteomics 2011, 10, M111.013284. [CrossRef] [PubMed]
    • (2011) Mol. Cell. Proteomics , vol.10
    • Wagner, S.A.1    Beli, P.2    Weinert, B.T.3    Nielsen, M.L.4    Cox, J.5    Mann, M.6    Choudhary, C.A.7
  • 60
    • 33645078104 scopus 로고    scopus 로고
    • Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics
    • [CrossRef] [PubMed]
    • Hewett, J.W.; Zeng, J.; Niland, B.P.; Bragg, D.C.; Breakefield, X.O.: Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics. Neurobiol. Dis. 2006, 22, 98–111. [CrossRef] [PubMed]
    • (2006) Neurobiol. Dis , vol.22 , pp. 98-111
    • Hewett, J.W.1    Zeng, J.2    Niland, B.P.3    Bragg, D.C.4    Breakefield, X.O.5
  • 62
    • 34249668426 scopus 로고    scopus 로고
    • Proteins that associate with lamins: Many faces, many functions
    • [CrossRef] [PubMed]
    • Schirmer, E.C.; Foisner, R. Proteins that associate with lamins: Many faces, many functions. Exp. Cell Res. 2007, 313, 2167–2179. [CrossRef] [PubMed]
    • (2007) Exp. Cell Res , vol.313 , pp. 2167-2179
    • Schirmer, E.C.1    Foisner, R.2
  • 63
    • 36049028674 scopus 로고    scopus 로고
    • P31comet blocks Mad2 activation through structural mimicry
    • [CrossRef] [PubMed]
    • Yang, M.; Li, B.; Tomchick, D.R.; Machius, M.; Rizo, J.; Yu, H.; Luo, X. p31comet blocks Mad2 activation through structural mimicry. Cell 2007, 131, 744–755. [CrossRef] [PubMed]
    • (2007) Cell , vol.131 , pp. 744-755
    • Yang, M.1    Li, B.2    Tomchick, D.R.3    Machius, M.4    Rizo, J.5    Yu, H.6    Luo, X.7
  • 64
    • 84862776998 scopus 로고    scopus 로고
    • Structure of the mitotic checkpoint complex
    • [CrossRef] [PubMed]
    • Chao, W.C.H.; Kulkarni, K.; Zhang, Z.; Kong, E.H.; Barford, D. Structure of the mitotic checkpoint complex. Nature 2012, 484, 208–213. [CrossRef] [PubMed]
    • (2012) Nature , vol.484 , pp. 208-213
    • Chao, W.C.H.1    Kulkarni, K.2    Zhang, Z.3    Kong, E.H.4    Barford, D.5
  • 65
    • 84916889629 scopus 로고    scopus 로고
    • LAP1 is a crucial protein for the maintenance of the nuclear envelope structure and cell cycle progression
    • [CrossRef] [PubMed]
    • Santos, M.; Costa, P.; Martins, F.; da Cruz e Silva, E.F.; da Cruz e Silva, O.A.B.; Rebelo, S. LAP1 is a crucial protein for the maintenance of the nuclear envelope structure and cell cycle progression. Mol. Cell. Biochem. 2015, 399, 143–153. [CrossRef] [PubMed]
    • (2015) Mol. Cell. Biochem , vol.399 , pp. 143-153
    • Santos, M.1    Costa, P.2    Martins, F.3    Da Cruz E Silva, E.F.4    Cruz E Silva, O.5    Rebelo, S.6
  • 68
    • 40349092941 scopus 로고    scopus 로고
    • Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates
    • [CrossRef] [PubMed]
    • Blethrow, J.D.; Glavy, J.S.; Morgan, D.O.; Shokat, K.M. Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates. Proc. Natl. Acad. Sci. USA 2008, 105, 1442–1447. [CrossRef] [PubMed]
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1442-1447
    • Blethrow, J.D.1    Glavy, J.S.2    Morgan, D.O.3    Shokat, K.M.4
  • 69
    • 67749093100 scopus 로고    scopus 로고
    • Ultraviolet Irradiation-Induces Epidermal Growth Factor Receptor (EGFR) Nuclear Translocation in Human Keratinocytes
    • [CrossRef] [PubMed]
    • Xu, Y.; Shao, Y.; Voorhees, J.J.; Fisher, G.J. Ultraviolet Irradiation-Induces Epidermal Growth Factor Receptor (EGFR) Nuclear Translocation in Human Keratinocytes. J. Cell. Biochem. 2009, 107, 873–880. [CrossRef] [PubMed]
    • (2009) J. Cell. Biochem , vol.107 , pp. 873-880
    • Xu, Y.1    Shao, Y.2    Voorhees, J.J.3    Fisher, G.J.4
  • 70
    • 24944460598 scopus 로고    scopus 로고
    • The protein complex that shapes and safeguards human telomeres
    • [CrossRef] [PubMed]
    • De Lange, T. Shelterin: The protein complex that shapes and safeguards human telomeres. Genes Dev. 2005, 19, 2100–2110. [CrossRef] [PubMed]
    • (2005) Genes Dev , vol.19 , pp. 2100-2110
    • De, L.1    Shelterin, T.2
  • 71
    • 3543064379 scopus 로고    scopus 로고
    • Human Rif1, ortholog of a yeast telomeric protein, is regulated by ATM and 53BP1 and functions in the S-phase checkpoint
    • [CrossRef] [PubMed]
    • Silverman, J.; Takai, H.; Buonomo, S.B.C.; Eisenhaber, F.; de Lange, T. Human Rif1, ortholog of a yeast telomeric protein, is regulated by ATM and 53BP1 and functions in the S-phase checkpoint. Genes Dev. 2004, 18, 2108–2019. [CrossRef] [PubMed]
    • (2004) Genes Dev , vol.18 , pp. 2019-2108
    • Silverman, J.1    Takai, H.2    Buonomo, S.B.C.3    Eisenhaber, F.4    De Lange, T.5
  • 72
    • 84930719986 scopus 로고    scopus 로고
    • Lamins: Nuclear Intermediate Filament Proteins with Fundamental Functions in Nuclear Mechanics and Genome Regulation. Annu
    • [CrossRef] [PubMed]
    • Gruenbaum, Y.; Foisner, R. Lamins: Nuclear Intermediate Filament Proteins with Fundamental Functions in Nuclear Mechanics and Genome Regulation. Annu. Rev. Biochem. 2015, 84, 131–164. [CrossRef] [PubMed]
    • (2015) Rev. Biochem , vol.84 , pp. 131-164
    • Gruenbaum, Y.1    Foisner, R.2
  • 73
    • 84946735654 scopus 로고    scopus 로고
    • Gene Ontology Consortium: Going forward
    • Gene, T.; Consortium, O.; Gene, T.; Go, O. Gene Ontology Consortium: Going forward. Nucleic Acids Res. 2015, 43, D1049–D1056.
    • (2015) Nucleic Acids Res , vol.43 , pp. D1049-D1056
    • Gene, T.1    Consortium, O.2    Gene, T.3    Go, O.4
  • 74
    • 24044440971 scopus 로고    scopus 로고
    • BiNGO: A Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks
    • [CrossRef] [PubMed]
    • Maere, S.; Heymans, K.; Kuiper, M. BiNGO: A Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks. Bioinformatics 2005, 21, 3448–3449. [CrossRef] [PubMed]
    • (2005) Bioinformatics , vol.21 , pp. 3448-3449
    • Maere, S.1    Heymans, K.2    Kuiper, M.3
  • 75
    • 85043206241 scopus 로고    scopus 로고
    • Gene Ontology Consortium, accessed on 23 October 2015
    • Gene Ontology Consortium. Available online: http://geneontology.org/ (accessed on 23 October 2015).
  • 76
    • 84874969184 scopus 로고    scopus 로고
    • PANTHER in 2013: Modeling the evolution of gene function, and other gene attributes, in the context of phylogenetic trees
    • [CrossRef] [PubMed]
    • Mi, H.; Muruganujan, A.; Thomas, P.D. PANTHER in 2013: Modeling the evolution of gene function, and other gene attributes, in the context of phylogenetic trees. Nucleic Acids Res. 2013, 41, D377–D386. [CrossRef] [PubMed]
    • (2013) Nucleic Acids Res , vol.41 , pp. D377-D386
    • Mi, H.1    Muruganujan, A.2    Thomas, P.D.3
  • 78
    • 33644873184 scopus 로고    scopus 로고
    • BioGRID: A general repository for interaction datasets
    • [CrossRef] [PubMed]
    • Stark, C. BioGRID: A general repository for interaction datasets. Nucleic Acids Res. 2006, 34, D535–D539. [CrossRef] [PubMed]
    • (2006) Nucleic Acids Res , vol.34 , pp. D535-D539
    • Stark, C.1
  • 80
    • 84881455143 scopus 로고    scopus 로고
    • Mentha: A Resource for Browsing Integrated Protein-Interaction Networks
    • [CrossRef] [PubMed]
    • Calderone, A.; Castagnoli, L.; Cesareni, G. Mentha: A Resource for Browsing Integrated Protein-Interaction Networks. Nat. Methods 2013, 10, 690–691. [CrossRef] [PubMed]
    • (2013) Nat. Methods , vol.10 , pp. 690-691
    • Calderone, A.1    Castagnoli, L.2    Cesareni, G.3
  • 81
    • 18744376914 scopus 로고    scopus 로고
    • Online Predicted Human Interaction Database
    • [CrossRef] [PubMed]
    • Brown, K.R.; Jurisica, I. Online Predicted Human Interaction Database. Bioinformatics 2005, 21, 2076–2082. [CrossRef] [PubMed]
    • (2005) Bioinformatics , vol.21 , pp. 2076-2082
    • Brown, K.R.1    Jurisica, I.2
  • 82
    • 33747853260 scopus 로고    scopus 로고
    • APID: Agile Protein Interaction DataAnalyzer
    • [CrossRef] [PubMed]
    • Prieto, C.; De Las Rivas, J. APID: Agile Protein Interaction DataAnalyzer. Nucleic Acids Res. 2006, 34, W298–W302. [CrossRef] [PubMed]
    • (2006) Nucleic Acids Res , vol.34 , pp. W298-W302
    • Prieto, C.1    De Las Rivas, J.2
  • 83
    • 84856918212 scopus 로고    scopus 로고
    • Hippie: Integrating protein interaction networks with experiment based quality scores
    • [CrossRef] [PubMed]
    • Schaefer, M.H.; Fontaine, J.F.; Vinayagam, A.; Porras, P.; Wanker, E.E.; Andrade-Navarro, M.A. Hippie: Integrating protein interaction networks with experiment based quality scores. PLoS ONE 2012, 7, 1–8. [CrossRef] [PubMed]
    • (2012) Plos ONE , vol.7 , pp. 1-8
    • Schaefer, M.H.1    Fontaine, J.F.2    Vinayagam, A.3    Porras, P.4    Wanker, E.E.5    Andrade-Navarro, M.A.6
  • 84
    • 33846056843 scopus 로고    scopus 로고
    • Entrez gene: Gene-centered information at NCBI
    • [CrossRef] [PubMed]
    • Maglott, D.; Ostell, J.; Pruitt, K.D.; Tatusova, T. Entrez gene: Gene-centered information at NCBI. Nucleic Acids Res. 2007, 35, D26–D31. [CrossRef] [PubMed]
    • (2007) Nucleic Acids Res , vol.35 , pp. D26-D31
    • Maglott, D.1    Ostell, J.2    Pruitt, K.D.3    Tatusova, T.4
  • 87
    • 85043161408 scopus 로고    scopus 로고
    • Cytoscape Consortium, accessed on 23 October 2015
    • Cytoscape Consortium. Available online: http://www.cytoscape.org/ (accessed on 23 October 2015).
  • 88
    • 85043169978 scopus 로고    scopus 로고
    • GeneMANIA Cytoscape plugin, accessed on 23 October 2015
    • GeneMANIA Cytoscape plugin. Available online: http://apps.cytoscape.org/apps/genemania (accessed on 23 October 2015).
  • 89
    • 77954269901 scopus 로고    scopus 로고
    • The GeneMANIA prediction server: Biological network integration for gene prioritization and predicting gene function
    • [CrossRef] [PubMed]
    • Warde-Farley, D.; Donaldson, S.L.; Comes, O.; Zuberi, K.; Badrawi, R.; Chao, P.; Franz, M.; Grouios, C.; Kazi, F.; Lopes, C.T. et al. The GeneMANIA prediction server: Biological network integration for gene prioritization and predicting gene function. Nucleic Acids Res. 2010, 38, W214–W220. [CrossRef] [PubMed]
    • (2010) Nucleic Acids Res , vol.38 , pp. W214-W220
    • Warde-Farley, D.1    Donaldson, S.L.2    Comes, O.3    Zuberi, K.4    Badrawi, R.5    Chao, P.6    Franz, M.7    Grouios, C.8    Kazi, F.9    Lopes, C.T.10
  • 90
    • 85043200015 scopus 로고    scopus 로고
    • accessed on 23 October 2015
    • Maere, S. BiNGO Cytoscape plugin. Available online: http://apps.cytoscape.org/apps/bingo (accessed on 23 October 2015).
    • Bingo Cytoscape Plugin
    • Maere, S.1
  • 91
    • 85043160291 scopus 로고    scopus 로고
    • QIAGEN Ingenuity Pathway Analysis, accessed on 23 October 2015
    • QIAGEN Ingenuity Pathway Analysis. Available online: www.qiagen.com/ingenuity (accessed on 23 October 2015).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.