메뉴 건너뛰기




Volumn 4, Issue 1, 1999, Pages 97-107

NSF N-terminal domain crystal structure: Models of NSF function

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

EID: 0033165864     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80191-4     Document Type: Article
Times cited : (107)

References (60)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J.P., and Leslie, A.G.W. (1996). Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D 52, 30-42.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 2
    • 0029996161 scopus 로고    scopus 로고
    • Domains of α-SNAP required for the stimulation of exocytosis and for N-ethylmaleimide-sensitive fusion protein (NSF) binding and activation
    • Barnard, R.J.O., Morgan, A., and Burgoyne, R.D. (1996). Domains of α-SNAP required for the stimulation of exocytosis and for N-ethylmaleimide-sensitive fusion protein (NSF) binding and activation. Mol. Biol. Cell 7, 693-701.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 693-701
    • Barnard, R.J.O.1    Morgan, A.2    Burgoyne, R.D.3
  • 3
    • 0030682481 scopus 로고    scopus 로고
    • Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis
    • Barnard, R.J.O., Morgan, A., and Burgoyne, R.D. (1997). Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis. J. Cell Biol. 139, 875-883.
    • (1997) J. Cell Biol. , vol.139 , pp. 875-883
    • Barnard, R.J.O.1    Morgan, A.2    Burgoyne, R.D.3
  • 4
    • 0027404604 scopus 로고
    • The molecular machinery for secretion is conserved from yeast to neurons
    • Bennett, M.K., and Scheller, R.H. (1993). The molecular machinery for secretion is conserved from yeast to neurons. Proc. Natl. Acad. Sci USA 90, 2559-2563.
    • (1993) Proc. Natl. Acad. Sci USA , vol.90 , pp. 2559-2563
    • Bennett, M.K.1    Scheller, R.H.2
  • 5
    • 0030867609 scopus 로고    scopus 로고
    • Sequence analysis of the AAA protein family
    • Beyer, A. (1997). Sequence analysis of the AAA protein family. Prot. Sci. 6, 2043-2058.
    • (1997) Prot. Sci. , vol.6 , pp. 2043-2058
    • Beyer, A.1
  • 7
    • 0030038545 scopus 로고    scopus 로고
    • Direct observation of protein solvation and discrete disorder with experimental crystallographic phases
    • Burling, F.T., Weis, W.I., Flaherty, K.M., and Brunger, AT. (1996). Direct observation of protein solvation and discrete disorder with experimental crystallographic phases. Science 271, 72-77.
    • (1996) Science , vol.271 , pp. 72-77
    • Burling, F.T.1    Weis, W.I.2    Flaherty, K.M.3    Brunger, A.T.4
  • 9
    • 0029328549 scopus 로고
    • A 200 amino acid ATPase module in search of a basic function
    • Confalonieri, F., and Duguet, M. (1995). A 200 amino acid ATPase module in search of a basic function. Bioessays 17, 639-650.
    • (1995) Bioessays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 10
    • 0030729838 scopus 로고    scopus 로고
    • Bobscript: An extensively modified version of molscript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. (1997). Bobscript: An extensively modified version of molscript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model 15, 132-134.
    • (1997) J. Mol. Graph. Model , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 11
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novick, S., and Jahn, R. (1994). Vesicle fusion from yeast to man. Nature 370, 191-193.
    • (1994) Nature , vol.370 , pp. 191-193
    • Ferro-Novick, S.1    Jahn, R.2
  • 13
    • 0033199044 scopus 로고    scopus 로고
    • A highly automated heavy-atom search procedure for macromolecular structures
    • in press
    • Grosse-Kunstleve, R.W., and Brunger, AT. (1999). A highly automated heavy-atom search procedure for macromolecular structures. Acta Crystallogr. D, in press.
    • (1999) Acta Crystallogr. D
    • Grosse-Kunstleve, R.W.1    Brunger, A.T.2
  • 14
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., Roth, R., Morisaki, H., Jahn, R., and Heuser, J.E. (1997). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 15
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay, J.C., and Scheller, R.H. (1997). SNAREs and NSF in targeted membrane fusion. Curr. Opin. Cell Biol. 9, 505-512.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.H.2
  • 16
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • Hayashi, T., McMahon, H., Yamasaki, S., Binz, T., Hata, Y., Südhof, T.C., and Niemann, H. (1994). Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly. EMBO J. 13, 5051-5061.
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1    McMahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Südhof, T.C.6    Niemann, H.7
  • 17
    • 0029004741 scopus 로고
    • Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro
    • Hayashi, T., Yamasaki, S., Nauenburg, S., Binz, T., and Niemann, H. (1995). Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro. EMBO J. 14, 2317-2325.
    • (1995) EMBO J. , vol.14 , pp. 2317-2325
    • Hayashi, T.1    Yamasaki, S.2    Nauenburg, S.3    Binz, T.4    Niemann, H.5
  • 18
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structures
    • Hendrickson, W.A. (1985). Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115, 252-270.
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 19
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchotron radiation
    • Hendrickson, W.A. (1991). Determination of macromolecular structures from anomalous diffraction of synchotron radiation. Science 254, 51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 20
    • 0032214690 scopus 로고    scopus 로고
    • Arrangement of subunits in 20S particles consisting of NSF, SNAPs, and SNARE complexes
    • Hohl, T.M., Paralti, F., Wimmer, C., Rothman, J.E., Söllner, T.H., and Engelhardt, H. (1998). Arrangement of subunits in 20S particles consisting of NSF, SNAPs, and SNARE complexes. Mol. Cell 2, 539-548.
    • (1998) Mol. Cell , vol.2 , pp. 539-548
    • Hohl, T.M.1    Paralti, F.2    Wimmer, C.3    Rothman, J.E.4    Söllner, T.H.5    Engelhardt, H.6
  • 21
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices (Dali 2.0)
    • Holm, L., and Sander, C. (1993). Protein structure comparison by alignment of distance matrices (Dali 2.0). J. Mol. Biol. 233,123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 22
    • 0028172551 scopus 로고
    • Protein hydration observed by x-ray diffraction: Solvation properties of penicillopepsin and neuramidase crystal structures
    • Jiang, J.S., and Brunger, A.T. (1994). Protein hydration observed by x-ray diffraction: Solvation properties of penicillopepsin and neuramidase crystal structures. J. Mol. Biol. 243, 100-115.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brunger, A.T.2
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 24
    • 33645941402 scopus 로고
    • The OPLS potential functions for protein energy minimizations for crystals of cyclic peptide and crambin
    • Jorgensen, W.L., and Tirado-Rives, J. (1988). The OPLS potential functions for protein energy minimizations for crystals of cyclic peptide and crambin. J. Am. Chem. Soc. 110, 1657-1666.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 25
    • 0030584663 scopus 로고    scopus 로고
    • A complex profile of protein elongation: Translating chemical energy into molecular movement
    • Jurnak, F., and Abel, K. (1996). A complex profile of protein elongation: Translating chemical energy into molecular movement. Structure 4, 229-238.
    • (1996) Structure , vol.4 , pp. 229-238
    • Jurnak, F.1    Abel, K.2
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983). Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 27
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
    • Kjeldgaard, M., Nissen, P., Thirup, S., and Nyborg, J. (1993). The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure 1, 35-50.
    • (1993) Structure , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3    Nyborg, J.4
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 29
    • 0028881975 scopus 로고
    • SURFNET: A program for visualizing molecular surfaces, cavities and intermolecular interactions
    • Laskowski, R.A. (1995). SURFNET: A program for visualizing molecular surfaces, cavities and intermolecular interactions. J. Mol. Graph. 13, 323-330.
    • (1995) J. Mol. Graph. , vol.13 , pp. 323-330
    • Laskowski, R.A.1
  • 30
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence, M.C., and Colman, P.M. (1993). Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234, 946-950.
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 31
    • 0033602381 scopus 로고    scopus 로고
    • Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease
    • Leonhard, K., Stiegler, A., Neupert, W., and Langer, T. (1999). Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease. Nature 398, 348-350.
    • (1999) Nature , vol.398 , pp. 348-350
    • Leonhard, K.1    Stiegler, A.2    Neupert, W.3    Langer, T.4
  • 32
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen, C.U., Steinmann, D., Whiteheart, S.W., and Weis, W.I. (1998). Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 33
    • 0027764344 scopus 로고
    • Protein sequence alignments: A strategy for the hierarchical analysis of residue conservation
    • Livingstone, C.D., and Barton, G.J. (1993). Protein sequence alignments: A strategy for the hierarchical analysis of residue conservation. Comput. Appl. Biosci. 9, 745-756.
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 745-756
    • Livingstone, C.D.1    Barton, G.J.2
  • 34
    • 0033163807 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein
    • May, A.P., Misura, K.M.S., Whiteheart, S.W., and Weis, W.I. (1999). Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein. Nat. Cell Biol. 1, 175-182.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 175-182
    • May, A.P.1    Misura, K.M.S.2    Whiteheart, S.W.3    Weis, W.I.4
  • 35
    • 0028870106 scopus 로고
    • A role for the soluble NSF attachment proteins (SNAPs) in regulated exocytosis in adrenal chromaffin cells
    • Morgan, A., and Burgoyne, R.D. (1995). A role for the soluble NSF attachment proteins (SNAPs) in regulated exocytosis in adrenal chromaffin cells. Eur. Mol. Biol. Organ. J. 14, 232-239.
    • (1995) Eur. Mol. Biol. Organ. J. , vol.14 , pp. 232-239
    • Morgan, A.1    Burgoyne, R.D.2
  • 36
    • 0028149757 scopus 로고
    • The ATPase activity of N-ethylmaleimide-sensitive fusion protein NSF is regulated by soluble NSF attachment proteins
    • Morgan, A., Dimaline, R., and Burgoyne, R.D. (1994). The ATPase activity of N-ethylmaleimide-sensitive fusion protein NSF is regulated by soluble NSF attachment proteins. J. Biol. Chem. 269, 29347-29350.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29347-29350
    • Morgan, A.1    Dimaline, R.2    Burgoyne, R.D.3
  • 37
    • 0028802295 scopus 로고
    • Each domain of N-ethylmaleimide-sensitive fusion protein contributes to its transport activity
    • Nagiec, E.E., Bernstein, A., and Whiteheart, S.W. (1995). Each domain of N-ethylmaleimide-sensitive fusion protein contributes to its transport activity. J. Biol. Chem. 49, 29182-29188.
    • (1995) J. Biol. Chem. , vol.49 , pp. 29182-29188
    • Nagiec, E.E.1    Bernstein, A.2    Whiteheart, S.W.3
  • 38
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • Pannu, N.S., and Read, R.J. (1996). Improved structure refinement through maximum likelihood. Acta Crystallogr. A 52, 659-668.
    • (1996) Acta Crystallogr. A , vol.52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 41
    • 0031973716 scopus 로고
    • The AAA team: Related ATPases with diverse functions
    • Patel, S., and Latterich, M. (1993). The AAA team: Related ATPases with diverse functions. Trends Cell Biol. 8, 65-71.
    • (1993) Trends Cell Biol. , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 42
    • 0000019861 scopus 로고
    • The use of anomalous scattering effects to phase diffraction patterson from macromolecules
    • Phillips, J.C., and Hodgson, K.O. (1980). The use of anomalous scattering effects to phase diffraction patterson from macromolecules. Acta Crystallogr. A 36, 856-864.
    • (1980) Acta Crystallogr. A , vol.36 , pp. 856-864
    • Phillips, J.C.1    Hodgson, K.O.2
  • 44
    • 0003550794 scopus 로고    scopus 로고
    • Indianapolis, IN: Cyborg Software Systems, Inc.
    • The POV-ray Team. (1998). Pov-ray - The Persistence of Vision Ray-Tracer (http://www.povray.org/) (Indianapolis, IN: Cyborg Software Systems, Inc.).
    • (1998) Pov-ray - The Persistence of Vision Ray-Tracer
  • 45
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 46
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • Rice, L.M., and Brunger, A.T. (1994). Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement. Proteins 19, 277-290.
    • (1994) Proteins , vol.19 , pp. 277-290
    • Rice, L.M.1    Brunger, A.T.2
  • 47
    • 0033165863 scopus 로고    scopus 로고
    • Crystal structure of the vesicular transport protein sec17: Implications for SNAP function in SNARE complex disassembly
    • this issue
    • Rice, L.M., and Brunger, A.T. (1999). Crystal structure of the vesicular transport protein sec17: Implications for SNAP function in SNARE complex disassembly. Mol. Cell 4, this issue, 85-95.
    • (1999) Mol. Cell , vol.4 , pp. 85-95
    • Rice, L.M.1    Brunger, A.T.2
  • 48
    • 0030020733 scopus 로고    scopus 로고
    • The protein machinery of vesicle budding and fusion
    • Rothman, J.E. (1996). The protein machinery of vesicle budding and fusion. Prot. Sci. 5, 185-194.
    • (1996) Prot. Sci. , vol.5 , pp. 185-194
    • Rothman, J.E.1
  • 49
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Söllner, T., Bennett, M.K., Whiteheart, S.W., Scheller, R.H., and Rothman, J.E. (1993). A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 50
    • 0028096570 scopus 로고
    • Role of two nucleotide-binding regions in an N-ethylmaleimide-sensitive factor involved in vesicle-mediated protein transport
    • Sumida, M., Hong, R.-M., and Tayaga, M. (1994). Role of two nucleotide-binding regions in an N-ethylmaleimide-sensitive factor involved in vesicle-mediated protein transport. J. Biol. Chem. 269, 20636-20641.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20636-20641
    • Sumida, M.1    Hong, R.-M.2    Tayaga, M.3
  • 51
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 å resolution
    • Sutton, R.B., Fasshauer, D., Jahn, R., and Brunger, AT. (1998). Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 å resolution. Nature 395, 347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 52
    • 0027474007 scopus 로고
    • Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport
    • Tayaga, M., Wilson, D.W., Brunner, M., Arango, N., and Rothman, J.E. (1993). Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport. J. Biol. Chem. 268, 2662-2666.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2662-2666
    • Tayaga, M.1    Wilson, D.W.2    Brunner, M.3    Arango, N.4    Rothman, J.E.5
  • 53
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994). CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 54
    • 0001607723 scopus 로고
    • Distantly related sequences in the beta- and gamma-subunits of ATPase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M.J., Runswick, J.J., and Gay, N.J. (1982). Distantly related sequences in the beta- and gamma-subunits of ATPase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.J.2    Runswick, J.J.3    Gay, N.J.4
  • 57
    • 0026720008 scopus 로고
    • Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in golgi membranes
    • Whiteheart, S.W., Brunner, M., Wilson, D.W., Wiedmann, M., and Rothman, J.E. (1992). Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAPreceptor complex in golgi membranes. J. Biol. Chem. 267, 12239-12243.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12239-12243
    • Whiteheart, S.W.1    Brunner, M.2    Wilson, D.W.3    Wiedmann, M.4    Rothman, J.E.5
  • 58
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart, S.W., Rossnagel, K., Buhrow, S.A., Brunner, M., Jaenicke, R., and Rothman, J.E. (1994). N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol. 126, 945-954.
    • (1994) J. Cell Biol. , vol.126 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 59
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu, R.C., Hanson, P.I., Jahn, R., and Brunger, A.T. (1998). Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat. Struct. Biol. 5, 803-811.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4
  • 60
    • 84944812185 scopus 로고
    • Histogram matching as a new density modification technique for phase refinement and extension of protein molecules
    • Zhang, K.Y.J., and Main, P. (1990). Histogram matching as a new density modification technique for phase refinement and extension of protein molecules. Acta Crystallogr. A 46, 41-46.
    • (1990) Acta Crystallogr. A , vol.46 , pp. 41-46
    • Zhang, K.Y.J.1    Main, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.