메뉴 건너뛰기




Volumn 24, Issue 3, 2017, Pages 205-213

Structural basis of dual Ca 2+ /pH regulation of the endolysosomal TRPML1 channel

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CYSTEINE; PROTEIN TRPML1; PROTON; TETRAMER; TRANSIENT RECEPTOR POTENTIAL CHANNEL; UNCLASSIFIED DRUG; AMINO ACID; CALCIUM; PROTEIN BINDING; PROTEIN SUBUNIT; TRANSIENT RECEPTOR POTENTIAL CHANNEL M; TRPM1 PROTEIN, HUMAN;

EID: 85010872102     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3362     Document Type: Article
Times cited : (80)

References (63)
  • 1
    • 84930539972 scopus 로고    scopus 로고
    • Organellar channels and transporters
    • Xu, H., Martinoia, E. & Szabo, I. Organellar channels and transporters. Cell Calcium 58, 1-10 (2015).
    • (2015) Cell Calcium , vol.58 , pp. 1-10
    • Xu, H.1    Martinoia, E.2    Szabo, I.3
  • 2
    • 84884540088 scopus 로고    scopus 로고
    • Intracellular ion channels and cancer
    • Leanza, L. et al. Intracellular ion channels and cancer. Front. Physiol. 4, 227 (2013).
    • (2013) Front. Physiol. , vol.4 , pp. 227
    • Leanza, L.1
  • 4
    • 84873690749 scopus 로고    scopus 로고
    • Chloride in vesicular trafficking and function
    • Stauber, T. & Jentsch, T.J. Chloride in vesicular trafficking and function. Annu. Rev. Physiol. 75, 453-477 (2013).
    • (2013) Annu. Rev. Physiol. , vol.75 , pp. 453-477
    • Stauber, T.1    Jentsch, T.J.2
  • 5
    • 84922794140 scopus 로고    scopus 로고
    • Lysosomal physiology
    • Xu, H. & Ren, D. Lysosomal physiology. Annu. Rev. Physiol. 77, 57-80 (2015).
    • (2015) Annu. Rev. Physiol. , vol.77 , pp. 57-80
    • Xu, H.1    Ren, D.2
  • 6
    • 84930541540 scopus 로고    scopus 로고
    • The role of TRPMLs in endolysosomal trafficking and function
    • Venkatachalam, K., Wong, C.O. & Zhu, M.X. The role of TRPMLs in endolysosomal trafficking and function. Cell Calcium 58, 48-56 (2015).
    • (2015) Cell Calcium , vol.58 , pp. 48-56
    • Venkatachalam, K.1    Wong, C.O.2    Zhu, M.X.3
  • 7
    • 84924065856 scopus 로고    scopus 로고
    • 2+-permeable channels
    • 2+-permeable channels. Cell Calcium 57, 222-230 (2015).
    • (2015) Cell Calcium , vol.57 , pp. 222-230
    • Patel, S.1    Cai, X.2
  • 8
    • 0035499903 scopus 로고    scopus 로고
    • Regulation of Ins(1,4,5)P3 receptor isoforms by endogenous modulators
    • Thrower, E.C., Hagar, R.E. & Ehrlich, B.E. Regulation of Ins(1,4,5)P3 receptor isoforms by endogenous modulators. Trends Pharmacol. Sci. 22, 580-586 (2001).
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 580-586
    • Thrower, E.C.1    Hagar, R.E.2    Ehrlich, B.E.3
  • 9
    • 0028180422 scopus 로고
    • 2+ release channels and their regulation by endogenous effectors
    • 2+ release channels and their regulation by endogenous effectors. Annu. Rev. Physiol. 56, 485-508 (1994).
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 485-508
    • Meissner, G.1
  • 11
    • 84960906119 scopus 로고    scopus 로고
    • Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana
    • Guo, J. et al. Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana. Nature 531, 196-201 (2016).
    • (2016) Nature , vol.531 , pp. 196-201
    • Guo, J.1
  • 12
    • 84898630877 scopus 로고    scopus 로고
    • Convergent regulation of the lysosomal two-pore channel-2 by Mg2, NAADP, PI(3,5)P and multiple protein kinases
    • Jha, A., Ahuja, M., Patel, S., Brailoiu, E. & Muallem, S. Convergent regulation of the lysosomal two-pore channel-2 by Mg2, NAADP, PI(3,5)P and multiple protein kinases. EMBO J. 33, 501-511 (2014).
    • (2014) EMBO J. , vol.33 , pp. 501-511
    • Jha, A.1    Ahuja, M.2    Patel, S.3    Brailoiu, E.4    Muallem, S.5
  • 13
    • 0034641869 scopus 로고    scopus 로고
    • Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel
    • Sun, M. et al. Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel. Hum. Mol. Genet. 9, 2471-2478 (2000).
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2471-2478
    • Sun, M.1
  • 14
    • 0033822172 scopus 로고    scopus 로고
    • Identification of the gene causing mucolipidosis type IV
    • Bargal, R. et al. Identification of the gene causing mucolipidosis type IV. Nat. Genet. 26, 118-123 (2000).
    • (2000) Nat. Genet. , vol.26 , pp. 118-123
    • Bargal, R.1
  • 15
    • 0033760264 scopus 로고    scopus 로고
    • Cloning of the gene encoding a novel integral membrane protein, mucolipidin-and identification of the two major founder mutations causing mucolipidosis type IV
    • Bassi, M.T. et al. Cloning of the gene encoding a novel integral membrane protein, mucolipidin-and identification of the two major founder mutations causing mucolipidosis type IV. Am. J. Hum. Genet. 67, 1110-1120 (2000).
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 1110-1120
    • Bassi, M.T.1
  • 16
    • 0023988795 scopus 로고
    • Clinical spectrum of mucolipidosis type IV
    • Weitz, R. & Kohn, G. Clinical spectrum of mucolipidosis type IV. Pediatrics 81, 602-603 (1988).
    • (1988) Pediatrics , vol.81 , pp. 602-603
    • Weitz, R.1    Kohn, G.2
  • 17
    • 0034894817 scopus 로고    scopus 로고
    • Mucolipidosis type IV
    • Bach, G. Mucolipidosis type IV. Mol. Genet. Metab. 73, 197-203 (2001).
    • (2001) Mol. Genet. Metab. , vol.73 , pp. 197-203
    • Bach, G.1
  • 19
    • 30044439235 scopus 로고    scopus 로고
    • TRP-ML1 is a lysosomal monovalent cation channel that undergoes proteolytic cleavage
    • Kiselyov, K. et al. TRP-ML1 is a lysosomal monovalent cation channel that undergoes proteolytic cleavage. J. Biol. Chem. 280, 43218-43223 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 43218-43223
    • Kiselyov, K.1
  • 20
    • 54049156405 scopus 로고    scopus 로고
    • The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
    • Dong, X.P. et al. The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature 455, 992-996 (2008).
    • (2008) Nature , vol.455 , pp. 992-996
    • Dong, X.P.1
  • 21
    • 70450236985 scopus 로고    scopus 로고
    • Activating mutations of the TRPML1 channel revealed by proline-scanning mutagenesis
    • Dong, X.P. et al. Activating mutations of the TRPML1 channel revealed by proline-scanning mutagenesis. J. Biol. Chem. 284, 32040-32052 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 32040-32052
    • Dong, X.P.1
  • 22
    • 80051473235 scopus 로고    scopus 로고
    • 2+ release channels in the endolysosome
    • 2+ release channels in the endolysosome. Nat. Commun. 1, 38 (2010).
    • (2010) Nat. Commun. , vol.1 , pp. 38
    • Dong, X.P.1
  • 23
    • 77949695459 scopus 로고    scopus 로고
    • TRP channels of intracellular membranes
    • Dong, X.P., Wang, X. & Xu, H. TRP channels of intracellular membranes. J. Neurochem. 113, 313-328 (2010).
    • (2010) J. Neurochem. , vol.113 , pp. 313-328
    • Dong, X.P.1    Wang, X.2    Xu, H.3
  • 24
    • 33751120702 scopus 로고    scopus 로고
    • Lysosomal exocytosis is impaired in mucolipidosis type IV
    • LaPlante, J.M. et al. Lysosomal exocytosis is impaired in mucolipidosis type IV. Mol. Genet. Metab. 89, 339-348 (2006).
    • (2006) Mol. Genet. Metab. , vol.89 , pp. 339-348
    • LaPlante, J.M.1
  • 25
    • 84884154195 scopus 로고    scopus 로고
    • A TRP channel in the lysosome regulates large particle phagocytosis via focal exocytosis
    • Samie, M. et al. A TRP channel in the lysosome regulates large particle phagocytosis via focal exocytosis. Dev. Cell 26, 511-524 (2013).
    • (2013) Dev. Cell , vol.26 , pp. 511-524
    • Samie, M.1
  • 26
    • 45149103982 scopus 로고    scopus 로고
    • Membrane traffic and turnover in TRP-ML1-deficient cells: A revised model for mucolipidosis type IV pathogenesis
    • Miedel, M.T. et al. Membrane traffic and turnover in TRP-ML1-deficient cells: a revised model for mucolipidosis type IV pathogenesis. J. Exp. Med. 205, 1477-1490 (2008).
    • (2008) J. Exp. Med. , vol.205 , pp. 1477-1490
    • Miedel, M.T.1
  • 27
    • 84960158035 scopus 로고    scopus 로고
    • A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation
    • Li, X. et al. A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation. Nat. Cell Biol. 18, 404-417 (2016).
    • (2016) Nat. Cell Biol. , vol.18 , pp. 404-417
    • Li, X.1
  • 28
    • 56349119573 scopus 로고    scopus 로고
    • Motor deficit in a Drosophila model of mucolipidosis type IV due to defective clearance of apoptotic cells
    • Venkatachalam, K. et al. Motor deficit in a Drosophila model of mucolipidosis type IV due to defective clearance of apoptotic cells. Cell 135, 838-851 (2008).
    • (2008) Cell , vol.135 , pp. 838-851
    • Venkatachalam, K.1
  • 30
    • 84977119521 scopus 로고    scopus 로고
    • MCOLN1 is a ROS sensor in lysosomes that regulates autophagy
    • Zhang, X. et al. MCOLN1 is a ROS sensor in lysosomes that regulates autophagy. Nat. Commun. 7, 12109 (2016).
    • (2016) Nat. Commun. , vol.7 , pp. 12109
    • Zhang, X.1
  • 31
    • 12144285845 scopus 로고    scopus 로고
    • Molecular pathophysiology of mucolipidosis type IV: PH dysregulation of the mucolipin-1 cation channel
    • Raychowdhury, M.K. et al. Molecular pathophysiology of mucolipidosis type IV: pH dysregulation of the mucolipin-1 cation channel. Hum. Mol. Genet. 13, 617-627 (2004).
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 617-627
    • Raychowdhury, M.K.1
  • 32
    • 26444444017 scopus 로고    scopus 로고
    • Cation channel activity of mucolipin-1: The effect of calcium
    • Cantiello, H.F. et al. Cation channel activity of mucolipin-1: the effect of calcium. Pflugers Arch. 451, 304-312 (2005).
    • (2005) Pflugers Arch. , vol.451 , pp. 304-312
    • Cantiello, H.F.1
  • 33
    • 84863922724 scopus 로고    scopus 로고
    • Phosphoinositide isoforms determine compartment-specific ion channel activity
    • Zhang, X., Li, X. & Xu, H. Phosphoinositide isoforms determine compartment-specific ion channel activity. Proc. Natl. Acad. Sci. USA 109, 11384-11389 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 11384-11389
    • Zhang, X.1    Li, X.2    Xu, H.3
  • 35
    • 79959804266 scopus 로고    scopus 로고
    • Transient receptor potential genes and human inherited disease
    • Everett, K.V. Transient receptor potential genes and human inherited disease. Adv. Exp. Med. Biol. 704, 1011-1032 (2011).
    • (2011) Adv. Exp. Med. Biol. , vol.704 , pp. 1011-1032
    • Everett, K.V.1
  • 36
    • 0035032399 scopus 로고    scopus 로고
    • Mucolipidosis type IV: Novel MCOLN1 mutations in Jewish and non-Jewish patients and the frequency of the disease in the Ashkenazi Jewish population
    • Bargal, R. et al. Mucolipidosis type IV: novel MCOLN1 mutations in Jewish and non-Jewish patients and the frequency of the disease in the Ashkenazi Jewish population. Hum. Mutat. 17, 397-402 (2001).
    • (2001) Hum. Mutat. , vol.17 , pp. 397-402
    • Bargal, R.1
  • 38
    • 36749008553 scopus 로고    scopus 로고
    • Activating mutation in a mucolipin transient receptor potential channel leads to melanocyte loss in varitint-waddler mice
    • Xu, H., Delling, M., Li, L., Dong, X. & Clapham, D.E. Activating mutation in a mucolipin transient receptor potential channel leads to melanocyte loss in varitint-waddler mice. Proc. Natl. Acad. Sci. USA 104, 18321-18326 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18321-18326
    • Xu, H.1    Delling, M.2    Li, L.3    Dong, X.4    Clapham, D.E.5
  • 39
    • 37649014647 scopus 로고    scopus 로고
    • A helix-breaking mutation in TRPML3 leads to constitutive activity underlying deafness in the varitint-waddler mouse
    • Grimm, C. et al. A helix-breaking mutation in TRPML3 leads to constitutive activity underlying deafness in the varitint-waddler mouse. Proc. Natl. Acad. Sci. USA 104, 19583-19588 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19583-19588
    • Grimm, C.1
  • 40
    • 37549009562 scopus 로고    scopus 로고
    • Gain-of-function mutation in TRPML3 causes the mouse Varitint-Waddler phenotype
    • Kim, H.J. et al. Gain-of-function mutation in TRPML3 causes the mouse Varitint-Waddler phenotype. J. Biol. Chem. 282, 36138-36142 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 36138-36142
    • Kim, H.J.1
  • 41
    • 0037069373 scopus 로고    scopus 로고
    • Mutations in Mcoln3 associated with deafness and pigmentation defects in varitint-waddler (Va) mice
    • Di Palma, F. et al. Mutations in Mcoln3 associated with deafness and pigmentation defects in varitint-waddler (Va) mice. Proc. Natl. Acad. Sci. USA 99, 14994-14999 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14994-14999
    • Di Palma, F.1
  • 42
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112 (2013).
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 43
    • 33748572921 scopus 로고    scopus 로고
    • Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide traffic
    • Pryor, P.R., Reimann, F., Gribble, F.M. & Luzio, J.P. Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide traffic. Traffic 7, 1388-1398 (2006).
    • (2006) Traffic , vol.7 , pp. 1388-1398
    • Pryor, P.R.1    Reimann, F.2    Gribble, F.M.3    Luzio, J.P.4
  • 44
    • 2942529414 scopus 로고    scopus 로고
    • Overexpression of wild-type and mutant mucolipin proteins in mammalian cells: Effects on the late endocytic compartment organization
    • Manzoni, M. et al. Overexpression of wild-type and mutant mucolipin proteins in mammalian cells: effects on the late endocytic compartment organization. FEBS Lett. 567, 219-224 (2004).
    • (2004) FEBS Lett. , vol.567 , pp. 219-224
    • Manzoni, M.1
  • 45
    • 33745193718 scopus 로고    scopus 로고
    • Lysosomal localization of TRPML3 depends on TRPML2 and the mucolipidosis-associated protein TRPML1
    • Venkatachalam, K., Hofmann, T. & Montell, C. Lysosomal localization of TRPML3 depends on TRPML2 and the mucolipidosis-associated protein TRPML1. J. Biol. Chem. 281, 17517-17527 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 17517-17527
    • Venkatachalam, K.1    Hofmann, T.2    Montell, C.3
  • 46
    • 33644655372 scopus 로고    scopus 로고
    • Two di-leucine motifs regulate trafficking of mucolipin-1 to lysosomes
    • Vergarajauregui, S. & Puertollano, R. Two di-leucine motifs regulate trafficking of mucolipin-1 to lysosomes. Traffic 7, 337-353 (2006).
    • (2006) Traffic , vol.7 , pp. 337-353
    • Vergarajauregui, S.1    Puertollano, R.2
  • 47
    • 0037072286 scopus 로고    scopus 로고
    • The neurogenetics of mucolipidosis type IV
    • Altarescu, G. et al. The neurogenetics of mucolipidosis type IV. Neurology 59, 306-313 (2002).
    • (2002) Neurology , vol.59 , pp. 306-313
    • Altarescu, G.1
  • 48
    • 76249097468 scopus 로고    scopus 로고
    • Mucolipidosis type IV: A subtle pediatric neurodegenerative disorder
    • Geer, J.S., Skinner, S.A., Goldin, E. & Holden, K.R. Mucolipidosis type IV: a subtle pediatric neurodegenerative disorder. Pediatr. Neurol. 42, 223-226 (2010).
    • (2010) Pediatr. Neurol. , vol.42 , pp. 223-226
    • Geer, J.S.1    Skinner, S.A.2    Goldin, E.3    Holden, K.R.4
  • 49
    • 84992597299 scopus 로고    scopus 로고
    • The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs
    • Shen, P.S. et al. The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs. Cell 167, 763-773.e711 (2016).
    • (2016) Cell , vol.167 , pp. 763e711-773e711
    • Shen, P.S.1
  • 50
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo, G. & De Camilli, P. Phosphoinositides in cell regulation and membrane dynamics. Nature 443, 651-657 (2006).
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 51
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 52
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB version 2.0
    • Weeks, C.M. & Miller, R. The design and implementation of SnB version 2.0. J. Appl. Crystallogr. 32, 120-124 (1999).
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 53
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution and density modification
    • Terwilliger, T.C. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 374, 22-37 (2003).
    • (2003) Methods Enzymol. , vol.374 , pp. 22-37
    • Terwilliger, T.C.1
  • 55
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 56
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A.J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 57
    • 33646011258 scopus 로고    scopus 로고
    • Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins
    • Kawate, T. & Gouaux, E. Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14, 673-681 (2006).
    • (2006) Structure , vol.14 , pp. 673-681
    • Kawate, T.1    Gouaux, E.2
  • 58
    • 84946482375 scopus 로고    scopus 로고
    • Asynchronous data acquisition and on-the-fly analysis of dose fractionated cryoEM images by UCSFImage
    • Li, X., Zheng, S., Agard, D.A. & Cheng, Y. Asynchronous data acquisition and on-the-fly analysis of dose fractionated cryoEM images by UCSFImage. J. Struct. Biol. 192, 174-178 (2015).
    • (2015) J. Struct. Biol. , vol.192 , pp. 174-178
    • Li, X.1    Zheng, S.2    Agard, D.A.3    Cheng, Y.4
  • 59
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584-590 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 60
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell, J.A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 61
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S.H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 62
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F.J. & Tagare, H.D. Quantifying the local resolution of cryo-EM density maps. Nat. Methods 11, 63-65 (2014).
    • (2014) Nat. Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 63
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera: A visualization system for exploratory research and analysis
    • Pettersen, E.F. et al. UCSF Chimera: a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.