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Volumn , Issue 96, 2015, Pages

Growth-based determination and biochemical confirmation of genetic requirements for protein degradation in Saccharomyces cerevisiae

Author keywords

Budding yeast; Endoplasmic reticulum associated degradation; Growth assay; Issue 96; Molecular biology; Mutants; Protein degradation; Protein extracts; Saccharomyces cerevisiae; Ubiquitin proteasome system; Western blotting; Yeast genetics

Indexed keywords

SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84923614495     PISSN: 1940087X     EISSN: None     Source Type: Journal    
DOI: 10.3791/52428     Document Type: Article
Times cited : (10)

References (59)
  • 1
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A. L. Protein degradation and protection against misfolded or damaged proteins. Nature. 426, 895-899 (2003).
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 2
    • 84860118506 scopus 로고    scopus 로고
    • The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology
    • Guerriero, C. J., Brodsky, J. L. The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology. Physiological Reviews. 92, 537-576 (2012).
    • (2012) Physiological Reviews , vol.92 , pp. 537-576
    • Guerriero, C.J.1    Brodsky, J.L.2
  • 3
    • 84876374189 scopus 로고    scopus 로고
    • Role of the ubiquitin proteasome system in the heart
    • Pagan, J., Seto, T., Pagano, M., Cittadini, A. Role of the ubiquitin proteasome system in the heart. Circulation Research. 112, 1046-1058 (2013).
    • (2013) Circulation Research , vol.112 , pp. 1046-1058
    • Pagan, J.1    Seto, T.2    Pagano, M.3    Cittadini, A.4
  • 4
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein, D. C. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature. 443, 780-786 (2006).
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 6
    • 78650824534 scopus 로고    scopus 로고
    • Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets
    • Bedford, L., Lowe, J., Dick, L. R., Mayer, R. J., Brownell, J. E. Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets. Nature Reviews Drug Discovery. 10, 29-46 (2011).
    • (2011) Nature Reviews Drug Discovery , vol.10 , pp. 29-46
    • Bedford, L.1    Lowe, J.2    Dick, L.R.3    Mayer, R.J.4    Brownell, J.E.5
  • 8
    • 58149159907 scopus 로고    scopus 로고
    • Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: Therapeutic approaches. BioEssays: News and Reviews in Molecular
    • Paul, S. Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: therapeutic approaches. BioEssays: News and Reviews in Molecular, Cellular and Developmental Biology. 30, 1172-1184 (2008).
    • (2008) Cellular and Developmental Biology , vol.30 , pp. 1172-1184
    • Paul, S.1
  • 10
    • 84867176120 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system of Saccharomyces cerevisiae
    • Finley, D., Ulrich, H. D., Sommer, T., Kaiser, P. The ubiquitin-proteasome system of Saccharomyces cerevisiae. Genetics. 192, 319-360 (2012).
    • (2012) Genetics , vol.192 , pp. 319-360
    • Finley, D.1    Ulrich, H.D.2    Sommer, T.3    Kaiser, P.4
  • 11
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner, M., Nuber, U., Huibregtse, J. M. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature. 373, 81-83 (1995).
    • (1995) Nature , vol.373 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 12
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • Ravid, T., Hochstrasser, M. Diversity of degradation signals in the ubiquitin-proteasome system. Nature Reviews Molecular Cell Biology. 9, 679-690 (2008).
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 14
    • 0025331090 scopus 로고
    • Vivo degradation of a transcriptional regulator: The yeast alpha 2 repressor
    • Hochstrasser, M., Varshavsky, A. In vivo degradation of a transcriptional regulator: the yeast alpha 2 repressor. Cell. 61, 697-708 (1990).
    • (1990) Cell , vol.61 , pp. 697-708
    • Hochstrasser, M.1    Varshavsky, A.2
  • 15
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays, N. W., Gardner, R. G., Seelig, L. P., Joazeiro, C. A., Hampton, R. Y. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nature Cell Biology. 3, 24-29 (2001).
    • (2001) Nature Cell Biology , vol.3 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3    Joazeiro, C.A.4    Hampton, R.Y.5
  • 16
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton, R. Y., Gardner, R. G., Rine, J. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Molecular Biology of the Cell. 7, 2029-2044 (1996).
    • (1996) Molecular Biology of the Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 17
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation
    • Swanson, R., Locher, M., Hochstrasser, M. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes & Development. 15, 2660-2674 (2001).
    • (2001) Genes & Development , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 18
    • 0023722309 scopus 로고
    • The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme
    • Goebl, M. G., et al. The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme. Science. 241, 1331-1335 (1988).
    • (1988) Science , vol.241 , pp. 1331-1335
    • Goebl, M.G.1
  • 19
    • 0023003380 scopus 로고
    • Vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., Finley, D., Varshavsky, A. In vivo half-life of a protein is a function of its amino-terminal residue. Science. 234, 179-186 (1986).
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 20
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor
    • Chen, P., Johnson, P., Sommer, T., Jentsch, S., Hochstrasser, M. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor. Cell. 74, 357-369 (1993).
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 22
    • 0025980627 scopus 로고
    • Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: Mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival
    • Heinemeyer, W., Kleinschmidt, J. A., Saidowsky, J., Escher, C., Wolf, D. H. Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. The EMBO Journal. 10, 555-562 (1991).
    • (1991) The EMBO Journal , vol.10 , pp. 555-562
    • Heinemeyer, W.1    Kleinschmidt, J.A.2    Saidowsky, J.3    Escher, C.4    Wolf, D.H.5
  • 23
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • Sommer, T., Jentsch, S. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature. 365, 176-179 (1993).
    • (1993) Nature , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 24
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M. M., Finger, A., Schweiger, M., Wolf, D. H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science. 273, 1725-1728 (1996).
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 25
    • 0026708316 scopus 로고
    • Vivo function of the proteasome in the ubiquitin pathway
    • Seufert, W., Jentsch, S. In vivo function of the proteasome in the ubiquitin pathway. The EMBO Journal. 11, 3077-3080 (1992).
    • (1992) The EMBO Journal , vol.11 , pp. 3077-3080
    • Seufert, W.1    Jentsch, S.2
  • 26
    • 0030041781 scopus 로고    scopus 로고
    • Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast
    • Knop, M., Finger, A., Braun, T., Hellmuth, K., Wolf, D. H. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. The EMBO Journal. 15, 753-763 (1996).
    • (1996) The EMBO Journal , vol.15 , pp. 753-763
    • Knop, M.1    Finger, A.2    Braun, T.3    Hellmuth, K.4    Wolf, D.H.5
  • 27
    • 84875478507 scopus 로고    scopus 로고
    • N-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates
    • Zattas, D., Adle, D. J., Rubenstein, E. M., Hochstrasser, M. N-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates. Molecular Biology of the Cell.24, 890-900 (2013).
    • (2013) Molecular Biology of the Cell , vol.24 , pp. 890-900
    • Zattas, D.1    Adle, D.J.2    Rubenstein, E.M.3    Hochstrasser, M.4
  • 28
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C. B., et al. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast. 14, 115-132 (1998).
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1
  • 29
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., Hieter, P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122, 19-27 (1989).
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 30
    • 84867446455 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae W303-K6001 cross-platform genome sequence: Insights into ancestry and physiology of a laboratory mutt
    • Ralser, M., et al. The Saccharomyces cerevisiae W303-K6001 cross-platform genome sequence: insights into ancestry and physiology of a laboratory mutt. Open Biology. 2, 120093 (2012).
    • (2012) Open Biology
    • Ralser, M.1
  • 31
    • 0034733591 scopus 로고    scopus 로고
    • Rapid and reliable protein extraction from yeast
    • Kushnirov, V. V. Rapid and reliable protein extraction from yeast. Yeast. 16, 857-860 (2000).
    • (2000) Yeast , vol.16 , pp. 857-860
    • Kushnirov, V.V.1
  • 32
  • 33
    • 0032526433 scopus 로고    scopus 로고
    • Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein
    • Mayer, T. U., Braun, T., Jentsch, S. Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. The EMBO Journal. 17, 3251-3257 (1998).
    • (1998) The EMBO Journal , vol.17 , pp. 3251-3257
    • Mayer, T.U.1    Braun, T.2    Jentsch, S.3
  • 34
    • 46249094620 scopus 로고    scopus 로고
    • Role of Sec61p in the ER-associated degradation of short-lived transmembrane proteins
    • Scott, D. C., Schekman, R. Role of Sec61p in the ER-associated degradation of short-lived transmembrane proteins. The Journal of Cell Biology. 181, 1095-1105 (2008).
    • (2008) The Journal of Cell Biology , vol.181 , pp. 1095-1105
    • Scott, D.C.1    Schekman, R.2
  • 35
    • 30944459275 scopus 로고    scopus 로고
    • The Png1-Rad23 complex regulates glycoprotein turnover
    • Kim, I., et al. The Png1-Rad23 complex regulates glycoprotein turnover. The Journal of Cell Biology. 172, 211-219 (2006).
    • (2006) The Journal of Cell Biology , vol.172 , pp. 211-219
    • Kim, I.1
  • 36
    • 0030860899 scopus 로고    scopus 로고
    • The degradation of apolipoprotein B100 is mediated by the ubiquitin-proteasome pathway and involves heat shock protein 70
    • Fisher, E. A., et al. The degradation of apolipoprotein B100 is mediated by the ubiquitin-proteasome pathway and involves heat shock protein 70. The Journal of Biological Chemistry. 272, 20427-20434 (1997).
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 20427-20434
    • Fisher, E.A.1
  • 37
    • 0035808302 scopus 로고    scopus 로고
    • Co-translational interactions of apoprotein B with the ribosome and translocon during lipoprotein assembly or targeting to the proteasome
    • Pariyarath, R., et al. Co-translational interactions of apoprotein B with the ribosome and translocon during lipoprotein assembly or targeting to the proteasome. The Journal of Biological Chemistry. 276, 541-550 (2001).
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 541-550
    • Pariyarath, R.1
  • 38
    • 10244270656 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway mediates intracellular degradation of apolipoprotein. B
    • Yeung, S. J., Chen, S. H., Chan, L. Ubiquitin-proteasome pathway mediates intracellular degradation of apolipoprotein. B. Biochemistry. 35, 13843-13848 (1996).
    • (1996) Biochemistry , vol.35 , pp. 13843-13848
    • Yeung, S.J.1    Chen, S.H.2    Chan, L.3
  • 39
    • 0028586017 scopus 로고
    • Regulatable promoters of Saccharomyces cerevisiae: Comparison of transcriptional activity and their use for heterologous expression
    • Mumberg, D., Muller, R., Funk, M. Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic Acids Research. 22, 5767-5768 (1994).
    • (1994) Nucleic Acids Research , vol.22 , pp. 5767-5768
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 42
    • 84901318174 scopus 로고    scopus 로고
    • Budding yeast for budding geneticists: A primer on the Saccharomyces cerevisiae model system
    • Duina, A. A., Miller, M. E., Keeney, J. B. Budding yeast for budding geneticists: a primer on the Saccharomyces cerevisiae model system. Genetics. 197, 33-48 (2014).
    • (2014) Genetics , vol.197 , pp. 33-48
    • Duina, A.A.1    Miller, M.E.2    Keeney, J.B.3
  • 44
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • Sherman, F. Getting started with yeast. Methods in Enzymology. 350, 3-41 (2002).
    • (2002) Methods in Enzymology , vol.350 , pp. 3-41
    • Sherman, F.1
  • 45
    • 77951806546 scopus 로고    scopus 로고
    • SUMO-independent in vivo activity of a SUMO-targeted ubiquitin ligase toward a short-lived transcription factor
    • Xie, Y., Rubenstein, E. M., Matt, T., Hochstrasser, M. SUMO-independent in vivo activity of a SUMO-targeted ubiquitin ligase toward a short-lived transcription factor. Genes & Development. 24, 893-903 (2010).
    • (2010) Genes & Development , vol.24 , pp. 893-903
    • Xie, Y.1    Rubenstein, E.M.2    Matt, T.3    Hochstrasser, M.4
  • 46
    • 32544437041 scopus 로고    scopus 로고
    • Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways
    • Ravid, T., Kreft, S. G., Hochstrasser, M. Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. The EMBO Journal. 25, 533-543 (2006).
    • (2006) The EMBO Journal , vol.25 , pp. 533-543
    • Ravid, T.1    Kreft, S.G.2    Hochstrasser, M.3
  • 47
    • 57749116223 scopus 로고    scopus 로고
    • Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery
    • Metzger, M. B., Maurer, M. J., Dancy, B. M., Michaelis, S. Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery. The Journal of Biological Chemistry. 283, 32302-32316 (2008).
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 32302-32316
    • Metzger, M.B.1    Maurer, M.J.2    Dancy, B.M.3    Michaelis, S.4
  • 48
    • 4444320698 scopus 로고    scopus 로고
    • A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation
    • Medicherla, B., Kostova, Z., Schaefer, A., Wolf, D. H. A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. EMBO Reports. 5, 692-697 (2004).
    • (2004) EMBO Reports , vol.5 , pp. 692-697
    • Medicherla, B.1    Kostova, Z.2    Schaefer, A.3    Wolf, D.H.4
  • 49
    • 47749090557 scopus 로고    scopus 로고
    • Ubiquitin ligase Hul5 is required for fragment-specific substrate degradation in endoplasmic reticulum-associated degradation
    • Kohlmann, S., Schafer, A., Wolf, D. H. Ubiquitin ligase Hul5 is required for fragment-specific substrate degradation in endoplasmic reticulum-associated degradation. The Journal of Biological Chemistry. 283, 16374-16383 (2008).
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 16374-16383
    • Kohlmann, S.1    Schafer, A.2    Wolf, D.H.3
  • 50
    • 0034429954 scopus 로고    scopus 로고
    • Mutagenesis assays in yeast
    • Crouse, G. F. Mutagenesis assays in yeast. Methods. 22, 116-119 (2000).
    • (2000) Methods , vol.22 , pp. 116-119
    • Crouse, G.F.1
  • 51
    • 0028912374 scopus 로고
    • A new version of the two-hybrid assay for detection of protein-protein interactions
    • Le Douarin, B., Pierrat, B., vom Baur, E., Chambon, F., Losson, R. A new version of the two-hybrid assay for detection of protein-protein interactions. Nucleic Acids Research. 23, 876-878 (1995).
    • (1995) Nucleic Acids Research , vol.23 , pp. 876-878
    • Le Douarin, B.1    Pierrat, B.2    Vom Baur, E.3    Chambon, F.4    Losson, R.5
  • 52
    • 0023484186 scopus 로고
    • R. 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke, J. D., Trueheart, J., Natsoulis, G., Fink, G. R. 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods in Enzymology. 154, 164-175 (1987).
    • (1987) Methods in Enzymology , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.4
  • 53
    • 0034035729 scopus 로고    scopus 로고
    • A counterselection for the tryptophan pathway in yeast: 5-fluoroanthranilic acid resistance
    • Toyn, J. H., Gunyuzlu, P. L., White, W. H., Thompson, L. A., Hollis, G. F. A counterselection for the tryptophan pathway in yeast: 5-fluoroanthranilic acid resistance. Yeast. 16, 553-560 (2000).
    • (2000) Yeast , vol.16 , pp. 553-560
    • Toyn, J.H.1    Gunyuzlu, P.L.2    White, W.H.3    Thompson, L.A.4    Hollis, G.F.5
  • 54
    • 20344372921 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated protein quality control and degradation: Genome-wide screen for ERAD components
    • Schafer, A., Wolf, D. H. Endoplasmic reticulum-associated protein quality control and degradation: genome-wide screen for ERAD components. Methods in Molecular Biology. 301, 289-292 (2005).
    • (2005) Methods in Molecular Biology , vol.301 , pp. 289-292
    • Schafer, A.1    Wolf, D.H.2
  • 56
    • 84857834844 scopus 로고    scopus 로고
    • Growth assays to assess polyglutamine toxicity in yeast
    • Duennwald, M. L. Growth assays to assess polyglutamine toxicity in yeast. The Journal of Visualized Experiments. (61), e3791 (2012).
    • (2012) The Journal of Visualized Experiments , Issue.61
    • Duennwald, M.L.1
  • 57
    • 77956054446 scopus 로고    scopus 로고
    • Synthetic genetic array (SGA) analysis in Saccharomyces cerevisiae and Schizosaccharomyces pombe
    • Baryshnikova, A., et al. Synthetic genetic array (SGA) analysis in Saccharomyces cerevisiae and Schizosaccharomyces pombe. Methods in Enzymology. 470, 145-179 (2010).
    • (2010) Methods in Enzymology , vol.470 , pp. 145-179
    • Baryshnikova, A.1
  • 58
    • 84886814349 scopus 로고    scopus 로고
    • Budding yeast protein extraction and purification for the study of function, interactions, and post-translational modifications
    • Szymanski, E. P., Kerscher, O. Budding yeast protein extraction and purification for the study of function, interactions, and post-translational modifications. The Journal of Visualized Experiments. (80), e50921 (2013).
    • (2013) The Journal of Visualized Experiments , Issue.80
    • Szymanski, E.P.1    Kerscher, O.2
  • 59
    • 0016811609 scopus 로고
    • Immunologically active and structurally similar fragments of protein A from Staphylococcus aureus
    • Hjelm, H., Sjodahl, J., Sjoquist, J. Immunologically active and structurally similar fragments of protein A from Staphylococcus aureus. European Journal of Biochemistry. 57, 395-403 (1975).
    • (1975) European Journal of Biochemistry , vol.57 , pp. 395-403
    • Hjelm, H.1    Sjodahl, J.2    Sjoquist, J.3


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