메뉴 건너뛰기




Volumn 427, Issue 4, 2015, Pages 737-752

Flexible stoichiometry and asymmetry of the PIDDosome core complex by heteronuclear NMR spectroscopy and mass spectrometry

Author keywords

death domain; ILV labeling; protein complex; spectral complexity; TROSY NMR

Indexed keywords

CASPASE 2; CRADD PROTEIN; DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEIN; P53 INDUCED DEATH DOMAIN PROTEIN; PROTEIN; UNCLASSIFIED DRUG; CRADD PROTEIN, HUMAN; MULTIPROTEIN COMPLEX; PIDD PROTEIN, HUMAN;

EID: 84922348019     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.11.021     Document Type: Article
Times cited : (15)

References (55)
  • 1
    • 84866279725 scopus 로고    scopus 로고
    • PIDD death-domain phosphorylation by ATM controls prodeath versus prosurvival PIDDosome signaling
    • K. Ando, J.L. Kernan, P.H. Liu, T. Sanda, E. Logette, and J. Tschopp PIDD death-domain phosphorylation by ATM controls prodeath versus prosurvival PIDDosome signaling Mol Cell 47 2012 681 693
    • (2012) Mol Cell , vol.47 , pp. 681-693
    • Ando, K.1    Kernan, J.L.2    Liu, P.H.3    Sanda, T.4    Logette, E.5    Tschopp, J.6
  • 2
    • 33846702221 scopus 로고    scopus 로고
    • Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
    • H.H. Park, E. Logette, S. Raunser, S. Cuenin, T. Walz, and J. Tschopp Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex Cell 128 2007 533 546
    • (2007) Cell , vol.128 , pp. 533-546
    • Park, H.H.1    Logette, E.2    Raunser, S.3    Cuenin, S.4    Walz, T.5    Tschopp, J.6
  • 3
    • 78649939211 scopus 로고    scopus 로고
    • In vitro reconstitution of the interactions in the PIDDosome
    • T.H. Jang, C. Zheng, H. Wu, J.H. Jeon, and H.H. Park In vitro reconstitution of the interactions in the PIDDosome Apoptosis 15 2010 1444 1452
    • (2010) Apoptosis , vol.15 , pp. 1444-1452
    • Jang, T.H.1    Zheng, C.2    Wu, H.3    Jeon, J.H.4    Park, H.H.5
  • 5
    • 54249096028 scopus 로고    scopus 로고
    • Caspases in apoptosis and beyond
    • J. Li, and J. Yuan Caspases in apoptosis and beyond Oncogene 27 2008 6194 6206
    • (2008) Oncogene , vol.27 , pp. 6194-6206
    • Li, J.1    Yuan, J.2
  • 7
    • 33846219997 scopus 로고    scopus 로고
    • Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway
    • A. Tinel, S. Janssens, S. Lippens, S. Cuenin, E. Logette, and B. Jaccard Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway EMBO J 26 2007 197 208
    • (2007) EMBO J , vol.26 , pp. 197-208
    • Tinel, A.1    Janssens, S.2    Lippens, S.3    Cuenin, S.4    Logette, E.5    Jaccard, B.6
  • 8
    • 62549095266 scopus 로고    scopus 로고
    • Autoinhibition of UNC5b revealed by the cytoplasmic domain structure of the receptor
    • R. Wang, Z. Wei, H. Jin, H. Wu, C. Yu, and W. Wen Autoinhibition of UNC5b revealed by the cytoplasmic domain structure of the receptor Mol Cell 33 2009 692 703
    • (2009) Mol Cell , vol.33 , pp. 692-703
    • Wang, R.1    Wei, Z.2    Jin, H.3    Wu, H.4    Yu, C.5    Wen, W.6
  • 9
    • 2442453730 scopus 로고    scopus 로고
    • The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress
    • A. Tinel, and J. Tschopp The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress Science 304 2004 843 846
    • (2004) Science , vol.304 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2
  • 10
    • 33748774114 scopus 로고    scopus 로고
    • Upon intracellular processing, the C-terminal death domain-containing fragment of the p53-inducible PIDD/LRDD protein translocates to the nucleoli and interacts with nucleolin
    • R. Pick, S. Badura, S. Bosser, and M. Zornig Upon intracellular processing, the C-terminal death domain-containing fragment of the p53-inducible PIDD/LRDD protein translocates to the nucleoli and interacts with nucleolin Biochem Biophys Res Commun 349 2006 1329 1338
    • (2006) Biochem Biophys Res Commun , vol.349 , pp. 1329-1338
    • Pick, R.1    Badura, S.2    Bosser, S.3    Zornig, M.4
  • 11
    • 8844224859 scopus 로고    scopus 로고
    • The biochemical mechanism of caspase-2 activation
    • B.C. Baliga, S.H. Read, and S. Kumar The biochemical mechanism of caspase-2 activation Cell Death Differ 11 2004 1234 1241
    • (2004) Cell Death Differ , vol.11 , pp. 1234-1241
    • Baliga, B.C.1    Read, S.H.2    Kumar, S.3
  • 14
    • 9644307904 scopus 로고    scopus 로고
    • Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids
    • M. Enoksson, J.D. Robertson, V. Gogvadze, P. Bu, A. Kropotov, and B. Zhivotovsky Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids J Biol Chem 279 2004 49575 49578
    • (2004) J Biol Chem , vol.279 , pp. 49575-49578
    • Enoksson, M.1    Robertson, J.D.2    Gogvadze, V.3    Bu, P.4    Kropotov, A.5    Zhivotovsky, B.6
  • 15
    • 28944447430 scopus 로고    scopus 로고
    • PIDD mediates NF-kappaB activation in response to DNA damage
    • S. Janssens, A. Tinel, S. Lippens, and J. Tschopp PIDD mediates NF-kappaB activation in response to DNA damage Cell 123 2005 1079 1092
    • (2005) Cell , vol.123 , pp. 1079-1092
    • Janssens, S.1    Tinel, A.2    Lippens, S.3    Tschopp, J.4
  • 16
    • 28944449953 scopus 로고    scopus 로고
    • PIDD: A switch hitter
    • Z.H. Wu, A. Mabb, and S. Miyamoto PIDD: a switch hitter Cell 123 2005 980 982
    • (2005) Cell , vol.123 , pp. 980-982
    • Wu, Z.H.1    Mabb, A.2    Miyamoto, S.3
  • 17
    • 67649668611 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray crystallographic studies of RAIDD death-domain (DD)
    • T.H. Jang, and H.H. Park Purification, crystallization and preliminary X-ray crystallographic studies of RAIDD death-domain (DD) Int J Mol Sci 10 2009 2501 2509
    • (2009) Int J Mol Sci , vol.10 , pp. 2501-2509
    • Jang, T.H.1    Park, H.H.2
  • 18
    • 0033542482 scopus 로고    scopus 로고
    • Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1
    • H. Qin, S.M. Srinivasula, G. Wu, T. Fernandes-Alnemri, E.S. Alnemri, and Y. Shi Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1 Nature 399 1999 549 557
    • (1999) Nature , vol.399 , pp. 549-557
    • Qin, H.1    Srinivasula, S.M.2    Wu, G.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5    Shi, Y.6
  • 19
    • 0035896406 scopus 로고    scopus 로고
    • A docking model of key components of the DISC complex: Death domain superfamily interactions redefined
    • C.H. Weber, and C. Vincenz A docking model of key components of the DISC complex: death domain superfamily interactions redefined FEBS Lett 492 2001 171 176
    • (2001) FEBS Lett , vol.492 , pp. 171-176
    • Weber, C.H.1    Vincenz, C.2
  • 20
    • 0033601077 scopus 로고    scopus 로고
    • Three-dimensional structure of a complex between the death domains of Pelle and Tube
    • T. Xiao, P. Towb, S.A. Wasserman, and S.R. Sprang Three-dimensional structure of a complex between the death domains of Pelle and Tube Cell 99 1999 545 555
    • (1999) Cell , vol.99 , pp. 545-555
    • Xiao, T.1    Towb, P.2    Wasserman, S.A.3    Sprang, S.R.4
  • 21
    • 34547399613 scopus 로고    scopus 로고
    • A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase
    • A. Velyvis, Y.R. Yang, H.K. Schachman, and L.E. Kay A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase Proc Natl Acad Sci U S A 104 2007 8815 8820
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 8815-8820
    • Velyvis, A.1    Yang, Y.R.2    Schachman, H.K.3    Kay, L.E.4
  • 22
    • 34548304719 scopus 로고    scopus 로고
    • Solution NMR of supramolecular complexes: Providing new insights into function
    • R. Sprangers, A. Velyvis, and L.E. Kay Solution NMR of supramolecular complexes: providing new insights into function Nat Methods 4 2007 697 703
    • (2007) Nat Methods , vol.4 , pp. 697-703
    • Sprangers, R.1    Velyvis, A.2    Kay, L.E.3
  • 23
    • 33847690197 scopus 로고    scopus 로고
    • The dynamic proteosome
    • I. Kaganman The dynamic proteosome Nat Methods 4 2007 202 203
    • (2007) Nat Methods , vol.4 , pp. 202-203
    • Kaganman, I.1
  • 24
    • 79955910554 scopus 로고    scopus 로고
    • Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view
    • L.E. Kay Solution NMR spectroscopy of supra-molecular systems, why bother? A methyl-TROSY view J Magn Reson 210 2011 159 170
    • (2011) J Magn Reson , vol.210 , pp. 159-170
    • Kay, L.E.1
  • 25
    • 77649179384 scopus 로고    scopus 로고
    • Methyl groups as probes of supra-molecular structure, dynamics and function
    • A.M. Ruschak, and L.E. Kay Methyl groups as probes of supra-molecular structure, dynamics and function J Biomol NMR 46 2010 75 87
    • (2010) J Biomol NMR , vol.46 , pp. 75-87
    • Ruschak, A.M.1    Kay, L.E.2
  • 26
    • 36049046667 scopus 로고    scopus 로고
    • Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR
    • I. Gelis, A.M.J.J. Bonvin, D. Keramisanou, M. Koukaki, G. Gouridis, and S. Karamanou Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR Cell 131 2007 756 769
    • (2007) Cell , vol.131 , pp. 756-769
    • Gelis, I.1    Bonvin, A.M.J.J.2    Keramisanou, D.3    Koukaki, M.4    Gouridis, G.5    Karamanou, S.6
  • 27
    • 79960698348 scopus 로고    scopus 로고
    • Dynamic interaction of Hsp90 with its client protein p53
    • S.J. Park, M. Kostic, and H.J. Dyson Dynamic interaction of Hsp90 with its client protein p53 J Mol Biol 411 2011 158 173
    • (2011) J Mol Biol , vol.411 , pp. 158-173
    • Park, S.J.1    Kostic, M.2    Dyson, H.J.3
  • 28
    • 84890111683 scopus 로고    scopus 로고
    • Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins
    • G. Mas, E. Crublet, O. Hamelin, P. Gans, and J. Boisbouvier Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins J Biomol NMR 57 2013 251 262
    • (2013) J Biomol NMR , vol.57 , pp. 251-262
    • Mas, G.1    Crublet, E.2    Hamelin, O.3    Gans, P.4    Boisbouvier, J.5
  • 29
    • 78650588910 scopus 로고    scopus 로고
    • Alanine methyl groups as NMR probes of molecular structure and dynamics in high-molecular-weight proteins
    • R. Godoy-Ruiz, C. Guo, and V. Tugarinov Alanine methyl groups as NMR probes of molecular structure and dynamics in high-molecular-weight proteins J Am Chem Soc 132 2010 18340 18350
    • (2010) J Am Chem Soc , vol.132 , pp. 18340-18350
    • Godoy-Ruiz, R.1    Guo, C.2    Tugarinov, V.3
  • 30
    • 78149412689 scopus 로고    scopus 로고
    • A simple strategy for (13)C, (1)H labeling at the Ile-gamma2 methyl position in highly deuterated proteins
    • A.M. Ruschak, A. Velyvis, and L.E. Kay A simple strategy for (13)C, (1)H labeling at the Ile-gamma2 methyl position in highly deuterated proteins J Biomol NMR 48 2010 129 135
    • (2010) J Biomol NMR , vol.48 , pp. 129-135
    • Ruschak, A.M.1    Velyvis, A.2    Kay, L.E.3
  • 31
    • 70450160965 scopus 로고    scopus 로고
    • Assignment of Ile, Leu, and Val methyl correlations in supra-molecular systems: An application to aspartate transcarbamoylase
    • A. Velyvis, H.K. Schachman, and L.E. Kay Assignment of Ile, Leu, and Val methyl correlations in supra-molecular systems: an application to aspartate transcarbamoylase J Am Chem Soc 131 2009 16534 16543
    • (2009) J Am Chem Soc , vol.131 , pp. 16534-16543
    • Velyvis, A.1    Schachman, H.K.2    Kay, L.E.3
  • 32
    • 84866272306 scopus 로고    scopus 로고
    • 3-threonine for solution NMR studies of large protein complexes: Application to the 670 kDa proteasome
    • 3-threonine for solution NMR studies of large protein complexes: application to the 670 kDa proteasome PLoS One 7 2012 e43725
    • (2012) PLoS One , vol.7 , pp. e43725
    • Velyvis, A.1    Ruschak, A.M.2    Kay, L.E.3
  • 33
    • 77957794023 scopus 로고    scopus 로고
    • Solution NMR investigation of the CD95/FADD homotypic death domain complex suggests lack of engagement of the CD95 C terminus
    • D. Esposito, A. Sankar, N. Morgner, C.V. Robinson, K. Rittinger, and P.C. Driscoll Solution NMR investigation of the CD95/FADD homotypic death domain complex suggests lack of engagement of the CD95 C terminus Structure 18 2010 1378 1390
    • (2010) Structure , vol.18 , pp. 1378-1390
    • Esposito, D.1    Sankar, A.2    Morgner, N.3    Robinson, C.V.4    Rittinger, K.5    Driscoll, P.C.6
  • 35
    • 28044440088 scopus 로고    scopus 로고
    • Quantitative NMR spectroscopy of supramolecular complexes: Dynamic side pores in ClpP are important for product release
    • R. Sprangers, A. Gribun, P.M. Hwang, W.A. Houry, and L.E. Kay Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release Proc Natl Acad Sci U S A 102 2005 16678 16683
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 16678-16683
    • Sprangers, R.1    Gribun, A.2    Hwang, P.M.3    Houry, W.A.4    Kay, L.E.5
  • 36
    • 84893140063 scopus 로고    scopus 로고
    • TROSY NMR spectroscopy of large soluble proteins
    • Y. Xu, and S. Matthews TROSY NMR spectroscopy of large soluble proteins Top Curr Chem. 335 2013 97 119
    • (2013) Top Curr Chem. , vol.335 , pp. 97-119
    • Xu, Y.1    Matthews, S.2
  • 37
    • 78549236456 scopus 로고    scopus 로고
    • The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations
    • L. Wang, J.K. Yang, V. Kabaleeswaran, A.J. Rice, A.C. Cruz, and A.Y. Park The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations Nat Struct Mol Biol 17 2010 1324 1329
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1324-1329
    • Wang, L.1    Yang, J.K.2    Kabaleeswaran, V.3    Rice, A.J.4    Cruz, A.C.5    Park, A.Y.6
  • 38
    • 34548215681 scopus 로고    scopus 로고
    • Protein complexes in the gas phase: Technology for structural genomics and proteomics
    • J.L. Benesch, B.T. Ruotolo, D.A. Simmons, and C.V. Robinson Protein complexes in the gas phase: technology for structural genomics and proteomics Chem Rev 107 2007 3544 3567
    • (2007) Chem Rev , vol.107 , pp. 3544-3567
    • Benesch, J.L.1    Ruotolo, B.T.2    Simmons, D.A.3    Robinson, C.V.4
  • 39
    • 0041930989 scopus 로고    scopus 로고
    • 13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes
    • 13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes J Am Chem Soc 125 2003 10420 10428
    • (2003) J Am Chem Soc , vol.125 , pp. 10420-10428
    • Tugarinov, V.1    Hwang, P.M.2    Ollerenshaw, J.E.3    Kay, L.E.4
  • 40
    • 0242267427 scopus 로고    scopus 로고
    • Methyl TROSY: Explanation and experimental verification
    • J.E. Ollerenshaw, V. Tugarinov, and L.E. Kay Methyl TROSY: explanation and experimental verification Magn Reson Chem 41 2003 843 852
    • (2003) Magn Reson Chem , vol.41 , pp. 843-852
    • Ollerenshaw, J.E.1    Tugarinov, V.2    Kay, L.E.3
  • 41
    • 79961085477 scopus 로고    scopus 로고
    • Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR
    • H. Kato, H. van Ingen, B.R. Zhou, H. Feng, M. Bustin, and L.E. Kay Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR Proc Natl Acad Sci U S A 108 2011 12283 12288
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12283-12288
    • Kato, H.1    Van Ingen, H.2    Zhou, B.R.3    Feng, H.4    Bustin, M.5    Kay, L.E.6
  • 42
    • 0027155345 scopus 로고
    • Disulfide bond isomerization in BPTI and BPTI(G36s) - An NMR study of correlated mobility in proteins
    • G. Otting, E. Liepinsh, and K. Wüthrich Disulfide bond isomerization in BPTI and BPTI(G36s) - an NMR study of correlated mobility in proteins Biochemistry 32 1993 3571 3582
    • (1993) Biochemistry , vol.32 , pp. 3571-3582
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 43
    • 84985715908 scopus 로고
    • NMR studies of the rates of proline cis-trans isomerization in oligopeptides
    • C. Grathwohl, and K. Wüthrich NMR studies of the rates of proline cis-trans isomerization in oligopeptides Biopolymers 20 1981 2623 2633
    • (1981) Biopolymers , vol.20 , pp. 2623-2633
    • Grathwohl, C.1    Wüthrich, K.2
  • 44
    • 0029068108 scopus 로고
    • Nuclear magnetic resonance characterization of the Jun leucine zipper domain: Unusual properties of coiled-coil interfacial polar residues
    • F.K. Junius, J.P. Mackay, W.A. Bubb, S.A. Jensen, A.S. Weiss, and G.F. King Nuclear magnetic resonance characterization of the Jun leucine zipper domain: unusual properties of coiled-coil interfacial polar residues Biochemistry 34 1995 6164 6174
    • (1995) Biochemistry , vol.34 , pp. 6164-6174
    • Junius, F.K.1    Mackay, J.P.2    Bubb, W.A.3    Jensen, S.A.4    Weiss, A.S.5    King, G.F.6
  • 46
    • 0037090685 scopus 로고    scopus 로고
    • Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT
    • Y. Yang, N. Declerck, X. Manival, S. Aymerich, and M. Kochoyan Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT EMBO J 21 2002 1987 1997
    • (2002) EMBO J , vol.21 , pp. 1987-1997
    • Yang, Y.1    Declerck, N.2    Manival, X.3    Aymerich, S.4    Kochoyan, M.5
  • 47
    • 34250191823 scopus 로고    scopus 로고
    • An asymmetric structure of the Bacillus subtilis replication terminator protein in complex with DNA
    • J.P. Vivian, C.J. Porter, J.A. Wilce, and M.C. Wilce An asymmetric structure of the Bacillus subtilis replication terminator protein in complex with DNA J Mol Biol 370 2007 481 491
    • (2007) J Mol Biol , vol.370 , pp. 481-491
    • Vivian, J.P.1    Porter, C.J.2    Wilce, J.A.3    Wilce, M.C.4
  • 49
    • 84896837095 scopus 로고    scopus 로고
    • Hsp90-tau complex reveals molecular basis for specificity in chaperone action
    • G.E. Karagoz, A.M. Duarte, E. Akoury, H. Ippel, J. Biernat, and T. Moran Luengo Hsp90-tau complex reveals molecular basis for specificity in chaperone action Cell 156 2014 963 974
    • (2014) Cell , vol.156 , pp. 963-974
    • Karagoz, G.E.1    Duarte, A.M.2    Akoury, E.3    Ippel, H.4    Biernat, J.5    Moran Luengo, T.6
  • 50
    • 0035961347 scopus 로고    scopus 로고
    • Nuclear magnetic resonance characterization of peptide models of collagen-folding diseases
    • A. Buevich, and J. Baum Nuclear magnetic resonance characterization of peptide models of collagen-folding diseases Philos Trans R Soc Lond B Biol Sci 356 2001 159 168
    • (2001) Philos Trans R Soc Lond B Biol Sci , vol.356 , pp. 159-168
    • Buevich, A.1    Baum, J.2
  • 51
    • 84861319116 scopus 로고    scopus 로고
    • Crystal structure of (Gly-Pro-Hyp)(9): Implications for the collagen molecular model
    • K. Okuyama, K. Miyama, K. Mizuno, and H.P. Bachinger Crystal structure of (Gly-Pro-Hyp)(9): implications for the collagen molecular model Biopolymers 97 2012 607 616
    • (2012) Biopolymers , vol.97 , pp. 607-616
    • Okuyama, K.1    Miyama, K.2    Mizuno, K.3    Bachinger, H.P.4
  • 52
    • 77950497745 scopus 로고    scopus 로고
    • Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR
    • T.L. Religa, R. Sprangers, and L.E. Kay Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR Science 328 2010 98 102
    • (2010) Science , vol.328 , pp. 98-102
    • Religa, T.L.1    Sprangers, R.2    Kay, L.E.3
  • 53
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling
    • S.C. Lin, Y.C. Lo, and H. Wu Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling Nature 465 2010 885 890
    • (2010) Nature , vol.465 , pp. 885-890
    • Lin, S.C.1    Lo, Y.C.2    Wu, H.3
  • 54
    • 60549106191 scopus 로고    scopus 로고
    • The Fas-FADD death domain complex structure unravels signalling by receptor clustering
    • F.L. Scott, B. Stec, C. Pop, M.K. Dobaczewska, J.J. Lee, and E. Monosov The Fas-FADD death domain complex structure unravels signalling by receptor clustering Nature 457 2009 1019 1022
    • (2009) Nature , vol.457 , pp. 1019-1022
    • Scott, F.L.1    Stec, B.2    Pop, C.3    Dobaczewska, M.K.4    Lee, J.J.5    Monosov, E.6
  • 55
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • F. Sobott, H. Hernandez, M.G. McCammon, M.A. Tito, and C.V. Robinson A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies Anal Chem 74 2002 1402 1407
    • (2002) Anal Chem , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.