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Volumn 119, Issue 5, 2015, Pages 1835-1846

Energy propagation and network energetic coupling in proteins

Author keywords

[No Author keywords available]

Indexed keywords

ENERGY EFFICIENCY; ENERGY TRANSFER;

EID: 84922422456     PISSN: 10895639     EISSN: 15205215     Source Type: Journal    
DOI: 10.1021/jp509906m     Document Type: Article
Times cited : (44)

References (60)
  • 1
    • 84883530539 scopus 로고    scopus 로고
    • Emerging Computational Approaches for the Study of Protein Allostery
    • Collier, G.; Ortiz, V. Emerging Computational Approaches for the Study of Protein Allostery Arch. Biochem. Biophys. 2013, 538, 6-15
    • (2013) Arch. Biochem. Biophys. , vol.538 , pp. 6-15
    • Collier, G.1    Ortiz, V.2
  • 2
    • 84896484176 scopus 로고    scopus 로고
    • Computational Approaches to Mapping Allosteric Pathways
    • Feher, V. a.; Durrant, J. D.; Van Wart, A. T.; Amaro, R. E. Computational Approaches to Mapping Allosteric Pathways Curr. Opin. Struct. Biol. 2014, 25, 98-103
    • (2014) Curr. Opin. Struct. Biol. , vol.25 , pp. 98-103
    • Durrant, J.D.1    Van Wart, A.T.2    Amaro, R.E.3
  • 3
    • 38049089909 scopus 로고    scopus 로고
    • A Computational Investigation of Allostery in the Catabolite Activator Protein
    • Li, L.; Uversky, V. N.; Dunker, a. K.; Meroueh, S. O. A Computational Investigation of Allostery in the Catabolite Activator Protein J. Am. Chem. Soc. 2007, 129, 15668-76
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15668-15676
    • Li, L.1    Uversky, V.N.2    Dunker, A.K.3    Meroueh, S.O.4
  • 4
    • 33749055796 scopus 로고    scopus 로고
    • Markov Propagation of Allosteric Effects in Biomolecular Systems: Application to GroEL-GroES
    • Chennubhotla, C.; Bahar, I. Markov Propagation of Allosteric Effects in Biomolecular Systems: Application to GroEL-GroES Mol. Sys. Biol. 2006, 2, 36
    • (2006) Mol. Sys. Biol. , vol.2 , pp. 36
    • Chennubhotla, C.1    Bahar, I.2
  • 5
    • 34848882812 scopus 로고    scopus 로고
    • Signal Propagation in Proteins and Relation to Equilibrium Fluctuations
    • Chennubhotla, C.; Bahar, I. Signal Propagation in Proteins and Relation to Equilibrium Fluctuations PLoS Comp. Biol. 2007, 3, 1716-1726
    • (2007) PLoS Comp. Biol. , vol.3 , pp. 1716-1726
    • Chennubhotla, C.1    Bahar, I.2
  • 6
    • 84863939894 scopus 로고    scopus 로고
    • Equilibrium Fluctuations of a Single Folded Protein Reveal a Multitude of Potential Cryptic Allosteric Sites
    • Bowman, G. R.; Geissler, P. L. Equilibrium Fluctuations of a Single Folded Protein Reveal a Multitude of Potential Cryptic Allosteric Sites Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 11681-11686
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 11681-11686
    • Bowman, G.R.1    Geissler, P.L.2
  • 9
    • 84883025863 scopus 로고    scopus 로고
    • Signaling Mechanisms of LOV Domains: New Insights from Molecular Dynamics Studies
    • Freddolino, P. L.; Gardner, K. H.; Schulten, K. Signaling Mechanisms of LOV Domains: New Insights From Molecular Dynamics Studies Photochem. Photobiol. Sci. 2013, 12, 1158-1170
    • (2013) Photochem. Photobiol. Sci. , vol.12 , pp. 1158-1170
    • Freddolino, P.L.1    Gardner, K.H.2    Schulten, K.3
  • 10
    • 84865063074 scopus 로고    scopus 로고
    • Exploring Residue Component Contributions to Dynamical Network Models of Allostery
    • Vanwart, A. T.; Eargle, J.; Luthey-Schulten, Z.; Amaro, R. E. Exploring Residue Component Contributions to Dynamical Network Models of Allostery J. Chem. Theory Comput. 2012, 8, 2949-2961
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 2949-2961
    • Vanwart, A.T.1    Eargle, J.2    Luthey-Schulten, Z.3    Amaro, R.E.4
  • 11
    • 35648944297 scopus 로고    scopus 로고
    • A Study of Communication Pathways in Methionyl- tRNA Synthetase by Molecular Dynamics Simulations and Structure Network Analysis
    • Ghosh, A.; Vishveshwara, S. A Study of Communication Pathways in Methionyl- tRNA Synthetase by Molecular Dynamics Simulations and Structure Network Analysis Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 15711-15716
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 15711-15716
    • Ghosh, A.1    Vishveshwara, S.2
  • 12
    • 41349118690 scopus 로고    scopus 로고
    • Small-World View of the Amino Acids That Play a Key Role in Protein Folding
    • Vendruscolo, M.; Dokholyan, N.; Paci, E.; Karplus, M. Small-World View of the Amino Acids That Play a Key Role in Protein Folding Phys. Rev. E 2002, 65, 061910
    • (2002) Phys. Rev. e , vol.65 , pp. 061910
    • Vendruscolo, M.1    Dokholyan, N.2    Paci, E.3    Karplus, M.4
  • 13
    • 0346057951 scopus 로고    scopus 로고
    • Small-World Communication of Residues and Significance for Protein Dynamics
    • Atilgan, A. R.; Akan, P.; Baysal, C. Small-World Communication of Residues and Significance for Protein Dynamics Biophys. J. 2004, 86, 85-91
    • (2004) Biophys. J. , vol.86 , pp. 85-91
    • Atilgan, A.R.1    Akan, P.2    Baysal, C.3
  • 14
    • 84864250598 scopus 로고    scopus 로고
    • Paths of Long-Range Communication in the E2 Enzymes of Family 3: A Molecular Dynamics Investigation
    • Papaleo, E.; Lindorff-Larsen, K.; De Gioia, L. Paths of Long-Range Communication in the E2 Enzymes of Family 3: A Molecular Dynamics Investigation Phys. Chem. Chem. Phys. 2012, 14, 12515-12525
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 12515-12525
    • Papaleo, E.1    Lindorff-Larsen, K.2    De Gioia, L.3
  • 15
    • 61649124866 scopus 로고    scopus 로고
    • Allostery Wiring Diagrams in the Transitions That Drive the GroEL Reaction Cycle
    • Tehver, R.; Chen, J.; Thirumalai, D. Allostery Wiring Diagrams in the Transitions That Drive the GroEL Reaction Cycle J. Mol. Biol. 2009, 387, 390-406
    • (2009) J. Mol. Biol. , vol.387 , pp. 390-406
    • Tehver, R.1    Chen, J.2    Thirumalai, D.3
  • 16
    • 84878477071 scopus 로고    scopus 로고
    • A Mechanistic Understanding of Allosteric Immune Escape Pathways in the HIV-1 Envelope Glycoprotein
    • Sethi, A.; Tian, J.; Derdeyn, C. A.; Korber, B.; Gnanakaran, S. A Mechanistic Understanding of Allosteric Immune Escape Pathways in the HIV-1 Envelope Glycoprotein PLoS Comp. Biol. 2013, 9, e1003046
    • (2013) PLoS Comp. Biol. , vol.9 , pp. 1003046
    • Sethi, A.1    Tian, J.2    Derdeyn, C.A.3    Korber, B.4    Gnanakaran, S.5
  • 18
    • 84898439664 scopus 로고    scopus 로고
    • Determination of Signaling Pathways in Proteins Through Network Theory: Importance of the Topology
    • Ribeiro, A. A. S. T.; Ortiz, V. Determination of Signaling Pathways in Proteins Through Network Theory: Importance of the Topology J. Chem. Theory Comput. 2014, 10, 1762-1769
    • (2014) J. Chem. Theory Comput. , vol.10 , pp. 1762-1769
    • Ribeiro, A.A.S.T.1    Ortiz, V.2
  • 19
    • 78649883885 scopus 로고    scopus 로고
    • Interaction Energy Based Protein Structure Networks
    • Vijayabaskar, M. S.; Vishveshwara, S. Interaction Energy Based Protein Structure Networks Biophys. J. 2010, 99, 3704-15
    • (2010) Biophys. J. , vol.99 , pp. 3704-3715
    • Vijayabaskar, M.S.1    Vishveshwara, S.2
  • 20
    • 43949129091 scopus 로고    scopus 로고
    • Energy Flow in Proteins
    • Leitner, D. M. Energy Flow in Proteins Annu. Rev. Phys. Chem. 2008, 59, 233-259
    • (2008) Annu. Rev. Phys. Chem. , vol.59 , pp. 233-259
    • Leitner, D.M.1
  • 21
    • 0030458933 scopus 로고    scopus 로고
    • Producing Positive, Negative, and No Cooperativity by Mutations at a Single Residue Located at the Subunit Interface in the Aspartate Receptor of Salmonella Typhimurium
    • Kolodziej, a. F.; Tan, T.; Koshland, D. E. Producing Positive, Negative, and No Cooperativity by Mutations at a Single Residue Located at the Subunit Interface in the Aspartate Receptor of Salmonella Typhimurium Biochemistry 1996, 35, 14782-14792
    • (1996) Biochemistry , vol.35 , pp. 14782-14792
    • Kolodziej, A.F.1    Tan, T.2    Koshland, D.E.3
  • 22
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families
    • Lockless, S. W.; Ranganathan, R. Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families Science 1999, 286, 295-299
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 23
    • 0001326710 scopus 로고    scopus 로고
    • Structure of the Amide i Band of Peptides Measured by Femtosecond Nonlinear-Infrared Spectroscopy
    • Hamm, P.; Lim, M.; Hochstrasser, R. M. Structure of the Amide I Band of Peptides Measured by Femtosecond Nonlinear-Infrared Spectroscopy J. Phys. Chem. B 1998, 5647, 6123-6138
    • (1998) J. Phys. Chem. B , vol.5647 , pp. 6123-6138
    • Hamm, P.1    Lim, M.2    Hochstrasser, R.M.3
  • 25
    • 0034283076 scopus 로고    scopus 로고
    • Energy Dissipation and Relaxation Processes in Deoxy Myoglobin after Photoexcitation in the Soret Region
    • Kholodenko, Y.; Volk, M.; Gooding, E.; Hochstrasser, R. Energy Dissipation and Relaxation Processes in Deoxy Myoglobin After Photoexcitation in the Soret Region Chem. Phys. 2000, 259, 71-87
    • (2000) Chem. Phys. , vol.259 , pp. 71-87
    • Kholodenko, Y.1    Volk, M.2    Gooding, E.3    Hochstrasser, R.4
  • 26
    • 33749574118 scopus 로고    scopus 로고
    • Role of Heme Propionates of Myoglobin in Vibrational Energy Relaxation
    • Koyama, M.; Neya, S.; Mizutani, Y. Role of Heme Propionates of Myoglobin in Vibrational Energy Relaxation Chem. Phys. Lett. 2006, 430, 404-408
    • (2006) Chem. Phys. Lett. , vol.430 , pp. 404-408
    • Koyama, M.1    Neya, S.2    Mizutani, Y.3
  • 28
    • 33644847828 scopus 로고    scopus 로고
    • Generalized Correlation for Biomolecular Dynamics
    • Lange, O. F.; Grubmüller, H. Generalized Correlation for Biomolecular Dynamics Proteins 2006, 62, 1053-1061
    • (2006) Proteins , vol.62 , pp. 1053-1061
    • Lange, O.F.1    Grubmüller, H.2
  • 29
    • 84945709831 scopus 로고
    • Algorithm 97: Shortest path
    • Floyd, R. W. Algorithm 97: Shortest path Commun. ACM 1962, 5, 345-345
    • (1962) Commun. ACM , vol.5 , pp. 345-345
    • Floyd, R.W.1
  • 30
    • 34247622363 scopus 로고    scopus 로고
    • The Importance of Bottlenecks in Protein Networks: Correlation with Gene Essentiality and Expression Dynamics
    • Yu, H.; Kim, P. M.; Sprecher, E.; Trifonov, V.; Gerstein, M. The Importance of Bottlenecks in Protein Networks: Correlation With Gene Essentiality and Expression Dynamics PLoS Comp. Biol. 2007, 3, e59
    • (2007) PLoS Comp. Biol. , vol.3 , pp. 59
    • Yu, H.1    Kim, P.M.2    Sprecher, E.3    Trifonov, V.4    Gerstein, M.5
  • 32
    • 0242663237 scopus 로고    scopus 로고
    • A Point-Charge Force Field for Molecular Mechanics Simulations of Proteins Based on Condensed-Phase Quantum Mechanical Calculations
    • Duan, Y.; Wu, C.; Chowdhury, S.; Lee, M. C.; Xiong, G.; Zhang, W. E. I.; Yang, R.; Cieplak, P.; Luo, R. A. Y.; Lee, T. A Point-Charge Force Field for Molecular Mechanics Simulations of Proteins Based on Condensed-Phase Quantum Mechanical Calculations J. Comput. Chem. 2003, 24, 1999-2012
    • (2003) J. Comput. Chem. , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5    Zhang, W.E.I.6    Yang, R.7    Cieplak, P.8    Luo, R.A.Y.9    Lee, T.10
  • 34
    • 33846086933 scopus 로고    scopus 로고
    • Canonical Sampling Through Velocity Rescaling
    • Bussi, G.; Donadio, D.; Parrinello, M. Canonical Sampling Through Velocity Rescaling J. Chem. Phys. 2007, 126, 014101
    • (2007) J. Chem. Phys. , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 35
    • 26144434487 scopus 로고
    • Crystal Structure and Pair Potentials: A Molecular-Dynamics Study
    • Parrinello, M.; Rahman, A. Crystal Structure and Pair Potentials: A Molecular-Dynamics Study Phys. Rev. Lett. 1980, 45, 1196-1199
    • (1980) Phys. Rev. Lett. , vol.45 , pp. 1196-1199
    • Parrinello, M.1    Rahman, A.2
  • 36
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A Parallel Linear Constraint Solver for Molecular Simulation
    • Hess, B. P-LINCS: a Parallel Linear Constraint Solver for Molecular Simulation J. Chem. Theor. Comp. 2008, 4, 116-122
    • (2008) J. Chem. Theor. Comp. , vol.4 , pp. 116-122
    • Hess, B.1
  • 37
    • 84986440341 scopus 로고
    • Settle: An Analytical Version of the SHAKE and RATTLE Algorithm for Rigid Water Models
    • Miyamoto, S.; Kollman, P. A. Settle: An Analytical Version of the SHAKE and RATTLE Algorithm for Rigid Water Models J. Comput. Chem. 1992, 13, 952-962
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 39
    • 4243551182 scopus 로고    scopus 로고
    • Vibrational Energy Transfer in Helices
    • Leitner, D. M. Vibrational Energy Transfer in Helices Phys. Rev. Lett. 2001, 87, 188102
    • (2001) Phys. Rev. Lett. , vol.87 , pp. 188102
    • Leitner, D.M.1
  • 40
    • 65949104571 scopus 로고    scopus 로고
    • Frequency-Resolved Communication Maps for Proteins and Other Nanoscale Materials
    • Leitner, D. M. Frequency-Resolved Communication Maps for Proteins and Other Nanoscale Materials J. Chem. Phys. 2009, 130, 195101
    • (2009) J. Chem. Phys. , vol.130 , pp. 195101
    • Leitner, D.M.1
  • 41
    • 22444450449 scopus 로고    scopus 로고
    • Intramolecular Signaling Pathways Revealed by Modeling Anisotropic Thermal Diffusion
    • Ota, N.; Agard, D. a. Intramolecular Signaling Pathways Revealed by Modeling Anisotropic Thermal Diffusion J. Mol. Biol. 2005, 351, 345-54
    • (2005) J. Mol. Biol. , vol.351 , pp. 345-354
    • Ota, N.1
  • 42
    • 80051928217 scopus 로고    scopus 로고
    • Mapping the Intramolecular Vibrational Energy Flow in Proteins Reveals Functionally Important Residues
    • Martínez, L.; Figueira, A. C. M.; Webb, P.; Polikarpov, I.; Skaf, M. S. Mapping the Intramolecular Vibrational Energy Flow in Proteins Reveals Functionally Important Residues J. Phys. Chem. Lett. 2011, 2, 2073-2078
    • (2011) J. Phys. Chem. Lett. , vol.2 , pp. 2073-2078
    • Martínez, L.1    Figueira, A.C.M.2    Webb, P.3    Polikarpov, I.4    Skaf, M.S.5
  • 43
    • 33749029273 scopus 로고    scopus 로고
    • Pump-Probe Molecular Dynamics as a Tool for Studying Protein Motion and Long Range Coupling
    • Sharp, K.; Skinner, J. J. Pump-Probe Molecular Dynamics as a Tool for Studying Protein Motion and Long Range Coupling Proteins: Struct., Funct. Bioinf. 2006, 361, 347-361
    • (2006) Proteins: Struct., Funct. Bioinf. , vol.361 , pp. 347-361
    • Sharp, K.1    Skinner, J.J.2
  • 44
    • 0036175240 scopus 로고    scopus 로고
    • Structural Evidence for Ammonia Tunneling Across the (Beta Alpha)(8) Barrel of the Imidazole Glycerol Phosphate Synthase Bienzyme Complex
    • Douangamath, A.; Walker, M.; Beismann-Driemeyer, S.; Vega-Fernandez, M. C.; Sterner, R.; Wilmanns, M. Structural Evidence for Ammonia Tunneling Across the (Beta Alpha)(8) Barrel of the Imidazole Glycerol Phosphate Synthase Bienzyme Complex Structure 2002, 10, 185-193
    • (2002) Structure , vol.10 , pp. 185-193
    • Douangamath, A.1    Walker, M.2    Beismann-Driemeyer, S.3    Vega-Fernandez, M.C.4    Sterner, R.5    Wilmanns, M.6
  • 45
    • 0034671172 scopus 로고    scopus 로고
    • Modeling the cAMP-induced Allosteric Transition Using the Crystal Structure of CAP-cAMP at 2.1 a Resolution
    • Passner, J. M.; Schultz, S. C.; Steitz, T. a. Modeling the cAMP-induced Allosteric Transition Using the Crystal Structure of CAP-cAMP at 2.1 a Resolution J. Mol. Biol. 2000, 304, 847-859
    • (2000) J. Mol. Biol. , vol.304 , pp. 847-859
    • Passner, J.M.1    Schultz, S.C.2
  • 47
    • 63749116038 scopus 로고    scopus 로고
    • Allostery in the LacI/GalR Family: Variations on a Theme
    • Swint-Kruse, L.; Matthews, K. S. Allostery in the LacI/GalR Family: Variations on a Theme Curr. Opin. Microbiol. 2009, 12, 129-137
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 129-137
    • Swint-Kruse, L.1    Matthews, K.S.2
  • 48
    • 0034089394 scopus 로고    scopus 로고
    • A Closer View of the Conformation of the Lac Repressor Bound to Operator
    • Bell, C. E.; Lewis, M. A Closer View of the Conformation of the Lac Repressor Bound to Operator Nat. Struct. Biol. 2000, 7, 209-214
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 209-214
    • Bell, C.E.1    Lewis, M.2
  • 49
    • 20444411150 scopus 로고    scopus 로고
    • The Lac Repressor
    • Lewis, M. The Lac Repressor Comp. R. Biol. 2005, 328, 521-548
    • (2005) Comp. R. Biol. , vol.328 , pp. 521-548
    • Lewis, M.1
  • 50
    • 0028076771 scopus 로고
    • Genetic Studies of the Lac Repressor XIV
    • Markiewicz, P.; Miller, J. Genetic Studies of the Lac Repressor XIV J. Mol. Biol. 1994, 240, 421-433
    • (1994) J. Mol. Biol. , vol.240 , pp. 421-433
    • Markiewicz, P.1    Miller, J.2
  • 51
    • 2342519701 scopus 로고    scopus 로고
    • Genetic Studies of the Lac Repressor. XV: 4000 Single Amino Acid Substitutions and Analysis of the Resulting Phenotypes on the Basis of the Protein Structure
    • Suckow, J.; Markiewicz, P.; Kleina, L. G.; Miller, J.; Kisters-Woike, B.; Müller-Hill, B. Genetic Studies of the Lac Repressor. XV: 4000 Single Amino Acid Substitutions and Analysis of the Resulting Phenotypes on the Basis of the Protein Structure J. Mol. Biol. 1996, 261, 509-523
    • (1996) J. Mol. Biol. , vol.261 , pp. 509-523
    • Suckow, J.1    Markiewicz, P.2    Kleina, L.G.3    Miller, J.4    Kisters-Woike, B.5    Müller-Hill, B.6
  • 53
    • 35348957264 scopus 로고    scopus 로고
    • Efficient Behavior of Small-World Networks
    • Latora, V.; Marchiori, M. Efficient Behavior of Small-World Networks Phys. Rev. Lett. 2001, 87, 198701
    • (2001) Phys. Rev. Lett. , vol.87 , pp. 198701
    • Latora, V.1    Marchiori, M.2
  • 54
    • 0025370815 scopus 로고
    • Dominant Forces in Protein Folding
    • Dill, K. A. Dominant Forces in Protein Folding Biochemistry 1990, 29, 7133-7155
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 56
    • 1842539352 scopus 로고    scopus 로고
    • A Linear Correlation between the Energetics of Allosteric Communication and Protein Flexibility in the Escherichia Coli Cyclic AMP Receptor Protein Revealed by Mutation-Induced Changes in Compressibility and Amide Hydrogen-Deuterium Exchange
    • Gekko, K.; Obu, N.; Li, J.; Lee, J. C. A Linear Correlation Between the Energetics of Allosteric Communication and Protein Flexibility in the Escherichia Coli Cyclic AMP Receptor Protein Revealed by Mutation-Induced Changes in Compressibility and Amide Hydrogen-Deuterium Exchange Biochemistry 2004, 43, 3844-52
    • (2004) Biochemistry , vol.43 , pp. 3844-3852
    • Gekko, K.1    Obu, N.2    Li, J.3    Lee, J.C.4
  • 58
    • 1942470563 scopus 로고    scopus 로고
    • Role of Residue 138 in the Interdomain Hinge Region in Transmitting Allosteric Signals for DNA Binding in Escherichia Coli cAMP Receptor Protein
    • Yu, S.; Lee, J. C. Role of Residue 138 in the Interdomain Hinge Region in Transmitting Allosteric Signals for DNA Binding in Escherichia Coli cAMP Receptor Protein Biochemistry 2004, 43, 4662-4669
    • (2004) Biochemistry , vol.43 , pp. 4662-4669
    • Yu, S.1    Lee, J.C.2
  • 59
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic Disorder as a Mechanism to Optimize Allosteric Coupling in Proteins
    • Hilser, V. J.; Thompson, E. B. Intrinsic Disorder as a Mechanism to Optimize Allosteric Coupling in Proteins Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 8311-8315
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 60
    • 84879392599 scopus 로고    scopus 로고
    • Signaling from Disordered Proteins
    • Hilser, V. J. Signaling From Disordered Proteins Nature 2012, 498, 308-310
    • (2012) Nature , vol.498 , pp. 308-310
    • Hilser, V.J.1


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