| Year |
Citation |
Score |
| 2023 |
Christensen S, Stenström O, Akke M, Bülow L. Conformational Dynamics of Phytoglobin BvPgb1.2 from ssp. . International Journal of Molecular Sciences. 24. PMID 36835381 DOI: 10.3390/ijms24043973 |
0.342 |
|
| 2022 |
Dreydoppel M, Akke M, Weininger U. Characterizing Fast Conformational Exchange of Aromatic Rings Using Residual Dipolar Couplings: Distinguishing Jumplike Flips from Other Exchange Mechanisms. The Journal of Physical Chemistry. B. PMID 36180044 DOI: 10.1021/acs.jpcb.2c05097 |
0.341 |
|
| 2021 |
Dreydoppel M, Lichtenecker RJ, Akke M, Weininger U. H R relaxation dispersion experiments in aromatic side chains. Journal of Biomolecular Nmr. PMID 34510298 DOI: 10.1007/s10858-021-00382-w |
0.329 |
|
| 2020 |
Köhler C, Carlström G, Gunnarsson A, Weininger U, Tångefjord S, Ullah V, Lepistö M, Karlsson U, Papavoine T, Edman K, Akke M. Dynamic allosteric communication pathway directing differential activation of the glucocorticoid receptor. Science Advances. 6. PMID 32832645 DOI: 10.1126/Sciadv.Abb5277 |
0.317 |
|
| 2020 |
Kraus J, Gupta R, Lu M, Gronenborn A, Akke M, Polenova T. Accurate Backbone 13C and 15N Chemical Shift Tensors in Galectin-3 by MAS NMR and QM/MM: Details of Structure and Environment Matter. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 32363727 DOI: 10.1002/Cphc.202000249 |
0.44 |
|
| 2019 |
Weininger U, Modig K, Ishida H, Vogel HJ, Akke M. Rotamer Jumps, Proton Exchange, and Amine Inversion Dynamics of Dimethylated Lysine Residues in Proteins Resolved by pH-Dependent H and C NMR Relaxation Dispersion. The Journal of Physical Chemistry. B. PMID 31580078 DOI: 10.1021/Acs.Jpcb.9B06408 |
0.458 |
|
| 2019 |
Carlström G, Elvander F, Swärd J, Jakobsson A, Akke M. Rapid NMR Relaxation Measurements Using Optimal Nonuniform Sampling of Multidimensional Accordion Data Analyzed by a Sparse Reconstruction Method. Journal of Physical Chemistry A. 123: 5718-5723. PMID 31194551 DOI: 10.1021/Acs.Jpca.9B04152 |
0.315 |
|
| 2019 |
Bille A, Jensen KS, Mohanty S, Akke M, Irbäck A. Stability and Local Unfolding of SOD1 in the Presence of Protein Crowders. The Journal of Physical Chemistry. B. PMID 30753785 DOI: 10.1021/Acs.Jpcb.8B10774 |
0.411 |
|
| 2019 |
Wernersson S, Bågenholm V, Persson C, Upadhyay SK, Stålbrand H, Akke M. Backbone H, C, and N resonance assignments of BoMan26A, a β-mannanase of the glycoside hydrolase family 26 from the human gut bacterium Bacteroides ovatus. Biomolecular Nmr Assignments. PMID 30734154 DOI: 10.1007/S12104-019-09879-W |
0.389 |
|
| 2019 |
Verteramo ML, Stenström O, Misini Ignjatovic M, Caldararu O, Olsson MA, Manzoni F, Leffler H, Oksanen E, Logan DT, Nilsson UJ, Ryde U, Akke M. Interplay between Conformational Entropy and Solvation Entropy in Protein-Ligand Binding. Journal of the American Chemical Society. PMID 30618244 DOI: 10.1021/Jacs.8B11099 |
0.388 |
|
| 2019 |
Wallerstein J, Akke M. Minute Additions of DMSO Affect Protein Dynamics Measurements by NMR Relaxation Experiments through Significant Changes in Solvent Viscosity. Chemphyschem. 20: 326-332. PMID 30102005 DOI: 10.1002/Cphc.201800626 |
0.411 |
|
| 2018 |
Manzoni F, Wallerstein J, Schrader TE, Ostermann A, Coates L, Akke M, Blakeley MP, Oksanen E, Logan DT. Elucidation of Hydrogen Bonding Patterns in Ligand-Free, Lactose- and Glycerol-Bound Galectin-3C by Neutron Crystallography to Guide Drug Design. Journal of Medicinal Chemistry. PMID 29672051 DOI: 10.1021/Acs.Jmedchem.8B00081 |
0.347 |
|
| 2018 |
Köhler C, Carlström G, Tångefjord S, Papavoine T, Lepistö M, Edman K, Akke M. Backbone H, C, and N resonance assignments of the ligand binding domain of the human wildtype glucocorticoid receptor and the F602S mutant variant. Biomolecular Nmr Assignments. PMID 29667121 DOI: 10.1007/S12104-018-9820-9 |
0.371 |
|
| 2018 |
Kraus J, Gupta R, Lu M, Yehl JB, Case DA, Gronenborn AM, Akke M, Polenova T. Chemical Shifts of the Carbohydrate Binding Domain of Galectin-3 from Magic Angle Spinning NMR and Hybrid Quantum Mechanics/Molecular Mechanics Calculations. The Journal of Physical Chemistry. B. PMID 29498857 DOI: 10.1021/Acs.Jpcb.8B00853 |
0.389 |
|
| 2018 |
Solomentsev G, Diehl C, Akke M. Conformational Entropy of FK506 Binding to FKBP12 Determined by Nuclear Magnetic Resonance Relaxation and Molecular Dynamics Simulations. Biochemistry. 57: 1451-1461. PMID 29412644 DOI: 10.1021/Acs.Biochem.7B01256 |
0.41 |
|
| 2018 |
Kohler C, Weininger U, Backstrom S, Carlstrom G, Lepisto M, Papavoine T, Edman K, Akke M. 1H, 13C, 15N backbone and 1H, 13C methionine methyl chemical shifts of human wildtype Glucocorticoid receptor Ligand Binding Domain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26756 |
0.361 |
|
| 2017 |
Noresson AL, Aurelius O, Öberg CT, Engström O, Sundin AP, Håkansson M, Stenström O, Akke M, Logan DT, Leffler H, Nilsson UJ. Designing interactions by control of protein-ligand complex conformation: tuning arginine-arene interaction geometry for enhanced electrostatic protein-ligand interactions. Chemical Science. 9: 1014-1021. PMID 29675148 DOI: 10.1039/C7Sc04749E |
0.351 |
|
| 2017 |
Towse CL, Akke M, Daggett V. The Dynameomics Entropy Dictionary: A Large-Scale Assessment of Conformational Entropy Across Protein Fold Space. The Journal of Physical Chemistry. B. PMID 28375008 DOI: 10.1021/Acs.Jpcb.7B00577 |
0.4 |
|
| 2017 |
Rutsdottir G, Härmark J, Weide Y, Hebert H, Rasmussen MI, Wernersson S, Respondek M, Akke M, Højrup P, Koeck PJB, Söderberg CAG, Emanuelsson C. Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity. The Journal of Biological Chemistry. 292: 8103-8121. PMID 28325834 DOI: 10.1074/Jbc.M116.766816 |
0.358 |
|
| 2016 |
Weininger U, Modig K, Geitner AJ, Schmidpeter PA, Koch JR, Akke M. Dynamics of Aromatic Side Chains in the Active Site of FKBP12. Biochemistry. PMID 27936610 DOI: 10.1021/Acs.Biochem.6B01157 |
0.411 |
|
| 2016 |
Quistgaard EM, Weininger U, Ural-Blimke Y, Modig K, Nordlund P, Akke M, Löw C. Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD. Bmc Biology. 14: 82. PMID 27664121 DOI: 10.1186/S12915-016-0300-3 |
0.366 |
|
| 2016 |
Diehl C, Akke M, Bekker-Jensen S, Mailand N, Streicher W, Wikström M. Structural analysis of a complex between small ubiquitin-like modifier 1 (SUMO1) and the ZZ domain of CREB-binding Protein (CBP/p300) reveals a new interaction surface on SUMO Journal of Biological Chemistry. 291: 12658-12672. PMID 27129204 DOI: 10.1074/Jbc.M115.711325 |
0.394 |
|
| 2015 |
Kukic P, Lundström P, Camilloni C, Evenäs J, Akke M, Vendruscolo M. Structural insights into the calcium-mediated allosteric transition in the C-terminal domain of calmodulin from NMR measurements. Biochemistry. PMID 26618792 DOI: 10.1021/Acs.Biochem.5B00961 |
0.444 |
|
| 2015 |
Wallerstein J, Weininger U, Khan MA, Linse S, Akke M. Site-specific protonation kinetics of acidic side chains in proteins determined by pH-dependent carboxyl (13)C NMR relaxation. Journal of the American Chemical Society. 137: 3093-101. PMID 25665463 DOI: 10.1021/Ja513205S |
0.393 |
|
| 2015 |
Rämisch S, Weininger U, Martnisson J, Akke M, André I. Computational Design of Repeat-Proteins with a Predefined Geometry Biophysical Journal. 108: 13a. DOI: 10.1016/J.Bpj.2014.11.097 |
0.323 |
|
| 2014 |
Genheden S, Akke M, Ryde U. Conformational Entropies and Order Parameters: Convergence, Reproducibility, and Transferability. Journal of Chemical Theory and Computation. 10: 432-8. PMID 26579922 DOI: 10.1021/Ct400747S |
0.428 |
|
| 2014 |
Rämisch S, Weininger U, Martinsson J, Akke M, André I. Computational design of a leucine-rich repeat protein with a predefined geometry. Proceedings of the National Academy of Sciences of the United States of America. 111: 17875-80. PMID 25427795 DOI: 10.1073/Pnas.1413638111 |
0.318 |
|
| 2014 |
Weininger U, Modig K, Akke M. Ring flips revisited: (13)C relaxation dispersion measurements of aromatic side chain dynamics and activation barriers in basic pancreatic trypsin inhibitor. Biochemistry. 53: 4519-25. PMID 24983918 DOI: 10.1021/Bi500462K |
0.397 |
|
| 2014 |
Weininger U, Brath U, Modig K, Teilum K, Akke M. Off-resonance rotating-frame relaxation dispersion experiment for 13C in aromatic side chains using L-optimized TROSY-selection. Journal of Biomolecular Nmr. 59: 23-9. PMID 24706175 DOI: 10.1007/S10858-014-9826-2 |
0.483 |
|
| 2013 |
Weininger U, Blissing AT, Hennig J, Ahlner A, Liu Z, Vogel HJ, Akke M, Lundström P. Protein conformational exchange measured by 1H R1ρ relaxation dispersion of methyl groups. Journal of Biomolecular Nmr. 57: 47-55. PMID 23904100 DOI: 10.1007/S10858-013-9764-4 |
0.418 |
|
| 2013 |
Weininger U, Respondek M, Löw C, Akke M. Slow aromatic ring flips detected despite near-degenerate NMR frequencies of the exchanging nuclei. The Journal of Physical Chemistry. B. 117: 9241-7. PMID 23859599 DOI: 10.1021/Jp4058065 |
0.348 |
|
| 2012 |
Weininger U, Liu Z, McIntyre DD, Vogel HJ, Akke M. Specific 12CβD(2)12CγD(2)S13CεHD(2) isotopomer labeling of methionine to characterize protein dynamics by 1H and 13C NMR relaxation dispersion. Journal of the American Chemical Society. 134: 18562-5. PMID 23106551 DOI: 10.1021/Ja309294U |
0.508 |
|
| 2012 |
Weininger U, Respondek M, Akke M. Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected 13C CPMG relaxation dispersion Journal of Biomolecular Nmr. 54: 9-14. PMID 22833056 DOI: 10.1007/S10858-012-9656-Z |
0.494 |
|
| 2012 |
Weininger U, Diehl C, Akke M. 13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy Journal of Biomolecular Nmr. 53: 181-190. PMID 22752933 DOI: 10.1007/S10858-012-9650-5 |
0.441 |
|
| 2012 |
Akke M. Conformational dynamics and thermodynamics of protein-ligand binding studied by NMR relaxation. Biochemical Society Transactions. 40: 419-423. PMID 22435823 DOI: 10.1042/Bst20110750 |
0.394 |
|
| 2012 |
Saraboji K, HÃ¥kansson M, Genheden S, Diehl C, Qvist J, Weininger U, Nilsson UJ, Leffler H, Ryde U, Akke M, Logan DT. The carbohydrate-binding site in galectin-3 is preorganized to recognize a sugarlike framework of oxygens: ultra-high-resolution structures and water dynamics. Biochemistry. 51: 296-306. PMID 22111949 DOI: 10.1021/Bi201459P |
0.393 |
|
| 2011 |
Blobel J, Brath U, Bernadó P, Diehl C, Ballester L, Sornosa A, Akke M, Pons M. Protein loop compaction and the origin of the effect of arginine and glutamic acid mixtures on solubility, stability and transient oligomerization of proteins. European Biophysics Journal : Ebj. 40: 1327-38. PMID 21390527 DOI: 10.1007/S00249-011-0686-3 |
0.371 |
|
| 2011 |
Oktaviani NA, Otten R, Dijkstra K, Scheek RM, Thulin E, Akke M, Mulder FA. 100% complete assignment of non-labile (1)H, (13)C, and (15)N signals for calcium-loaded Calbindin D(9k) P43G. Biomolecular Nmr Assignments. 5: 79-84. PMID 21069485 DOI: 10.1007/S12104-010-9272-3 |
0.653 |
|
| 2010 |
Genheden S, Diehl C, Akke M, Ryde U. Starting-Condition Dependence of Order Parameters Derived from Molecular Dynamics Simulations. Journal of Chemical Theory and Computation. 6: 2176-90. PMID 26615944 DOI: 10.1021/Ct900696Z |
0.359 |
|
| 2010 |
Lindman S, Bauer MC, Lund M, Diehl C, Mulder FAA, Akke M, Linse S. PKa values for the unfolded state under native conditions explain the pH-dependent stability of PGB1 Biophysical Journal. 99: 3365-3373. PMID 21081085 DOI: 10.1016/J.Bpj.2010.08.078 |
0.343 |
|
| 2010 |
Dhulesia A, Cremades N, Kumita JR, Hsu ST, Mossuto MF, Dumoulin M, Nietlispach D, Akke M, Salvatella X, Dobson CM. Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution. Journal of the American Chemical Society. 132: 15580-8. PMID 20958028 DOI: 10.1021/Ja103524M |
0.36 |
|
| 2010 |
Diehl C, Engström O, Delaine T, Håkansson M, Genheden S, Modig K, Leffler H, Ryde U, Nilsson UJ, Akke M. Protein flexibility and conformational entropy in ligand design targeting the carbohydrate recognition domain of galectin-3. Journal of the American Chemical Society. 132: 14577-89. PMID 20873837 DOI: 10.1021/Ja105852Y |
0.389 |
|
| 2010 |
Bernadó P, Modig K, Grela P, Svergun DI, Tchorzewski M, Pons M, Akke M. Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR Relaxation. Biophysical Journal. 98: 2374-82. PMID 20483347 DOI: 10.1016/J.Bpj.2010.02.012 |
0.4 |
|
| 2009 |
Teilum K, Smith MH, Schulz E, Christensen LC, Solomentsev G, Oliveberg M, Akke M. Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization. Proceedings of the National Academy of Sciences of the United States of America. 106: 18273-8. PMID 19828437 DOI: 10.1073/Pnas.0907387106 |
0.36 |
|
| 2009 |
Diehl C, Genheden S, Modig K, Ryde U, Akke M. Conformational entropy changes upon lactose binding to the carbohydrate recognition domain of galectin-3. Journal of Biomolecular Nmr. 45: 157-69. PMID 19641853 DOI: 10.1007/S10858-009-9356-5 |
0.445 |
|
| 2009 |
Brath U, Akke M. Differential responses of the backbone and side-chain conformational dynamics in FKBP12 upon binding the transition-state analog FK506: implications for transition-state stabilization and target protein recognition. Journal of Molecular Biology. 387: 233-244. PMID 19361439 DOI: 10.1016/J.Jmb.2009.01.047 |
0.39 |
|
| 2008 |
Paquin R, Ferrage F, Mulder FA, Akke M, Bodenhausen G. Multiple-timescale dynamics of side-chain carboxyl and carbonyl groups in proteins by 13C nuclear spin relaxation. Journal of the American Chemical Society. 130: 15805-7. PMID 18975903 DOI: 10.1021/Ja803794G |
0.682 |
|
| 2007 |
Igumenova TI, Brath U, Akke M, Palmer AG. Characterization of chemical exchange using residual dipolar coupling. Journal of the American Chemical Society. 129: 13396-7. PMID 17929930 DOI: 10.1021/Ja0761636 |
0.387 |
|
| 2007 |
Lundström P, Teilum K, Carstensen T, Bezsonova I, Wiesner S, Hansen DF, Religa TL, Akke M, Kay LE. Fractional 13C enrichment of isolated carbons using [1-13C]- or [2- 13C]-glucose facilitates the accurate measurement of dynamics at backbone Calpha and side-chain methyl positions in proteins. Journal of Biomolecular Nmr. 38: 199-212. PMID 17554498 DOI: 10.1007/S10858-007-9158-6 |
0.535 |
|
| 2007 |
Grela P, Helgstrand M, Krokowski D, Boguszewska A, Svergun D, Liljas A, Bernadó P, Grankowski N, Akke M, Tchórzewski M. Structural characterization of the ribosomal P1A-P2B protein dimer by small-angle X-ray scattering and NMR spectroscopy. Biochemistry. 46: 1988-98. PMID 17261029 DOI: 10.1021/Bi0616450 |
0.382 |
|
| 2007 |
Helgstrand M, Mandava CS, Mulder FA, Liljas A, Sanyal S, Akke M. The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G and RF3 via a conserved region of the L12 C-terminal domain. Journal of Molecular Biology. 365: 468-79. PMID 17070545 DOI: 10.1016/J.Jmb.2006.10.025 |
0.645 |
|
| 2006 |
Teilum K, Poulsen FM, Akke M. The inverted chevron plot measured by NMR relaxation reveals a native-like unfolding intermediate in acyl-CoA binding protein. Proceedings of the National Academy of Sciences of the United States of America. 103: 6877-82. PMID 16641108 DOI: 10.1073/Pnas.0509100103 |
0.376 |
|
| 2006 |
Brath U, Akke M, Yang D, Kay LE, Mulder FA. Functional dynamics of human FKBP12 revealed by methyl 13C rotating frame relaxation dispersion NMR spectroscopy. Journal of the American Chemical Society. 128: 5718-27. PMID 16637639 DOI: 10.1021/Ja0570279 |
0.729 |
|
| 2006 |
Teilum K, Brath U, Lundström P, Akke M. Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements. Journal of the American Chemical Society. 128: 2506-7. PMID 16492013 DOI: 10.1021/Ja055660O |
0.428 |
|
| 2005 |
Lundström P, Mulder FA, Akke M. Correlated dynamics of consecutive residues reveal transient and cooperative unfolding of secondary structure in proteins. Proceedings of the National Academy of Sciences of the United States of America. 102: 16984-9. PMID 16278300 DOI: 10.1073/Pnas.0504361102 |
0.685 |
|
| 2005 |
Fast J, Mossberg A, Nilsson H, Svanborg C, Akke M, Linse S. Compact oleic acid in HAMLET Febs Letters. 579: 6095-6100. PMID 16229842 DOI: 10.1016/J.Febslet.2005.08.089 |
0.317 |
|
| 2005 |
Lundström P, Akke M. Off-resonance rotating-frame amide proton spin relaxation experiments measuring microsecond chemical exchange in proteins. Journal of Biomolecular Nmr. 32: 163-173. PMID 16034667 DOI: 10.1007/S10858-005-5027-3 |
0.42 |
|
| 2005 |
Lundström P, Akke M. Microsecond protein dynamics measured by C-13(alpha) rotating-frame spin relaxation Chembiochem. 6: 1685-1692. PMID 16028301 DOI: 10.1002/Cbic.200500086 |
0.466 |
|
| 2005 |
Ternström T, Svendsen A, Akke M, Adlercreutz P. Unfolding and inactivation of cutinases by AOT and guanidine hydrochloride. Biochimica Et Biophysica Acta. 1748: 74-83. PMID 15752695 DOI: 10.1016/J.Bbapap.2004.12.014 |
0.333 |
|
| 2004 |
Otzen DE, Miron S, Akke M, Oliveberg M. Transient aggregation and stable dimerization induced by introducing an Alzheimer sequence into a water-soluble protein. Biochemistry. 43: 12964-12978. PMID 15476390 DOI: 10.1021/Bi048509K |
0.33 |
|
| 2004 |
Mulder FA, Bouakaz L, Lundell A, Venkataramana M, Liljas A, Akke M, Sanyal S. Conformation and dynamics of ribosomal stalk protein L12 in solution and on the ribosome. Biochemistry. 43: 5930-6. PMID 15147176 DOI: 10.1021/Bi0495331 |
0.645 |
|
| 2004 |
Helgstrand M, Vanbelle C, Thulin E, Linse S, Akke M. Letter to the Editor: Sequential H-1, N-15 and C-13 NMR assignment of human calbindin D28k Journal of Biomolecular Nmr. 28: 305-306. PMID 14752267 DOI: 10.1023/B:Jnmr.0000013690.46725.53 |
0.348 |
|
| 2004 |
Lundström P, Akke M. Quantitative analysis of conformational exchange contributions to H-1-N-15 multiple-quantum relaxation using field-dependent measurements. Time scale and structural characterization of exchange in a calmodulin C-terminal domain mutant Journal of the American Chemical Society. 126: 928-935. PMID 14733570 DOI: 10.1021/Ja037529R |
0.42 |
|
| 2003 |
Bernadó P, Akerud T, García de la Torre J, Akke M, Pons M. Combined use of NMR relaxation measurements and hydrodynamic calculations to study protein association. Evidence for tetramers of low molecular weight protein tyrosine phosphatase in solution. Journal of the American Chemical Society. 125: 916-23. PMID 12537489 DOI: 10.1021/Ja027836H |
0.416 |
|
| 2003 |
Mulder FAA, Akke M. Carbonyl 13C Transverse Relaxation Measurements to Sample Protein Backbone Dynamics. Magnetic Resonance in Chemistry. 41: 853-865. DOI: 10.1002/Mrc.1252 |
0.436 |
|
| 2002 |
Akke M. NMR methods for characterizing microsecond to millisecond dynamics in recognition and catalysis. Current Opinion in Structural Biology. 12: 642-647. PMID 12464317 DOI: 10.1016/S0959-440X(02)00369-X |
0.344 |
|
| 2002 |
Akerud T, Thulin E, Van Etten RL, Akke M. Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: a model for changes in dynamics upon target binding. Journal of Molecular Biology. 322: 137-52. PMID 12215420 DOI: 10.1016/S0022-2836(02)00714-3 |
0.47 |
|
| 2002 |
Eisenmesser EZ, Bosco DA, Akke M, Kern D. Enzyme dynamics during catalysis. Science (New York, N.Y.). 295: 1520-3. PMID 11859194 DOI: 10.1126/Science.1066176 |
0.342 |
|
| 2001 |
Akke M, Chazin WJ. An open and shut case Nature Structural Biology. 8: 910-912. PMID 11685229 DOI: 10.1038/Nsb1101-910 |
0.37 |
|
| 2001 |
Evenäs J, Malmendal A, Akke M. Dynamics of the Transition between Open and Closed Conformations in a Calmodulin C-Terminal Domain Mutant Structure. 9: 185-195. PMID 11286885 DOI: 10.1016/S0969-2126(01)00575-5 |
0.387 |
|
| 2000 |
Cavanagh J, Akke M. May the driving force be with you--whatever it is. Nature Structural Biology. 7: 11-3. PMID 10625416 DOI: 10.1038/71202 |
0.306 |
|
| 1999 |
Ternström T, Mayor U, Akke M, Oliveberg M. From snapshot to movie: φ analysis of protein folding transition states taken one step further Proceedings of the National Academy of Sciences of the United States of America. 96: 14854-14859. PMID 10611302 DOI: 10.1073/Pnas.96.26.14854 |
0.345 |
|
| 1999 |
Malmendal A, Evenäs J, Forsén S, Akke M. Structural dynamics in the C-terminal domain of calmodulin at low calcium levels. Journal of Molecular Biology. 293: 883-899. PMID 10543974 DOI: 10.1006/Jmbi.1999.3188 |
0.393 |
|
| 1999 |
Evenäs J, Forsén S, Malmendal A, Akke M. Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations. Journal of Molecular Biology. 289: 603-617. PMID 10356332 DOI: 10.1006/Jmbi.1999.2770 |
0.439 |
|
| 1998 |
Malmendal A, Carlström G, Hambraeus C, Drakenberg T, Forsén S, Akke M. Sequence and context dependence of EF-hand loop dynamics. An 15N relaxation study of a calcium-binding site mutant of calbindin D9k. Biochemistry. 37: 2586-2595. PMID 9485409 DOI: 10.1021/Bi971798A |
0.429 |
|
| 1998 |
Akke M, Liu J, Cavanagh J, Erickson HP, Palmer AG. Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain. Nature Structural Biology. 5: 55-9. PMID 9437430 DOI: 10.1038/nsb0198-55 |
0.3 |
|
| 1996 |
Mandel AM, Akke M, Palmer AG. Dynamics of ribonuclease H: temperature dependence of motions on multiple time scales. Biochemistry. 35: 16009-23. PMID 8973171 DOI: 10.1021/Bi962089K |
0.377 |
|
| 1996 |
Akke M, Palmer AG. Monitoring Macromolecular Motions on Microsecond to Millisecond Time Scales by R1ρ−R1 Constant Relaxation Time NMR Spectroscopy Journal of the American Chemical Society. 118: 911-912. DOI: 10.1021/Ja953503R |
0.307 |
|
| 1995 |
Akke M, Forsén S, Chazin WJ. Solution structure of (Cd2+)1-calbindin D9k reveals details of the stepwise structural changes along the Apo → (Ca2+)1II → (Ca2+)2I,II binding pathway Journal of Molecular Biology. 252: 102-121. PMID 7666423 DOI: 10.1006/Jmbi.1995.0478 |
0.4 |
|
| 1993 |
Kordel J, Skelton NJ, Akke M, Chazin WJ. High-resolution structure of calcium-loaded calbindin D9k. Journal of Molecular Biology. 231: 711-734. DOI: 10.2210/Pdb2Bca/Pdb |
0.305 |
|
| 1993 |
Skelton NJ, Palmer AG, Akke M, Kordel J, Rance M, Chazin WJ. Practical Aspects of Two-Dimensional Proton-Detected 15N Spin Relaxation Measurements Journal of Magnetic Resonance, Series B. 102: 253-264. DOI: 10.1006/Jmrb.1993.1095 |
0.374 |
|
| 1993 |
Akke M, Forsén S, Chazin WJ. 15N NMR assignments of (Cd2+,)2‐calbindin D9k and comparison with (Ca2+)2‐calbindin D9k. Cadmium as a substitute for calcium in calcium‐binding proteins Magnetic Resonance in Chemistry. 31. DOI: 10.1002/Mrc.1260311324 |
0.318 |
|
| 1992 |
Akke M, Drakenberg T, Chazin WJ. Three-dimensional solution structure of Ca2+-loaded porcine calbindin D9k determined by nuclear magnetic resonance spectroscopy Biochemistry®. 31: 1011-1020. PMID 1734952 DOI: 10.1021/Bi00119A009 |
0.33 |
|
| 1992 |
Kördel J, Skelton NJ, Akke M, Palmer AG, Chazin WJ. Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-detected 15N NMR spectroscopy. Biochemistry. 31: 4856-66. PMID 1591246 DOI: 10.1021/Bi00135A017 |
0.331 |
|
| 1992 |
Skelton NJ, Kördel J, Akke M, Chazin WJ. Nuclear magnetic resonance studies of the internal dynamics in apo, (Cd2+)1 and (Ca2+)2 Calbindin D9k. The rates of amide proton exchange with solvent Journal of Molecular Biology. 227: 1100-1117. PMID 1331470 DOI: 10.1016/0022-2836(92)90524-N |
0.388 |
|
| 1991 |
Akke M, Forsén S, Chazin WJ. Molecular basis for co-operativity in Ca2+ binding to calbindin D9k. 1H nuclear magnetic resonance studies of (Cd2+)1-bovine calbindin D9k Journal of Molecular Biology. 220: 173-189. PMID 2067016 DOI: 10.1016/0022-2836(91)90389-N |
0.404 |
|
| 1991 |
Forsén S, Akke M, Linse S, Chazin W. Ca2+-Binding in proteins of the calmodulin superfamily:Cooperativity and its molecular basis. Journal of Inorganic Biochemistry. 43: 387. DOI: 10.1016/0162-0134(91)84372-G |
0.326 |
|
| 1990 |
Akke M, Forsén S. Protein stability and electrostatic interactions between solvent exposed charged side chains Proteins. 8: 23-29. PMID 2217161 DOI: 10.1002/Prot.340080106 |
0.337 |
|
| 1989 |
Forsén S, Akke M, Brodin P, Bayley P, Drakenberg T, Grundström T, Johansson C, Linse S, Martin S, Thulin E. Neutralization of surface charges markedly affects the properties of bovine calbindin D9k. Advances in Experimental Medicine and Biology. 255: 185-94. PMID 2618856 DOI: 10.1007/978-1-4684-5679-0_20 |
0.386 |
|
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