메뉴 건너뛰기




Volumn 5, Issue 1, 2004, Pages 45-52

A complete set of SNAREs in yeast

Author keywords

Anchored proteins; Genomics; Membrane fusion; SNARE; Tail

Indexed keywords

ENVELOPE PROTEIN; MEMBRANE PROTEIN; MITOCHONDRIAL PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SNARE PROTEIN;

EID: 0742272120     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1600-0854.2003.00151.x     Document Type: Review
Times cited : (125)

References (70)
  • 1
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE. Mechanisms of intracellular protein transport. Nature 1994;372:55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 2
    • 0033602030 scopus 로고    scopus 로고
    • SNAREs and the secretory pathway-lessons from yeast
    • Pelham HR. SNAREs and the secretory pathway-lessons from yeast. Exp Cell Res 1999;247:1-8.
    • (1999) Exp. Cell Res. , vol.247 , pp. 1-8
    • Pelham, H.R.1
  • 6
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer D, Sutton RB, Brunger AT, Jahn R. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc Natl Acad Sci USA 1998;95:15781-15786.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 7
    • 0035865345 scopus 로고    scopus 로고
    • A genomic perspective on membrane compartment organization
    • Bock JB, Matern HT, Peden AA, Scheller RH. A genomic perspective on membrane compartment organization. Nature 2001;409:839-841.
    • (2001) Nature , vol.409 , pp. 839-841
    • Bock, J.B.1    Matern, H.T.2    Peden, A.A.3    Scheller, R.H.4
  • 11
    • 0024828306 scopus 로고
    • The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations
    • Oyler GA, Higgins GA, Hart RA, Battenberg E, Billingsley M, Bloom FE, Wilson MC. The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations. J Cell Biol 1989;109:3039-3052.
    • (1989) J. Cell Biol. , vol.109 , pp. 3039-3052
    • Oyler, G.A.1    Higgins, G.A.2    Hart, R.A.3    Battenberg, E.4    Billingsley, M.5    Bloom, F.E.6    Wilson, M.C.7
  • 12
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett MK, Calakos N, Scheller RH. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 1992;257:255-259.
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 13
    • 0019424489 scopus 로고
    • Order of events in the yeast secretory pathway
    • Novick P, Ferro S, Schekman R. Order of events in the yeast secretory pathway. Cell 1981;25:461-469.
    • (1981) Cell , vol.25 , pp. 461-469
    • Novick, P.1    Ferro, S.2    Schekman, R.3
  • 14
    • 0025277750 scopus 로고
    • Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway
    • Kaiser CA, Schekman R. Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Cell 1990;61:723-733.
    • (1990) Cell , vol.61 , pp. 723-733
    • Kaiser, C.A.1    Schekman, R.2
  • 15
    • 0028030275 scopus 로고
    • Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis
    • Brennwald P, Kearns B, Champion K, Keranen S, Bankaitis V, Novick P. Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell 1994;79: 245-258.
    • (1994) Cell , vol.79 , pp. 245-258
    • Brennwald, P.1    Kearns, B.2    Champion, K.3    Keranen, S.4    Bankaitis, V.5    Novick, P.6
  • 16
    • 0036346255 scopus 로고    scopus 로고
    • Predicting the distribution, conservation, and functions of SNAREs and related proteins in fungi
    • Gupta GD, Brent Heath I. Predicting the distribution, conservation, and functions of SNAREs and related proteins in fungi. Fungal Genet Biol 2002;36:1-21.
    • (2002) Fungal Genet. Biol. , vol.36 , pp. 1-21
    • Gupta, G.D.1    Brent Heath, I.2
  • 17
    • 0037089090 scopus 로고    scopus 로고
    • Novel syntaxin gene sequences from Giardia, Trypanosoma and algae: Implications for the ancient evolution of the eukaryotic endomembrane system
    • Dacks JB, Doolittle WF. Novel syntaxin gene sequences from Giardia, Trypanosoma and algae: implications for the ancient evolution of the eukaryotic endomembrane system. J Cell Sci 2002;115:1635-1642.
    • (2002) J. Cell Sci. , vol.115 , pp. 1635-1642
    • Dacks, J.B.1    Doolittle, W.F.2
  • 19
    • 0029932226 scopus 로고    scopus 로고
    • SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum
    • Lewis MJ, Pelham HR. SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Cell 1996;85:205-215.
    • (1996) Cell , vol.85 , pp. 205-215
    • Lewis, M.J.1    Pelham, H.R.2
  • 20
    • 0030668326 scopus 로고    scopus 로고
    • Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic
    • Lupashin VV, Pokrovskaya ID, McNew JA, Waters MG. Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic. Mol Biol Cell 1997;8:2659-2676.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2659-2676
    • Lupashin, V.V.1    Pokrovskaya, I.D.2    McNew, J.A.3    Waters, M.G.4
  • 23
    • 0036899471 scopus 로고    scopus 로고
    • A new yeast endosomal SNARE related to mammalian syntaxin 8
    • Lewis MJ, Pelham HR. A new yeast endosomal SNARE related to mammalian syntaxin 8. Traffic 2002;3:922-929.
    • (2002) Traffic , vol.3 , pp. 922-929
    • Lewis, M.J.1    Pelham, H.R.2
  • 24
    • 0032404442 scopus 로고    scopus 로고
    • A model for structural similarity between different SNARE complexes based on sequence relationships
    • Weimbs T, Mostov K, Low SH, Hofmann K. A model for structural similarity between different SNARE complexes based on sequence relationships. Trends Cell Biol 1998;8:260-262.
    • (1998) Trends Cell Biol. , vol.8 , pp. 260-262
    • Weimbs, T.1    Mostov, K.2    Low, S.H.3    Hofmann, K.4
  • 28
    • 0037424360 scopus 로고    scopus 로고
    • Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae
    • Beilharz T, Egan B, Silver PA, Hofmann K, Lithgow T. Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae. J Biol Chem 2003;278:8219-8223.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8219-8223
    • Beilharz, T.1    Egan, B.2    Silver, P.A.3    Hofmann, K.4    Lithgow, T.5
  • 29
    • 0035102443 scopus 로고    scopus 로고
    • Targeting of C-terminal (tail) -anchored proteins: Understanding how cytoplasmic activities are anchored to intracellular membranes
    • Wattenberg B, Lithgow T. Targeting of C-terminal (tail) -anchored proteins: understanding how cytoplasmic activities are anchored to intracellular membranes. Traffic 2001;2:66-71.
    • (2001) Traffic , vol.2 , pp. 66-71
    • Wattenberg, B.1    Lithgow, T.2
  • 30
    • 0028837490 scopus 로고
    • Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane
    • Kutay U, Ahnert-Hilger G, Hartmann E, Wiedenmann B, Rapoport TA. Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane. EMBO J 1995;14:217-223.
    • (1995) EMBO J. , vol.14 , pp. 217-223
    • Kutay, U.1    Ahnert-Hilger, G.2    Hartmann, E.3    Wiedenmann, B.4    Rapoport, T.A.5
  • 31
    • 0033601172 scopus 로고    scopus 로고
    • Identification of the endoplasmic reticulum targeting signal in vesicle-associated membrane proteins
    • Kim PK, Hollerbach C, Trimble WS, Leber B, Andrews DW. Identification of the endoplasmic reticulum targeting signal in vesicle-associated membrane proteins. J Biol Chem 1999;274:36876-36882.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36876-36882
    • Kim, P.K.1    Hollerbach, C.2    Trimble, W.S.3    Leber, B.4    Andrews, D.W.5
  • 32
    • 0036786921 scopus 로고    scopus 로고
    • Tail-anchored protein insertion into yeast ER requires a novel posttranslational mechanism which is independent of the SEC machinery
    • Steel GJ, Brownsword J, Stirling CJ. Tail-anchored protein insertion into yeast ER requires a novel posttranslational mechanism which is independent of the SEC machinery. Biochemistry 2002;41: 11914-11920.
    • (2002) Biochemistry , vol.41 , pp. 11914-11920
    • Steel, G.J.1    Brownsword, J.2    Stirling, C.J.3
  • 33
    • 0034675978 scopus 로고    scopus 로고
    • Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion
    • Grote E, Baba M, Ohsumi Y, Novick PJ. Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion. J Cell Biol 2000;51: 453-466.
    • (2000) J. Cell Biol. , vol.51 , pp. 453-466
    • Grote, E.1    Baba, M.2    Ohsumi, Y.3    Novick, P.J.4
  • 35
    • 0033197735 scopus 로고    scopus 로고
    • The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion
    • McNew JA, Weber T, Engelman DM, Söllner TH, Rothman JE. The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion. Mol Cell 1999;4:415-421.
    • (1999) Mol. Cell , vol.4 , pp. 415-421
    • McNew, J.A.1    Weber, T.2    Engelman, D.M.3    Söllner, T.H.4    Rothman, J.E.5
  • 36
    • 0035943407 scopus 로고    scopus 로고
    • Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity
    • Langosch D, Crane JM, Brosig B, Hellwig A, Tamm LK, Reed J. Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity. J Mol Biol 2001;311: 709-721.
    • (2001) J. Mol. Biol. , vol.311 , pp. 709-721
    • Langosch, D.1    Crane, J.M.2    Brosig, B.3    Hellwig, A.4    Tamm, L.K.5    Reed, J.6
  • 37
    • 0029165107 scopus 로고
    • An investigation of the role of transmembrane domains in Golgi protein retention
    • Munro S. An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J 1995;14:4695-4704.
    • (1995) EMBO J. , vol.14 , pp. 4695-4704
    • Munro, S.1
  • 38
    • 0030945486 scopus 로고    scopus 로고
    • Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast
    • Rayner JC, Pelham HR. Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO J 1997;16:1832-1841.
    • (1997) EMBO J. , vol.16 , pp. 1832-1841
    • Rayner, J.C.1    Pelham, H.R.2
  • 39
    • 0034805876 scopus 로고    scopus 로고
    • Transmembrane domain length determines intracellular membrane compartment localization of syntaxins 3, 4 and 5
    • Watson RT, Pessin JE. Transmembrane domain length determines intracellular membrane compartment localization of syntaxins 3, 4 and 5. Am J Physiol Cell Physiol 2001;281:C215-C223.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Watson, R.T.1    Pessin, J.E.2
  • 40
    • 0032584717 scopus 로고    scopus 로고
    • Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs
    • Springer S, Schekman R. Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs. Science 1998;281:698-700.
    • (1998) Science , vol.281 , pp. 698-700
    • Springer, S.1    Schekman, R.2
  • 41
    • 0037193471 scopus 로고    scopus 로고
    • ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat
    • Rein U, Andag U, Duden R, Schmitt HD, Spang A. ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat. J Cell Biol 2002;157:395-404.
    • (2002) J. Cell Biol. , vol.157 , pp. 395-404
    • Rein, U.1    Andag, U.2    Duden, R.3    Schmitt, H.D.4    Spang, A.5
  • 42
    • 0032215324 scopus 로고    scopus 로고
    • Coat assembly directs v-SNARE concentration into synthetic COPII vesicles
    • Matsuoka K, Morimitsu Y, Uchida K, Schekman R. Coat assembly directs v-SNARE concentration into synthetic COPII vesicles. Mol Cell 1998;2:703-708.
    • (1998) Mol. Cell , vol.2 , pp. 703-708
    • Matsuoka, K.1    Morimitsu, Y.2    Uchida, K.3    Schekman, R.4
  • 43
    • 0038529726 scopus 로고    scopus 로고
    • The SNARE motif contributes to rbet1 intracellular targeting and dynamics independently of SNARE interactions
    • Joglekar AP, Xu D, Rigotti DJ, Fairman R, Hay JC. The SNARE motif contributes to rbet1 intracellular targeting and dynamics independently of SNARE interactions. J Biol Chem 2003;278:14121-14133.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14121-14133
    • Joglekar, A.P.1    Xu, D.2    Rigotti, D.J.3    Fairman, R.4    Hay, J.C.5
  • 44
    • 0029005106 scopus 로고
    • A targeting signal in VAMP regulating transport to synaptic vesicles
    • Grote E, Hao JC, Bennett MK, Kelly RB. A targeting signal in VAMP regulating transport to synaptic vesicles. Cell 1995;81:581-589.
    • (1995) Cell , vol.81 , pp. 581-589
    • Grote, E.1    Hao, J.C.2    Bennett, M.K.3    Kelly, R.B.4
  • 45
    • 0034735540 scopus 로고    scopus 로고
    • A selective transport route from Golgi to late endosomes that requires the yeast GGA proteins
    • Black MW, Pelham HR. A selective transport route from Golgi to late endosomes that requires the yeast GGA proteins. J Cell Biol 2000;151:587-600.
    • (2000) J. Cell Biol. , vol.151 , pp. 587-600
    • Black, M.W.1    Pelham, H.R.2
  • 46
    • 0041328109 scopus 로고    scopus 로고
    • Molecular recognition of cargo by the COPII complex: A most accommodating coat
    • Barlowe C. Molecular recognition of cargo by the COPII complex: a most accommodating coat. Cell 2003;112:395-399.
    • (2003) Cell , vol.112 , pp. 395-399
    • Barlowe, C.1
  • 47
    • 0037323502 scopus 로고    scopus 로고
    • Mammalian Ykt6 is a neuronal SNARE targeted to a specialized compartment by its profilin-like amino terminal domain
    • Hasegawa H, Zinsser S, Rhee Y, Vik-Mo EO, Davanger S, Hay JC. Mammalian Ykt6 is a neuronal SNARE targeted to a specialized compartment by its profilin-like amino terminal domain. Mol Biol Cell 2003;14:698-720.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 698-720
    • Hasegawa, H.1    Zinsser, S.2    Rhee, Y.3    Vik-Mo, E.O.4    Davanger, S.5    Hay, J.C.6
  • 49
    • 0033597815 scopus 로고    scopus 로고
    • SNAP-25 is targeted to the plasma membrane through a novel membrane-binding domain
    • Gonzalo S, Greentree WK, Linder ME. SNAP-25 is targeted to the plasma membrane through a novel membrane-binding domain. J Biol Chem 1999;274:21313-21318.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21313-21318
    • Gonzalo, S.1    Greentree, W.K.2    Linder, M.E.3
  • 50
    • 0037072816 scopus 로고    scopus 로고
    • SNAP-25 traffics to the plasma membrane by a syntaxin-independent mechanism
    • Loranger SS, Linder ME. SNAP-25 traffics to the plasma membrane by a syntaxin-independent mechanism. J Biol Chem 2002;277:34303-34309.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34303-34309
    • Loranger, S.S.1    Linder, M.E.2
  • 51
    • 0034599993 scopus 로고    scopus 로고
    • Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes
    • Cao X, Barlowe C. Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes. J Cell Biol 2000;149:55-56.
    • (2000) J. Cell Biol. , vol.149 , pp. 55-56
    • Cao, X.1    Barlowe, C.2
  • 52
    • 0037086618 scopus 로고    scopus 로고
    • Yeast vacuoles and membrane fusion pathways
    • Wickner W. Yeast vacuoles and membrane fusion pathways. EMBO J 2002;21:1241-1247.
    • (2002) EMBO J. , vol.21 , pp. 1241-1247
    • Wickner, W.1
  • 53
    • 0037377234 scopus 로고    scopus 로고
    • Vesicle trafficking, pleasure and pain from SM genes
    • Toonen RF, Verhage M. Vesicle trafficking, pleasure and pain from SM genes. Trends Cell Biol 2003;13:177-186.
    • (2003) Trends Cell Biol. , vol.13 , pp. 177-186
    • Toonen, R.F.1    Verhage, M.2
  • 54
    • 0036193747 scopus 로고    scopus 로고
    • Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
    • Yamaguchi T, Dulubova I, Min SW, Chen X, Rizo J, Südhof TC. Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev Cell 2002;2:295-305.
    • (2002) Dev. Cell , vol.2 , pp. 295-305
    • Yamaguchi, T.1    Dulubova, I.2    Min, S.W.3    Chen, X.4    Rizo, J.5    Südhof, T.C.6
  • 55
    • 0035796402 scopus 로고    scopus 로고
    • Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation
    • Bryant NJ, James DE. Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation. EMBO J 2001;20:3380-3388.
    • (2001) EMBO J. , vol.20 , pp. 3380-3388
    • Bryant, N.J.1    James, D.E.2
  • 57
    • 0036166318 scopus 로고    scopus 로고
    • Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs
    • Antonin W, Fasshauer D, Becker S, Jahn R, Schneider TR. Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs. Nat Struct Biol 2002;9:107-111.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 107-111
    • Antonin, W.1    Fasshauer, D.2    Becker, S.3    Jahn, R.4    Schneider, T.R.5
  • 58
    • 0035968198 scopus 로고    scopus 로고
    • A novel snare N-terminal domain revealed by the crystal structure of Sec22b
    • Gonzalez LC, Weis WI, Scheller RH. A novel snare N-terminal domain revealed by the crystal structure of Sec22b. J Biol Chem 2001;276: 24203-24211.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24203-24211
    • Gonzalez, L.C.1    Weis, W.I.2    Scheller, R.H.3
  • 59
    • 0037112932 scopus 로고    scopus 로고
    • Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p
    • Bracher A, Weissenhorn W. Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p. EMBO J 2002;21:6114-6124.
    • (2002) EMBO J. , vol.21 , pp. 6114-6124
    • Bracher, A.1    Weissenhorn, W.2
  • 60
    • 0035958644 scopus 로고    scopus 로고
    • An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p
    • Tochio H, Tsui MM, Banfield DK, Zhang M. An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p. Science 2001;293:698-702.
    • (2001) Science , vol.293 , pp. 698-702
    • Tochio, H.1    Tsui, M.M.2    Banfield, D.K.3    Zhang, M.4
  • 62
    • 0033880985 scopus 로고    scopus 로고
    • Identification of domains required for developmentally regulated SNARE function in Saccharomyces cerevisiae
    • Neiman AM, Katz L, Brennwald PJ. Identification of domains required for developmentally regulated SNARE function in Saccharomyces cerevisiae. Genetics 2000;155:1643-1655.
    • (2000) Genetics , vol.155 , pp. 1643-1655
    • Neiman, A.M.1    Katz, L.2    Brennwald, P.J.3
  • 63
    • 0038136900 scopus 로고    scopus 로고
    • Molecular interactions of yeast frequenin (Frq1) with the phosphatidylinositol 4-kinase isoform, Pik1
    • Huttner IG, Strahl T, Osawa M, King DS, Ames JB, Thorner J. Molecular interactions of yeast frequenin (Frq1) with the phosphatidylinositol 4-kinase isoform, Pik1. J Biol Chem 2003;278: 4862-4874.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4862-4874
    • Huttner, I.G.1    Strahl, T.2    Osawa, M.3    King, D.S.4    Ames, J.B.5    Thorner, J.6
  • 64
    • 0027294075 scopus 로고
    • The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20p
    • Sweet DJ, Pelham HR. The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20p. EMBO J 1993;12: 2831-2840.
    • (1993) EMBO J. , vol.12 , pp. 2831-2840
    • Sweet, D.J.1    Pelham, H.R.2
  • 66
    • 0036180245 scopus 로고    scopus 로고
    • Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle
    • Wang L, Seeley ES, Wickner W, Merz AJ. Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle. Cell 2002;108:357-369.
    • (2002) Cell , vol.108 , pp. 357-369
    • Wang, L.1    Seeley, E.S.2    Wickner, W.3    Merz, A.J.4
  • 69
  • 70
    • 0037184043 scopus 로고    scopus 로고
    • The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly
    • Antonin W, Dulubova I, Arac D, Pabst S, Plitzner J, Rizo J, Jahn R. The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly. J Biol Chem 2002;277:36449-36456.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36449-36456
    • Antonin, W.1    Dulubova, I.2    Arac, D.3    Pabst, S.4    Plitzner, J.5    Rizo, J.6    Jahn, R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.