메뉴 건너뛰기




Volumn 290, Issue 46, 2015, Pages 27533-27544

The regulatory domain of squalene monooxygenase contains a re-entrant loop and senses cholesterol via a conformational change

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; CHEMICAL REACTIONS; CONFORMATIONS; TOPOLOGY;

EID: 84946925425     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.675181     Document Type: Article
Times cited : (40)

References (57)
  • 1
    • 79952174597 scopus 로고    scopus 로고
    • Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase
    • Gill, S., Stevenson, J., Kristiana, I., and Brown, A. J. (2011) Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase. Cell Metab. 13, 260-273
    • (2011) Cell Metab. , vol.13 , pp. 260-273
    • Gill, S.1    Stevenson, J.2    Kristiana, I.3    Brown, A.J.4
  • 2
    • 0346101770 scopus 로고    scopus 로고
    • Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3-methylglutaryl-coa reductase stimulated by sterols and geranylgeraniol
    • Sever, N., and Song, B. L., Yabe, D., Goldstein, J. L., and Brown, M. S., and DeBose-Boyd, R. A. (2003) Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3-methylglutaryl-CoA reductase stimulated by sterols and geranylgeraniol. J. Biol. Chem. 278, 52479-52490
    • (2003) J. Biol. Chem. , vol.278 , pp. 52479-52490
    • Sever, N.1    Song, B.L.2    Yabe, D.3    Goldstein, J.L.4    Brown, M.S.5    DeBose-Boyd, R.A.6
  • 4
    • 18544378347 scopus 로고    scopus 로고
    • Insig-mediated degradation of HMG CoA reductase stimulatedby lanosterol, an intermediate in the synthesis of cholesterol
    • Song, B.-L., Javitt, N. B., and DeBose-Boyd, R. A. (2005) Insig-mediated degradation of HMG CoA reductase stimulatedby lanosterol, an intermediate in the synthesis of cholesterol. Cell Metab. 1, 179-189
    • (2005) Cell Metab. , vol.1 , pp. 179-189
    • Song, B.-L.1    Javitt, N.B.2    DeBose-Boyd, R.A.3
  • 5
    • 84880707873 scopus 로고    scopus 로고
    • Sterol homeostasis requires regulated degradation of squalene monooxygenase by the ubiquitin ligase doa10/Teb4
    • Foresti, O., Ruggiano, A., Hannibal-Bach, H. K., Ejsing, C. S., and Carvalho, P. (2013) Sterol homeostasis requires regulated degradation of squalene monooxygenase by the ubiquitin ligase Doa10/Teb4. Elife 2, e00953
    • (2013) Elife , vol.2
    • Foresti, O.1    Ruggiano, A.2    Hannibal-Bach, H.K.3    Ejsing, C.S.4    Carvalho, P.5
  • 6
    • 84895820661 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase MARCH6 degrades squalene monooxygenase and affects 3-hydroxy-3-methyl-glutaryl coenzyme A reductase and the cholesterol synthesis pathway
    • Zelcer, N., and Sharpe, L. J., Loregger, A., Kristiana, I., Cook, E. C., Phan, L., Stevenson, J., and Brown, A. J. (2014) The E3 ubiquitin ligase MARCH6 degrades squalene monooxygenase and affects 3-hydroxy-3-methyl-glutaryl coenzyme A reductase and the cholesterol synthesis pathway. Mol. Cell. Biol. 34, 1262-1270
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 1262-1270
    • Zelcer, N.1    Sharpe, L.J.2    Loregger, A.3    Kristiana, I.4    Cook, E.C.5    Phan, L.6    Stevenson, J.7    Brown, A.J.8
  • 7
    • 84874644958 scopus 로고    scopus 로고
    • Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells
    • Hulce, J. J., and Cognetta, A. B., Niphakis, M. J., Tully, S. E., and Cravatt, B. F. (2013) Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells. Nat. Methods 10, 259-264
    • (2013) Nat. Methods , vol.10 , pp. 259-264
    • Hulce, J.J.1    Cognetta, A.B.2    Niphakis, M.J.3    Tully, S.E.4    Cravatt, B.F.5
  • 10
    • 0034971386 scopus 로고    scopus 로고
    • In vivo action of the HRD ubiquitin ligase complex: Mechanisms of endoplasmic reticulum quality control and sterol regulation
    • Gardner, R. G., and Shearer, A. G., and Hampton, R. Y. (2001) In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation. Mol. Cell. Biol. 21, 4276-4291
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4276-4291
    • Gardner, R.G.1    Shearer, A.G.2    Hampton, R.Y.3
  • 12
    • 0036792050 scopus 로고    scopus 로고
    • Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins
    • Yabe, D., and Brown, M. S., and Goldstein, J. L. (2002) Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins. Proc. Natl. Acad. Sci. U.S.A. 99, 12753-12758
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12753-12758
    • Yabe, D.1    Brown, M.S.2    Goldstein, J.L.3
  • 13
    • 84893498225 scopus 로고    scopus 로고
    • A practical comparison of ligation-independent cloning techniques
    • Stevenson, J., and Krycer, J. R., Phan, L., and Brown, A. J. (2013) A practical comparison of ligation-independent cloning techniques. PLoS One 8, e83888
    • (2013) PLoS One , vol.8
    • Stevenson, J.1    Krycer, J.R.2    Phan, L.3    Brown, A.J.4
  • 14
    • 41149148236 scopus 로고    scopus 로고
    • Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts
    • Klock, H. E., and Koesema, E. J., Knuth, M. W., and Lesley, S. A. (2008) Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts. Proteins Struct. Funct. Genet. 71, 982-994
    • (2008) Proteins Struct. Funct. Genet. , vol.71 , pp. 982-994
    • Klock, H.E.1    Koesema, E.J.2    Knuth, M.W.3    Lesley, S.A.4
  • 16
    • 0036671360 scopus 로고    scopus 로고
    • Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism
    • Brown, A. J., Sun, L., Feramisco, J. D., and Brown, M. S., and Goldstein, J. L. (2002) Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism. Mol. Cell 10, 237-245
    • (2002) Mol. Cell , vol.10 , pp. 237-245
    • Brown, A.J.1    Sun, L.2    Feramisco, J.D.3    Brown, M.S.4    Goldstein, J.L.5
  • 17
    • 84897497834 scopus 로고    scopus 로고
    • DHCR24 associates strongly with the endoplasmic reticulum beyond predicted membrane domains: Implications for the activities of this multi-functional enzyme
    • Zerenturk, E. J., and Sharpe, L. J., and Brown, A. J. (2014) DHCR24 associates strongly with the endoplasmic reticulum beyond predicted membrane domains: implications for the activities of this multi-functional enzyme. Biosci. Rep. 34, 107-118
    • (2014) Biosci. Rep. , vol.34 , pp. 107-118
    • Zerenturk, E.J.1    Sharpe, L.J.2    Brown, A.J.3
  • 18
    • 1542379024 scopus 로고    scopus 로고
    • Membrane topology of human insig-1, a protein regulator of lipid synthesis
    • Feramisco, J. D., and Goldstein, J. L., and Brown, M. S. (2004) Membrane topology of human insig-1, a protein regulator of lipid synthesis. J. Biol. Chem. 279, 8487-8496
    • (2004) J. Biol. Chem. , vol.279 , pp. 8487-8496
    • Feramisco, J.D.1    Goldstein, J.L.2    Brown, M.S.3
  • 19
    • 34249861927 scopus 로고    scopus 로고
    • Sterolregulated transport of SREBPs from endoplasmic reticulum to golgi: Insig renders sorting signal in scap inaccessible to COPII proteins
    • Sun, L.-P., Seemann, J., and Goldstein, J. L., and Brown, M. S. (2007) Sterolregulated transport of SREBPs from endoplasmic reticulum to Golgi: Insig renders sorting signal in Scap inaccessible to COPII proteins. Proc. Natl. Acad. Sci. U.S.A. 104, 6519-6526
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 6519-6526
    • Sun, L.-P.1    Seemann, J.2    Goldstein, J.L.3    Brown, M.S.4
  • 20
    • 51049099817 scopus 로고    scopus 로고
    • Analysis of the membrane topology of transmembrane segments in the C-terminal hydrophobic domain of the yeast vacuolar ATPase subunit a (Vph1p) by chemical modification
    • Wang, Y., Toei, M., and Forgac, M. (2008) Analysis of the membrane topology of transmembrane segments in the C-terminal hydrophobic domain of the yeast vacuolar ATPase subunit a (Vph1p) by chemical modification. J. Biol. Chem. 283, 20696-20702
    • (2008) J. Biol. Chem. , vol.283 , pp. 20696-20702
    • Wang, Y.1    Toei, M.2    Forgac, M.3
  • 21
    • 0030854859 scopus 로고    scopus 로고
    • Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein
    • Sakai, J., Nohturfft, A., Cheng, D., Ho, Y. K., and Brown, M. S., and Goldstein, J. L. (1997) Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein. J. Biol. Chem. 272, 20213-20221
    • (1997) J. Biol. Chem. , vol.272 , pp. 20213-20221
    • Sakai, J.1    Nohturfft, A.2    Cheng, D.3    Ho, Y.K.4    Brown, M.S.5    Goldstein, J.L.6
  • 22
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.2
  • 23
    • 0036557845 scopus 로고    scopus 로고
    • Basic charge clusters and predictions of membrane protein topology
    • Juretić, D., Zoranić, L., and Zucić, D. (2002) Basic charge clusters and predictions of membrane protein topology. J. Chem. Inf. Comput. Sci. 42, 620-632
    • (2002) J. Chem. Inf. Comput. Sci. , vol.42 , pp. 620-632
    • Juretić, D.1    Zoranić, L.2    Zucić, D.3
  • 24
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305, 567-580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 25
    • 34047151404 scopus 로고    scopus 로고
    • Improving the accuracy of transmembrane protein topology prediction using evolutionary information
    • Jones, D. T. (2007) Improving the accuracy of transmembrane protein topology prediction using evolutionary information. Bioinformatics 23, 538-544
    • (2007) Bioinformatics , vol.23 , pp. 538-544
    • Jones, D.T.1
  • 26
    • 84866158866 scopus 로고    scopus 로고
    • Detecting pore-lining regions in transmembrane protein sequences
    • Nugent, T., and Jones, D. T. (2012) Detecting pore-lining regions in transmembrane protein sequences. BMC Bioinformatics 13, 169
    • (2012) BMC Bioinformatics , vol.13 , pp. 169
    • Nugent, T.1    Jones, D.T.2
  • 28
    • 84979862598 scopus 로고    scopus 로고
    • The TOPCONS web server for consensus prediction of membrane protein topology and signal peptides
    • Tsirigos, K. D., Peters, C., Shu, N., Käll, L., and Elofsson, A. (2015) The TOPCONS web server for consensus prediction of membrane protein topology and signal peptides. Nucleic Acids Res. 43, W401-W407
    • (2015) Nucleic Acids Res. , vol.43 , pp. W401-W407
    • Tsirigos, K.D.1    Peters, C.2    Shu, N.3    Käll, L.4    Elofsson, A.5
  • 30
    • 2942564436 scopus 로고    scopus 로고
    • N-terminal myristoylation predictions by ensembles of neural networks
    • Bologna, G., Yvon, C., Duvaud, S., and Veuthey, A. L. (2004) N-terminal myristoylation predictions by ensembles of neural networks. Proteomics 4, 1626-1632
    • (2004) Proteomics , vol.4 , pp. 1626-1632
    • Bologna, G.1    Yvon, C.2    Duvaud, S.3    Veuthey, A.L.4
  • 31
    • 0036290648 scopus 로고    scopus 로고
    • N-terminal N-myristoylation of proteins: Prediction of substrate proteins from amino acid sequence
    • Maurer-Stroh, S., Eisenhaber, B., and Eisenhaber, F. (2002) N-terminal N-myristoylation of proteins: prediction of substrate proteins from amino acid sequence. J. Mol. Biol. 317, 541-557
    • (2002) J. Mol. Biol. , vol.317 , pp. 541-557
    • Maurer-Stroh, S.1    Eisenhaber, B.2    Eisenhaber, F.3
  • 32
    • 0032409445 scopus 로고    scopus 로고
    • Sequence properties of GPI-anchored proteins near the ω-site: Constraints for the polypeptide binding site of the putative transamidase
    • Eisenhaber, B., Bork, P., and Eisenhaber, F. (1998) Sequence properties of GPI-anchored proteins near the ω-site: constraints for the polypeptide binding site of the putative transamidase. Protein Eng 11, 1155-1161
    • (1998) Protein Eng , vol.11 , pp. 1155-1161
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 33
    • 33646366606 scopus 로고    scopus 로고
    • Refinement and prediction of protein prenylation motifs
    • Maurer-Stroh, S., and Eisenhaber, F. (2005) Refinement and prediction of protein prenylation motifs. Genome Biol. 6, R55
    • (2005) Genome Biol. , vol.6 , pp. R55
    • Maurer-Stroh, S.1    Eisenhaber, F.2
  • 34
    • 54249148026 scopus 로고    scopus 로고
    • CSS-palm 2.0: An updated software for palmitoylation sites prediction
    • Ren, J., Wen, L., Gao, X., Jin, C., Xue, Y., and Yao, X. (2008) CSS-Palm 2.0: an updated software for palmitoylation sites prediction. Protein Eng. Des. Sel. 21, 639-644
    • (2008) Protein Eng. Des. Sel. , vol.21 , pp. 639-644
    • Ren, J.1    Wen, L.2    Gao, X.3    Jin, C.4    Xue, Y.5    Yao, X.6
  • 35
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. (1999) Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292, 195-202
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 36
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., and Hubbard, A. L., Fowler, S., and Lazarow, P. B. (1982) Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93, 97-102
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 37
    • 4944242989 scopus 로고    scopus 로고
    • An ENSEMBLE machine learning approach for the prediction of all-α membrane proteins
    • Martelli, P. L., Fariselli, P., and Casadio, R. (2003) An ENSEMBLE machine learning approach for the prediction of all-α membrane proteins. Bioinformatics 19, Suppl. 1, i205-i211
    • (2003) Bioinformatics , vol.19 , pp. i205-i211
    • Martelli, P.L.1    Fariselli, P.2    Casadio, R.3
  • 38
    • 48249151108 scopus 로고    scopus 로고
    • OCTOPUS: Improving topology prediction by two-track ANN-based preference scores and an extended topological grammar
    • Viklund, H., and Elofsson, A. (2008) OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar. Bioinformatics 24, 1662-1668
    • (2008) Bioinformatics , vol.24 , pp. 1662-1668
    • Viklund, H.1    Elofsson, A.2
  • 40
    • 79953745092 scopus 로고    scopus 로고
    • Superfolder GFP is fluorescent in oxidising environments when targeted via the sec translocon
    • Aronson, D. E., and Costantini, L. M., and Snapp, E. L. (2011) Superfolder GFP is fluorescent in oxidising environments when targeted via the sec translocon. Traffic 12, 543-548
    • (2011) Traffic , vol.12 , pp. 543-548
    • Aronson, D.E.1    Costantini, L.M.2    Snapp, E.L.3
  • 41
    • 0023548717 scopus 로고
    • Lipid fluidity and membrane protein dynamics
    • Lenaz, G. (1987) Lipid fluidity and membrane protein dynamics. Biosci. Rep. 7, 823-837
    • (1987) Biosci. Rep. , vol.7 , pp. 823-837
    • Lenaz, G.1
  • 42
    • 0031713885 scopus 로고    scopus 로고
    • Sequence determinants for regulated degradation of yeast 3-hydroxy-3-methylglutaryl-coa reductase, an integral endoplasmic reticulum membrane protein
    • Gardner, R., Cronin, S., Leader, B., Rine, J., Hampton, R., and Leder, B. (1998) Sequence determinants for regulated degradation of yeast 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 9, 2611-2626
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2611-2626
    • Gardner, R.1    Cronin, S.2    Leader, B.3    Rine, J.4    Hampton, R.5    Leder, B.6
  • 43
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures?
    • Gekko, K., and Timasheff, S. (1981) Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures? Biochemistry 20, 4667-4676
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.2
  • 44
    • 72749102457 scopus 로고    scopus 로고
    • Mechanisms of protein stabilization and prevention of protein aggregation by glycerol
    • Vagenende, V., and Yap, M. G., and Trout, B. L. (2009) Mechanisms of protein stabilization and prevention of protein aggregation by glycerol. Biochemistry 48, 11084-11096
    • (2009) Biochemistry , vol.48 , pp. 11084-11096
    • Vagenende, V.1    Yap, M.G.2    Trout, B.L.3
  • 45
    • 0028839090 scopus 로고
    • Molecular cloning and expression of rat squalene epoxidase
    • Sakakibara, J., Watanabe, R., Kanai, Y., and Ono, T. (1995) Molecular cloning and expression of rat squalene epoxidase. J. Biol. Chem. 270, 17-20
    • (1995) J. Biol. Chem. , vol.270 , pp. 17-20
    • Sakakibara, J.1    Watanabe, R.2    Kanai, Y.3    Ono, T.4
  • 46
    • 33746361201 scopus 로고    scopus 로고
    • Structural classification and prediction of reentrant regions in α-helical transmembrane proteins: Application to complete genomes
    • Viklund, H., Granseth, E., and Elofsson, A. (2006) Structural classification and prediction of reentrant regions in α-helical transmembrane proteins: application to complete genomes. J. Mol. Biol. 361, 591-603
    • (2006) J. Mol. Biol. , vol.361 , pp. 591-603
    • Viklund, H.1    Granseth, E.2    Elofsson, A.3
  • 47
    • 85027922406 scopus 로고    scopus 로고
    • An analysis of reentrant loops
    • Yan, C., and Luo, J. (2010) An analysis of reentrant loops. Protein J. 29, 350-354
    • (2010) Protein J. , vol.29 , pp. 350-354
    • Yan, C.1    Luo, J.2
  • 48
    • 84924769665 scopus 로고    scopus 로고
    • Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway
    • Park, S.-E., Kim, J.-M., Seok, O.-H., Cho, H., Wadas, B., Kim, S.-Y., Varshavsky, A., and Hwang, C.-S. (2015) Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway. Science 347, 1249-1252
    • (2015) Science , vol.347 , pp. 1249-1252
    • Park, S.-E.1    Kim, J.-M.2    Seok, O.-H.3    Cho, H.4    Wadas, B.5    Kim, S.-Y.6    Varshavsky, A.7    Hwang, C.-S.8
  • 49
    • 84859490749 scopus 로고    scopus 로고
    • Protein N-terminal acetyltransferases: When the start matters
    • Starheim, K. K., Gevaert, K., and Arnesen, T. (2012) Protein N-terminal acetyltransferases: when the start matters. Trends Biochem. Sci. 37, 152-161
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 152-161
    • Starheim, K.K.1    Gevaert, K.2    Arnesen, T.3
  • 50
    • 0345743607 scopus 로고    scopus 로고
    • Degradation of the id2 developmental regulator: Targeting via N-terminal ubiquitination
    • Fajerman, I., and Schwartz, A. L., and Ciechanover, A. (2004) Degradation of the Id2 developmental regulator: targeting via N-terminal ubiquitination. Biochem. Biophys. Res. Commun. 314, 505-512
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 505-512
    • Fajerman, I.1    Schwartz, A.L.2    Ciechanover, A.3
  • 51
    • 21744433861 scopus 로고    scopus 로고
    • Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase
    • Cadwell, K., and Coscoy, L. (2005) Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase. Science 309, 127-130
    • (2005) Science , vol.309 , pp. 127-130
    • Cadwell, K.1    Coscoy, L.2
  • 52
    • 68549119002 scopus 로고    scopus 로고
    • Role of the RING-CH domain of viral ligase mK3 in ubiquitination of non-lysine and lysine MHC I residues
    • Herr, R. A., Harris, J., Fang, S., Wang, X., and Hansen, T. H. (2009) Role of the RING-CH domain of viral ligase mK3 in ubiquitination of non-lysine and lysine MHC I residues. Traffic 10, 1301-1317
    • (2009) Traffic , vol.10 , pp. 1301-1317
    • Herr, R.A.1    Harris, J.2    Fang, S.3    Wang, X.4    Hansen, T.H.5
  • 53
    • 0032531925 scopus 로고    scopus 로고
    • A novel site for ubiquitination: The N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein
    • Breitschopf, K., Bengal, E., Ziv, T., Admon, A., and Ciechanover, A. (1998) A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein. EMBO J. 17, 5964-5973
    • (1998) EMBO J. , vol.17 , pp. 5964-5973
    • Breitschopf, K.1    Bengal, E.2    Ziv, T.3    Admon, A.4    Ciechanover, A.5
  • 54
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. (2001) Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 57
    • 67849130558 scopus 로고    scopus 로고
    • TOP-CONS: Consensus prediction of membrane protein topology
    • Bernsel, A., Viklund, H., Hennerdal, A., and Elofsson, A. (2009) TOP-CONS: consensus prediction of membrane protein topology. Nucleic Acids Res. 37, W465-W468
    • (2009) Nucleic Acids Res. , vol.37 , pp. W465-W468
    • Bernsel, A.1    Viklund, H.2    Hennerdal, A.3    Elofsson, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.