메뉴 건너뛰기




Volumn 173, Issue 2, 2011, Pages 271-281

Structural insight into the glycosylphosphatidylinositol transamidase subunits PIG-K and PIG-S from yeast

Author keywords

Glycosylphosphatidylinositol transamidase; GPI anchor; PIG K; PIG S; Post translational modification

Indexed keywords

ENZYME; GLYCOSYLPHOSPHATIDYLINOSITOL; GLYCOSYLPHOSPHATIDYLINOSITOL TRANSAMIDASE; PROTEIN PIG K; PROTEIN PIG S; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 78751566519     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.11.026     Document Type: Article
Times cited : (12)

References (60)
  • 2
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade M.A., Chacón P., Merelo J.J., Morán F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 1993, 6:383-390.
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4
  • 3
    • 0036499652 scopus 로고    scopus 로고
    • Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins
    • Aravind L., Koonin E.V. Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins. Proteins 2002, 46:355-367.
    • (2002) Proteins , vol.46 , pp. 355-367
    • Aravind, L.1    Koonin, E.V.2
  • 8
    • 0027190626 scopus 로고
    • An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum
    • Deléage G., Geourjon C. An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum. Comput. Appl. Biosci 1993, 9:197-199.
    • (1993) Comput. Appl. Biosci , vol.9 , pp. 197-199
    • Deléage, G.1    Geourjon, C.2
  • 9
    • 77952778270 scopus 로고    scopus 로고
    • Prediction of posttranslational modification of proteins from their amino acid sequence
    • Eisenhaber B., Eisenhaber F. Prediction of posttranslational modification of proteins from their amino acid sequence. Methods Mol. Biol. 2010, 609:365-384.
    • (2010) Methods Mol. Biol. , vol.609 , pp. 365-384
    • Eisenhaber, B.1    Eisenhaber, F.2
  • 10
    • 0032409445 scopus 로고    scopus 로고
    • Sequence properties of GPI-anchored proteins near the omega-site: constraints for the polypeptide binding site of the putative transamidase
    • Eisenhaber B., Bork P., Eisenhaber F. Sequence properties of GPI-anchored proteins near the omega-site: constraints for the polypeptide binding site of the putative transamidase. Protein Eng. 1998, 11:1155-1161.
    • (1998) Protein Eng. , vol.11 , pp. 1155-1161
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 11
    • 0033600935 scopus 로고    scopus 로고
    • Prediction of potential GPI-modification sites in proprotein sequences
    • Eisenhaber B., Bork P., Eisenhaber F. Prediction of potential GPI-modification sites in proprotein sequences. J. Mol. Biol. 1999, 292:741-758.
    • (1999) J. Mol. Biol. , vol.292 , pp. 741-758
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 12
    • 0035049164 scopus 로고    scopus 로고
    • Post-translational GPI lipid anchor modification of proteins in kingdoms of life: analysis of protein sequence data from complete genomes
    • Eisenhaber B., Bork P., Eisenhaber F. Post-translational GPI lipid anchor modification of proteins in kingdoms of life: analysis of protein sequence data from complete genomes. Protein Eng. 2001, 14:17-25.
    • (2001) Protein Eng. , vol.14 , pp. 17-25
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 13
    • 0037387522 scopus 로고    scopus 로고
    • Enzymes and auxiliary factors for GPI lipid anchor biosynthesis and post-translational transfer to proteins
    • Eisenhaber B., Maurer-Stroh S., Novatchkova M., Schneider G., Eisenhaber F. Enzymes and auxiliary factors for GPI lipid anchor biosynthesis and post-translational transfer to proteins. Bioessays 2003, 25:367-385.
    • (2003) Bioessays , vol.25 , pp. 367-385
    • Eisenhaber, B.1    Maurer-Stroh, S.2    Novatchkova, M.3    Schneider, G.4    Eisenhaber, F.5
  • 14
    • 1442348239 scopus 로고    scopus 로고
    • A sensitive predictor for potential GPI lipid modification sites in fungal protein sequences and its application to genome-wide studies for Aspergillus nidulans, Candida albicans, Neurospora crassa, Saccharomyces cerevisiae and Schizosaccharomyces pombe
    • Eisenhaber B., Schneider G., Wildpaner M., Eisenhaber F. A sensitive predictor for potential GPI lipid modification sites in fungal protein sequences and its application to genome-wide studies for Aspergillus nidulans, Candida albicans, Neurospora crassa, Saccharomyces cerevisiae and Schizosaccharomyces pombe. J. Mol. Biol. 2004, 337:243-253.
    • (2004) J. Mol. Biol. , vol.337 , pp. 243-253
    • Eisenhaber, B.1    Schneider, G.2    Wildpaner, M.3    Eisenhaber, F.4
  • 17
    • 0038386050 scopus 로고    scopus 로고
    • 3D-Jury: a simple approach to improve protein structure predictions
    • Ginalski K., Elofsson A., Fischer D., Rychlewski L. 3D-Jury: a simple approach to improve protein structure predictions. Bioinformatics 2003, 19:1015-1018.
    • (2003) Bioinformatics , vol.19 , pp. 1015-1018
    • Ginalski, K.1    Elofsson, A.2    Fischer, D.3    Rychlewski, L.4
  • 20
    • 0038247909 scopus 로고    scopus 로고
    • Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins
    • Hong Y., Ohishi K., Kang J.Y., Tanaka S., Inoue N., Nishimura J., Maeda Y., Kinoshita T. Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins. Mol. Biol. Cell 2003, 14:1780-1789.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1780-1789
    • Hong, Y.1    Ohishi, K.2    Kang, J.Y.3    Tanaka, S.4    Inoue, N.5    Nishimura, J.6    Maeda, Y.7    Kinoshita, T.8
  • 21
    • 58149287887 scopus 로고    scopus 로고
    • Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 N-acetylglucosaminyl transferase in Trypanosoma brucei
    • Izquierdo L., Nakanishi M., Mehlert A., Machray G., Barton G.J., Ferguson M.A.J. Identification of a glycosylphosphatidylinositol anchor-modifying beta1-3 N-acetylglucosaminyl transferase in Trypanosoma brucei. Mol. Microbiol. 2009, 71:478-491.
    • (2009) Mol. Microbiol. , vol.71 , pp. 478-491
    • Izquierdo, L.1    Nakanishi, M.2    Mehlert, A.3    Machray, G.4    Barton, G.J.5    Ferguson, M.A.J.6
  • 23
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000daltons
    • Karas M., Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000daltons. Anal. Chem. 1988, 60:2299-2301.
    • (1988) Anal. Chem. , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 24
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley L.A., Sternberg M.J.E. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 2009, 4:363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • Manavalan P., Johnson W.C. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 1987, 167:76-85.
    • (1987) Anal. Biochem. , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson, W.C.2
  • 27
    • 0029096233 scopus 로고
    • An active carbonyl formed during glycosylphosphatidylinositol addition to a protein is evidence of catalysis by a transamidase
    • Maxwell S.E., Ramalingam S., Gerber L.D., Brink L., Udenfriend S. An active carbonyl formed during glycosylphosphatidylinositol addition to a protein is evidence of catalysis by a transamidase. J. Biol. Chem. 1995, 270:19576-19582.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19576-19582
    • Maxwell, S.E.1    Ramalingam, S.2    Gerber, L.D.3    Brink, L.4    Udenfriend, S.5
  • 28
    • 0028950984 scopus 로고
    • Cleavage without anchor addition accompanies the processing of a nascent protein to its glycosylphosphatidylinositol-anchored form
    • Maxwell S.E., Ramalingam S., Gerber L.D., Udenfriend S. Cleavage without anchor addition accompanies the processing of a nascent protein to its glycosylphosphatidylinositol-anchored form. Proc. Natl. Acad. Sci. USA 1995, 92:1550-1554.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1550-1554
    • Maxwell, S.E.1    Ramalingam, S.2    Gerber, L.D.3    Udenfriend, S.4
  • 29
    • 34248581962 scopus 로고    scopus 로고
    • Truncation of the caspase-related subunit (Gpi8p) of Saccharomyces cerevisiae GPI transamidase: dimerization revealed
    • Meitzler J.L., Gray J.J., Hendrickson T.L. Truncation of the caspase-related subunit (Gpi8p) of Saccharomyces cerevisiae GPI transamidase: dimerization revealed. Arch. Biochem. Biophys. 2007, 462:83-93.
    • (2007) Arch. Biochem. Biophys. , vol.462 , pp. 83-93
    • Meitzler, J.L.1    Gray, J.J.2    Hendrickson, T.L.3
  • 30
    • 0034724159 scopus 로고    scopus 로고
    • Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins
    • Meyer U., Benghezal M., Imhof I., Conzelmann A. Active site determination of Gpi8p, a caspase-related enzyme required for glycosylphosphatidylinositol anchor addition to proteins. Biochemistry 2000, 39:3461-3471.
    • (2000) Biochemistry , vol.39 , pp. 3461-3471
    • Meyer, U.1    Benghezal, M.2    Imhof, I.3    Conzelmann, A.4
  • 31
    • 0141814703 scopus 로고    scopus 로고
    • GPI transamidase of Trypanosoma brucei has two previously uncharacterized (trypanosomatid transamidase 1 and 2) and three common subunits
    • Nagamune K., Ohishi K., Ashida H., Hong Y., Hino J., Kangawa K., Inoue N., Maeda Y., Kinoshita T. GPI transamidase of Trypanosoma brucei has two previously uncharacterized (trypanosomatid transamidase 1 and 2) and three common subunits. Proc. Natl. Acad. Sci. USA 2003, 100:10682-10687.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10682-10687
    • Nagamune, K.1    Ohishi, K.2    Ashida, H.3    Hong, Y.4    Hino, J.5    Kangawa, K.6    Inoue, N.7    Maeda, Y.8    Kinoshita, T.9
  • 33
    • 0032918610 scopus 로고    scopus 로고
    • Developmental abnormalities of glycosylphosphatidylinositol-anchor-deficient embryos revealed by Cre/loxP system
    • Nozaki M., Ohishi K., Yamada N., Kinoshita T., Nagy A., Takeda J. Developmental abnormalities of glycosylphosphatidylinositol-anchor-deficient embryos revealed by Cre/loxP system. Lab. Invest. 1999, 79:293-299.
    • (1999) Lab. Invest. , vol.79 , pp. 293-299
    • Nozaki, M.1    Ohishi, K.2    Yamada, N.3    Kinoshita, T.4    Nagy, A.5    Takeda, J.6
  • 34
    • 0034108088 scopus 로고    scopus 로고
    • Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins
    • Ohishi K., Inoue N., Maeda Y., Takeda J., Riezman H., Kinoshita T. Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins. Mol. Biol. Cell 2000, 11:1523-1533.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1523-1533
    • Ohishi, K.1    Inoue, N.2    Maeda, Y.3    Takeda, J.4    Riezman, H.5    Kinoshita, T.6
  • 35
    • 0035421238 scopus 로고    scopus 로고
    • PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8
    • Ohishi K., Inoue N., Kinoshita T. PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J 2001, 20:4088-4098.
    • (2001) EMBO J , vol.20 , pp. 4088-4098
    • Ohishi, K.1    Inoue, N.2    Kinoshita, T.3
  • 36
    • 0037853150 scopus 로고    scopus 로고
    • Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge
    • Ohishi K., Nagamune K., Maeda Y., Kinoshita T. Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge. J. Biol. Chem. 2003, 278:13959-13967.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13959-13967
    • Ohishi, K.1    Nagamune, K.2    Maeda, Y.3    Kinoshita, T.4
  • 38
    • 34248227584 scopus 로고    scopus 로고
    • Thematic review series: lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids
    • Orlean P., Menon A.K. Thematic review series: lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids. J. Lipid Res. 2007, 48:993-1011.
    • (2007) J. Lipid Res. , vol.48 , pp. 993-1011
    • Orlean, P.1    Menon, A.K.2
  • 39
    • 46849102138 scopus 로고    scopus 로고
    • The glycosylphosphatidylinositol anchor: a complex membrane-anchoring structure for proteins
    • Paulick M.G., Bertozzi C.R. The glycosylphosphatidylinositol anchor: a complex membrane-anchoring structure for proteins. Biochemistry 2008, 47:6991-7000.
    • (2008) Biochemistry , vol.47 , pp. 6991-7000
    • Paulick, M.G.1    Bertozzi, C.R.2
  • 40
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov M.V., Svergun D.I. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 2005, 89:1237-1250.
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 41
    • 33947232747 scopus 로고    scopus 로고
    • Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae
    • Pittet M., Conzelmann A. Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 2007, 1771:405-420.
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 405-420
    • Pittet, M.1    Conzelmann, A.2
  • 42
    • 0020176542 scopus 로고
    • A constrained regularization method for inverting data represented by linear algebraic or integral equations
    • Provencher S.W. A constrained regularization method for inverting data represented by linear algebraic or integral equations. Computer Physics. Commun. 1982, 27:213-227.
    • (1982) Computer Physics. Commun. , vol.27 , pp. 213-227
    • Provencher, S.W.1
  • 43
    • 0029794879 scopus 로고    scopus 로고
    • COOH-terminal processing of nascent polypeptides by the glycosylphosphatidylinositol transamidase in the presence of hydrazine is governed by the same parameters as glycosylphosphatidylinositol addition
    • Ramalingam S., Maxwell S.E., Medof M.E., Chen R., Gerber L.D., Udenfriend S. COOH-terminal processing of nascent polypeptides by the glycosylphosphatidylinositol transamidase in the presence of hydrazine is governed by the same parameters as glycosylphosphatidylinositol addition. Proc. Natl. Acad. Sci. USA 1996, 93:7528-7533.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7528-7533
    • Ramalingam, S.1    Maxwell, S.E.2    Medof, M.E.3    Chen, R.4    Gerber, L.D.5    Udenfriend, S.6
  • 44
    • 59449110909 scopus 로고    scopus 로고
    • DOG 1.0: illustrator of protein domain structures
    • Ren J., Wen L., Gao X., Jin C., Xue Y., Yao X. DOG 1.0: illustrator of protein domain structures. Cell Res 2009, 19:271-273.
    • (2009) Cell Res , vol.19 , pp. 271-273
    • Ren, J.1    Wen, L.2    Gao, X.3    Jin, C.4    Xue, Y.5    Yao, X.6
  • 47
    • 77952786465 scopus 로고    scopus 로고
    • Integrated tools for biomolecular sequence-based function prediction as exemplified by the ANNOTATOR software environment
    • Schneider G., Wildpaner M., Sirota F.L., Maurer-Stroh S., Eisenhaber B., Eisenhaber F. Integrated tools for biomolecular sequence-based function prediction as exemplified by the ANNOTATOR software environment. Methods Mol. Biol. 2010, 609:257-267.
    • (2010) Methods Mol. Biol. , vol.609 , pp. 257-267
    • Schneider, G.1    Wildpaner, M.2    Sirota, F.L.3    Maurer-Stroh, S.4    Eisenhaber, B.5    Eisenhaber, F.6
  • 48
    • 0034331886 scopus 로고    scopus 로고
    • Soluble GPI8 restores glycosylphosphatidylinositol anchoring in a trypanosome cell-free system depleted of lumenal endoplasmic reticulum proteins
    • Sharma D.K., Hilley J.D., Bangs J.D., Coombs G.H., Mottram J.C., Menon A.K. Soluble GPI8 restores glycosylphosphatidylinositol anchoring in a trypanosome cell-free system depleted of lumenal endoplasmic reticulum proteins. Biochem. J. 2000, 351:717-722.
    • (2000) Biochem. J. , vol.351 , pp. 717-722
    • Sharma, D.K.1    Hilley, J.D.2    Bangs, J.D.3    Coombs, G.H.4    Mottram, J.C.5    Menon, A.K.6
  • 49
    • 10644286553 scopus 로고    scopus 로고
    • Chemical validation of GPI biosynthesis as a drug target against African sleeping sickness
    • Smith T.K., Crossman A., Brimacombe J.S., Ferguson M.A.J. Chemical validation of GPI biosynthesis as a drug target against African sleeping sickness. EMBO J. 2004, 23:4701-4708.
    • (2004) EMBO J. , vol.23 , pp. 4701-4708
    • Smith, T.K.1    Crossman, A.2    Brimacombe, J.S.3    Ferguson, M.A.J.4
  • 50
    • 0035844125 scopus 로고    scopus 로고
    • Early events in glycosylphosphatidylinositol anchor addition. Substrate proteins associate with the transamidase subunit gpi8p
    • Spurway T.D., Dalley J.A., High S., Bulleid N.J. Early events in glycosylphosphatidylinositol anchor addition. Substrate proteins associate with the transamidase subunit gpi8p. J. Biol. Chem 2001, 276:15975-15982.
    • (2001) J. Biol. Chem , vol.276 , pp. 15975-15982
    • Spurway, T.D.1    Dalley, J.A.2    High, S.3    Bulleid, N.J.4
  • 51
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama N., Woody R.W. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem 1993, 209:32-44.
    • (1993) Anal. Biochem , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 52
    • 0027578071 scopus 로고
    • A direct indirect method of small-angle scattering data treatment
    • Svergun D.I. A direct indirect method of small-angle scattering data treatment. J. Appl. Crystallogr. 1993, 26:258-267.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 258-267
    • Svergun, D.I.1
  • 53
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 1999, 76:2879-2886.
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 54
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun D.I., Petoukhov M.V., Koch M.H. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 2001, 80:2946-2953.
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 55
    • 0036302007 scopus 로고    scopus 로고
    • Peptide and protein analysis with mass spectrometry
    • Trauger S., Webb W., Siuzdak G. Peptide and protein analysis with mass spectrometry. Spectroscopy 2002, 16:15-28.
    • (2002) Spectroscopy , vol.16 , pp. 15-28
    • Trauger, S.1    Webb, W.2    Siuzdak, G.3
  • 56
    • 0028981209 scopus 로고
    • How glycosylphosphatidylinositol-anchored membrane proteins are made
    • Udenfriend S., Kodukula K. How glycosylphosphatidylinositol-anchored membrane proteins are made. Annu. Rev. Biochem. 1995, 64:563-591.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 563-591
    • Udenfriend, S.1    Kodukula, K.2
  • 57
    • 58149164667 scopus 로고    scopus 로고
    • Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues
    • Urbaniak M.D., Yashunsky D.V., Crossman A., Nikolaev A.V., Ferguson M.A.J. Probing enzymes late in the trypanosomal glycosylphosphatidylinositol biosynthetic pathway with synthetic glycosylphosphatidylinositol analogues. ACS Chem. Biol. 2008, 3:625-634.
    • (2008) ACS Chem. Biol. , vol.3 , pp. 625-634
    • Urbaniak, M.D.1    Yashunsky, D.V.2    Crossman, A.3    Nikolaev, A.V.4    Ferguson, M.A.J.5
  • 58
    • 0037406141 scopus 로고    scopus 로고
    • Can correct protein models be identified?
    • Wallner B., Elofsson A. Can correct protein models be identified?. Protein Sci. 2003, 12:1073-1086.
    • (2003) Protein Sci. , vol.12 , pp. 1073-1086
    • Wallner, B.1    Elofsson, A.2
  • 59
    • 0029901640 scopus 로고    scopus 로고
    • Analysis of compositionally biased regions in sequence databases
    • Wootton J.C., Federhen S. Analysis of compositionally biased regions in sequence databases. Meth. Enzymol. 1996, 266:554-571.
    • (1996) Meth. Enzymol. , vol.266 , pp. 554-571
    • Wootton, J.C.1    Federhen, S.2
  • 60
    • 20444434331 scopus 로고    scopus 로고
    • Gpi17p does not stably interact with other subunits of glycosylphosphatidylinositol transamidase in Saccharomyces cerevisiae
    • Zhu Y., Fraering P., Vionnet C., Conzelmann A. Gpi17p does not stably interact with other subunits of glycosylphosphatidylinositol transamidase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 2005, 1735:79-88.
    • (2005) Biochim. Biophys. Acta , vol.1735 , pp. 79-88
    • Zhu, Y.1    Fraering, P.2    Vionnet, C.3    Conzelmann, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.