Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase
暂无分享,去创建一个
Bharat V. Adkar | E. Shakhnovich | O. Dym | Dorit Levy | G. Haran | I. Riven | Marija Iljina | Sanchari Bhattacharyya | David Scheerer
[1] Wenfei Li,et al. Role of Repeated Conformational Transitions in Substrate Binding of Adenylate Kinase , 2022, The journal of physical chemistry. B.
[2] Juan P. Bustamante,et al. Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR , 2021, Nature Communications.
[3] M. Wilmanns,et al. Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex , 2021, Nature Communications.
[4] Jun Wang,et al. Overcoming the Bottleneck of the Enzymatic Cycle by Steric Frustration. , 2019, Physical review letters.
[5] N. Elad,et al. Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine , 2019, Nature Communications.
[6] Amy I Gilson,et al. Substrate inhibition imposes fitness penalty at high protein stability , 2018, Proceedings of the National Academy of Sciences.
[7] D. Thirumalai,et al. Symmetry, Rigidity, and Allosteric Signaling: From Monomeric Proteins to Molecular Machines. , 2018, Chemical reviews.
[8] Gilad Haran,et al. Direct observation of ultrafast large-scale dynamics of an enzyme under turnover conditions , 2018, Proceedings of the National Academy of Sciences.
[9] Q. Cui,et al. Multiple Pathways and Time Scales for Conformational Transitions in apo-Adenylate Kinase. , 2018, Journal of chemical theory and computation.
[10] Nam Ki Lee,et al. Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study , 2017, Nature Methods.
[11] U. Sauer,et al. Structural basis for ligand binding to an enzyme by a conformational selection pathway , 2017, Proceedings of the National Academy of Sciences.
[12] Toma E Tomov,et al. Photon-by-Photon Hidden Markov Model Analysis for Microsecond Single-Molecule FRET Kinetics. , 2016, The journal of physical chemistry. B.
[13] Benjamin T. Porebski,et al. Consensus protein design , 2016, Protein engineering, design & selection : PEDS.
[14] Arieh Warshel,et al. Perspective: Defining and quantifying the role of dynamics in enzyme catalysis. , 2016, The Journal of chemical physics.
[15] Itay Mayrose,et al. ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules , 2016, Nucleic Acids Res..
[16] U. Sauer,et al. Structural basis for catalytically restrictive dynamics of a high-energy enzyme state , 2015, Nature Communications.
[17] B. Brooks,et al. The Atomistic Mechanism of Conformational Transition of Adenylate Kinase Investigated by Lorentzian Structure-Based Potential. , 2015, Journal of Chemical Theory and Computation.
[18] Michele Parrinello,et al. Energetics and Structural Characterization of the large-scale Functional Motion of Adenylate Kinase , 2015, Scientific Reports.
[19] R. Dyer,et al. The Dynamical Nature of Enzymatic Catalysis , 2014, Accounts of chemical research.
[20] Timothy D Craggs,et al. Alternating-laser excitation: single-molecule FRET and beyond. , 2014, Chemical Society reviews.
[21] P. Zwart,et al. Towards automated crystallographic structure refinement with phenix.refine , 2012, Acta crystallographica. Section D, Biological crystallography.
[22] Wei Li,et al. A Dynamic Knockout Reveals That Conformational Fluctuations Influence the Chemical Step of Enzyme Catalysis , 2011, Science.
[23] Tal Pupko,et al. ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids , 2010, Nucleic Acids Res..
[24] M. Devore,et al. Detecting intramolecular dynamics and multiple Förster resonance energy transfer states by fluorescence correlation spectroscopy. , 2010, The journal of physical chemistry. B.
[25] V. Hilser,et al. Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins , 2009, Proceedings of the National Academy of Sciences.
[26] A. Szabó,et al. Decoding the pattern of photon colors in single-molecule FRET. , 2009, The journal of physical chemistry. B.
[27] A. Terzic,et al. Adenylate Kinase and AMP Signaling Networks: Metabolic Monitoring, Signal Communication and Body Energy Sensing , 2009, International journal of molecular sciences.
[28] D. Kern,et al. Dynamic personalities of proteins , 2007, Nature.
[29] Mark A. Wilson,et al. Intrinsic motions along an enzymatic reaction trajectory , 2007, Nature.
[30] J. Chu,et al. Illuminating the mechanistic roles of enzyme conformational dynamics , 2007, Proceedings of the National Academy of Sciences.
[31] Marcia Levitus,et al. Measuring conformational dynamics: a new FCS-FRET approach. , 2007, The journal of physical chemistry. B.
[32] Osamu Miyashita,et al. Conformational transitions of adenylate kinase: switching by cracking. , 2007, Journal of molecular biology.
[33] Airlie J. McCoy,et al. Solving structures of protein complexes by molecular replacement with Phaser , 2006, Acta crystallographica. Section D, Biological crystallography.
[34] G. Phillips,et al. Crystal structure of ADP/AMP complex of Escherichia coli adenylate kinase , 2005, Proteins.
[35] P. Evans,et al. Scaling and assessment of data quality. , 2006, Acta crystallographica. Section D, Biological crystallography.
[36] L. Kay,et al. Intrinsic dynamics of an enzyme underlies catalysis , 2005, Nature.
[37] Martin Karplus,et al. Large amplitude conformational change in proteins explored with a plastic network model: adenylate kinase. , 2005, Journal of molecular biology.
[38] T. Noma. Dynamics of nucleotide metabolism as a supporter of life phenomena. , 2005, The journal of medical investigation : JMI.
[39] Nam Ki Lee,et al. Accurate FRET measurements within single diffusing biomolecules using alternating-laser excitation. , 2005, Biophysical journal.
[40] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[41] Georgia Hadjipavlou,et al. Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair , 2004, Nature Structural &Molecular Biology.
[42] Xian-Ming Pan,et al. An Iso-random Bi Bi Mechanism for Adenylate Kinase* , 1999, The Journal of Biological Chemistry.
[43] A Libchaber,et al. Kinetics of conformational fluctuations in DNA hairpin-loops. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[44] G. Murshudov,et al. Refinement of macromolecular structures by the maximum-likelihood method. , 1997, Acta crystallographica. Section D, Biological crystallography.
[45] E. Haas,et al. Towards a mechanism of AMP‐substrate inhibition in adenylate kinase from Escherichia coli , 1996, FEBS letters.
[46] E. Haas,et al. Domain closure in adenylate kinase. , 1996, Biochemistry.
[47] G. Schulz,et al. Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases. , 1995, Structure.
[48] G. Phillips,et al. The closed conformation of a highly flexible protein: The structure of E. coli adenylate kinase with bound AMP and AMPPNP , 1994, Proteins.
[49] G. Schulz,et al. Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state. , 1992, Journal of molecular biology.
[50] G. Schulz,et al. Induced-fit movements in adenylate kinases. , 1990, Faraday discussions.
[51] G. Phillips,et al. Assignment of the nucleotide binding sites and the mechanism of substrate inhibition of Escherichia coli adenylate kinase , 1991, Proteins.
[52] I R Vetter,et al. Fluorescence and NMR investigations on the ligand binding properties of adenylate kinases. , 1990, Biochemistry.
[53] R. Huss. Regulation of Adenylate Kinase , 1985 .
[54] S. French,et al. On the treatment of negative intensity observations , 1978 .
[55] I. H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems , 1975 .
[56] W Ferdinand,et al. The interpretation of non-hyperbolic rate curves for two-substrate enzymes. A possible mechanism for phosphofructokinase. , 1966, The Biochemical journal.