Shina Caroline Lynn Kamerlin, Ph.D. - Publications

Affiliations: 
2018- Department of Chemistry - BMC Uppsala University, Uppsala, Uppsala län, Sweden 
Area:
Computational enzymology, physical organic chemistry
Website:
kamerlinlab.com

80 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Kulkarni YS, Amyes TL, Richard J, Kamerlin SCL. Uncovering the Role of Key Active Site Side Chains in Catalysis: An Extended Brønsted Relationship for Substrate Deprotonation Catalysed by Wild-Type and Variants of Triosephosphate Isomerase. Journal of the American Chemical Society. PMID 31508957 DOI: 10.1021/jacs.9b08713  1
2019 Calixto AR, Moreira C, Pabis A, Kötting C, Gerwert K, Rudack T, Kamerlin SCL. GTP Hydrolysis Without an Active Site Base: A Unifying Mechanism for Ras and Related GTPases. Journal of the American Chemical Society. PMID 31199130 DOI: 10.1021/jacs.9b03193  1
2019 Al-Smadi D, Enugala TR, Kessler V, Mhashal AR, Kamerlin SCL, Kihlberg J, Norberg T, Widersten M. Chemical and Biochemical Approaches for the Synthesis of Substituted Dihydroxybutanones and Di-, and Tri-Hydroxypentanones. The Journal of Organic Chemistry. PMID 31066559 DOI: 10.1021/acs.joc.9b00742  1
2019 Tatum NJ, Duarte F, Kamerlin SCL, Pohl E. Relative Binding Energies Predict Crystallographic Binding Modes of Ethionamide Booster Lead Compounds. The Journal of Physical Chemistry Letters. PMID 30965004 DOI: 10.1021/acs.jpclett.9b00741  1
2018 Holbrook JB, Curry S, Kamerlin SCL. Debate on academic freedom and open access is healthy. Nature. 562: 494. PMID 30356191 DOI: 10.1038/d41586-018-07153-y  0.32
2018 Hong NS, Petrović D, Lee R, Gryn'ova G, Purg M, Saunders J, Bauer P, Carr PD, Lin CY, Mabbitt PD, Zhang W, Altamore T, Easton C, Coote ML, Kamerlin SCL, et al. The evolution of multiple active site configurations in a designed enzyme. Nature Communications. 9: 3900. PMID 30254369 DOI: 10.1038/s41467-018-06305-y  1
2018 Miton CM, Jonas S, Fischer G, Duarte F, Mohamed MF, van Loo B, Kintses B, Kamerlin SCL, Tokuriki N, Hyvönen M, Hollfelder F. Evolutionary repurposing of a sulfatase: A new Michaelis complex leads to efficient transition state charge offset. Proceedings of the National Academy of Sciences of the United States of America. PMID 30012610 DOI: 10.1073/pnas.1607817115  1
2018 Kaltenbach M, Burke JR, Dindo M, Pabis A, Munsberg FS, Rabin A, Kamerlin SCL, Noel JP, Tawfik DS. Publisher Correction: Evolution of chalcone isomerase from a noncatalytic ancestor. Nature Chemical Biology. PMID 29760514 DOI: 10.1038/s41589-018-0079-3  1
2018 Janfalk Carlsson Å, Bauer P, Dobritzsch D, Kamerlin SCL, Widersten M. Epoxide hydrolysis as a model system for understanding flux through a branched reaction scheme. Iucrj. 5: 269-282. PMID 29755743 DOI: 10.1107/S2052252518003573  1
2018 Kaltenbach M, Burke JR, Dindo M, Pabis A, Munsberg FS, Rabin A, Kamerlin SCL, Noel JP, Tawfik DS. Evolution of chalcone isomerase from a noncatalytic ancestor. Nature Chemical Biology. PMID 29686356 DOI: 10.1038/s41589-018-0042-3  1
2018 Österlund N, Kulkarni YS, Misiaszek AD, Wallin C, Krüger DM, Liao Q, Mashayekhy Rad F, Jarvet J, Strodel B, Wärmländer SKTS, Ilag LL, Kamerlin SCL, Gräslund A. Amyloid-β peptide interactions with amphiphilic surfactants: electrostatic and hydrophobic effects. Acs Chemical Neuroscience. PMID 29683649 DOI: 10.1021/acschemneuro.8b00065  1
2018 Kulkarni YS, Liao Q, Byléhn F, Amyes TL, Richard JP, Kamerlin SCL. The Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase. Journal of the American Chemical Society. PMID 29516737 DOI: 10.1021/jacs.8b00251  1
2017 Krüger DM, Kamerlin SCL. Micelle Maker: An Online Tool for Generating Equilibrated Micelles as Direct Input for Molecular Dynamics Simulations. Acs Omega. 2: 4524-4530. PMID 28884160 DOI: 10.1021/acsomega.7b00820  1
2017 Pabis A, Williams NH, Kamerlin SCL. Simulating the reactions of substituted pyridinio-N-phosphonates with pyridine as a model for biological phosphoryl transfer. Organic & Biomolecular Chemistry. PMID 28819656 DOI: 10.1039/c7ob01734k  1
2017 Maximoff SN, Kamerlin SCL, Florian J. DNA Polymerase λ Active Site Favors a Mutagenic Mispair Between the Enol Form of Deoxyguanosine Triphosphate Substrate and the Keto Form of Thymidine Template. A Free Energy Perturbation Study. The Journal of Physical Chemistry. B. PMID 28732447 DOI: 10.1021/acs.jpcb.7b04874  0.28
2017 Risso VA, Martinez-Rodriguez S, Candel AM, Krüger DM, Pantoja-Uceda D, Ortega-Muñoz M, Santoyo-Gonzalez F, Gaucher EA, Kamerlin SCL, Bruix M, Gavira JA, Sanchez-Ruiz JM. De novo active sites for resurrected Precambrian enzymes. Nature Communications. 8: 16113. PMID 28719578 DOI: 10.1038/ncomms16113  1
2017 Kulkarni YS, Liao Q, Petrovic D, Krüger DM, Strodel B, Amyes TL, Richard J, Kamerlin SCL. Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase. Journal of the American Chemical Society. PMID 28683550 DOI: 10.1021/jacs.7b05576  1
2017 Zhan S, Mårtensson D, Purg M, Kamerlin SCL, Ahlquist MSG. Capturing the Role of Explicit Solvent in the Dimerization of Ru(V) (bda) Water Oxidation Catalysts. Angewandte Chemie (International Ed. in English). PMID 28493633 DOI: 10.1002/anie.201701488  1
2016 Ma H, Szeler K, Kamerlin SCL, Widersten M. Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA). Chemical Science. 7: 1415-1421. PMID 29910900 DOI: 10.1039/c5sc03666f  1
2016 Duarte F, Barrozo A, Aqvist J, Williams NH, Kamerlin SC. The Competing Mechanisms of Phosphate Monoester Dianion Hydrolysis. Journal of the American Chemical Society. PMID 27471914 DOI: 10.1021/jacs.6b06277  1
2016 Pabis A, Duarte F, Kamerlin SC. Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer. Biochemistry. PMID 27187273 DOI: 10.1021/acs.biochem.6b00297  1
2016 Wallin C, Kulkarni YS, Abelein A, Jarvet J, Liao Q, Strodel B, Olsson L, Luo J, Abrahams JP, Sholts SB, Roos PM, Kamerlin SC, Gräslund A, Wärmländer SK. Characterization of Mn(II) ion binding to the amyloid-β peptide in Alzheimer's disease. Journal of Trace Elements in Medicine and Biology : Organ of the Society For Minerals and Trace Elements (Gms). PMID 27085215 DOI: 10.1016/j.jtemb.2016.03.009  1
2015 Amrein BA, Bauer P, Duarte F, Janfalk Carlsson Å, Naworyta A, Mowbray SL, Widersten M, Kamerlin SC. Expanding the Catalytic Triad in Epoxide Hydrolases and Related Enzymes. Acs Catalysis. 5: 5702-5713. PMID 26527505 DOI: 10.1021/acscatal.5b01639  1
2015 Åqvist J, Kamerlin SC. Exceptionally large entropy contributions enable the high rates of GTP hydrolysis on the ribosome. Scientific Reports. 5: 15817. PMID 26497916 DOI: 10.1038/srep15817  1
2015 Carvalho AT, Gouveia ML, Raju Kanna C, Wärmländer SK, Platts J, Kamerlin SC. Theoretical modelling of epigenetically modified DNA sequences. F1000research. 4: 52. PMID 26448859 DOI: 10.12688/f1000research.6148.1  1
2015 Liao Q, Kamerlin SC, Strodel B. Development and Application of a Nonbonded Cu(2+) Model That Includes the Jahn-Teller Effect. The Journal of Physical Chemistry Letters. 6: 2657-62. PMID 26167255 DOI: 10.1021/acs.jpclett.5b01122  1
2015 Barrozo A, Duarte F, Bauer P, Carvalho AT, Kamerlin SC. Cooperative Electrostatic Interactions Drive Functional Evolution in the Alkaline Phosphatase Superfamily. Journal of the American Chemical Society. PMID 26091851 DOI: 10.1021/jacs.5b03945  1
2015 Carvalho AT, O'Donoghue AC, Hodgson DR, Kamerlin SC. Understanding thio-effects in simple phosphoryl systems: role of solvent effects and nucleophile charge. Organic & Biomolecular Chemistry. 13: 5391-8. PMID 25797408 DOI: 10.1039/c5ob00309a  1
2015 Carvalho AT, Szeler K, Vavitsas K, Qvist J, Kamerlin SC. Modeling the mechanisms of biological GTP hydrolysis. Archives of Biochemistry and Biophysics. PMID 25731854 DOI: 10.1016/j.abb.2015.02.027  1
2015 Ben-David M, Sussman JL, Maxwell CI, Szeler K, Kamerlin SC, Tawfik DS. Catalytic stimulation by restrained active-site floppiness--the case of high density lipoprotein-bound serum paraoxonase-1. Journal of Molecular Biology. 427: 1359-74. PMID 25644661 DOI: 10.1016/j.jmb.2015.01.013  1
2015 Åqvist J, Kamerlin SC. The conformation of a catalytic loop is central to GTPase activity on the ribosome. Biochemistry. 54: 546-56. PMID 25515218 DOI: 10.1021/bi501373g  1
2015 Duarte F, Åqvist J, Williams NH, Kamerlin SC. Resolving apparent conflicts between theoretical and experimental models of phosphate monoester hydrolysis. Journal of the American Chemical Society. 137: 1081-93. PMID 25423607 DOI: 10.1021/ja5082712  1
2015 Shurki A, Derat E, Barrozo A, Kamerlin SC. How valence bond theory can help you understand your (bio)chemical reaction. Chemical Society Reviews. 44: 1037-52. PMID 25352378 DOI: 10.1039/c4cs00241e  1
2015 Duarte F, Amrein BA, Blaha-Nelson D, Kamerlin SC. Recent advances in QM/MM free energy calculations using reference potentials. Biochimica Et Biophysica Acta. 1850: 954-965. PMID 25038480 DOI: 10.1016/j.bbagen.2014.07.008  1
2014 Carvalho AT, Gouveia L, Kanna CR, Wärmländer SK, Platts JA, Kamerlin SC. Understanding the structural and dynamic consequences of DNA epigenetic modifications: computational insights into cytosine methylation and hydroxymethylation. Epigenetics : Official Journal of the Dna Methylation Society. 9: 1604-12. PMID 25625845 DOI: 10.4161/15592294.2014.988043  1
2014 Carvalho AT, Barrozo A, Doron D, Kilshtain AV, Major DT, Kamerlin SC. Challenges in computational studies of enzyme structure, function and dynamics. Journal of Molecular Graphics & Modelling. 54: 62-79. PMID 25306098 DOI: 10.1016/j.jmgm.2014.09.003  1
2014 Repi? M, Vianello R, Purg M, Duarte F, Bauer P, Kamerlin SC, Mavri J. Empirical valence bond simulations of the hydride transfer step in the monoamine oxidase B catalyzed metabolism of dopamine. Proteins. 82: 3347-55. PMID 25220264 DOI: 10.1002/prot.24690  1
2014 O'Donoghue AC, Kamerlin SC. Editorial overview: Mechanisms: Chemical and computational probes of biological mechanism. Current Opinion in Chemical Biology. 21: viii-x. PMID 25129687 DOI: 10.1016/j.cbpa.2014.07.025  1
2014 Duarte F, Bauer P, Barrozo A, Amrein BA, Purg M, Aqvist J, Kamerlin SC. Force field independent metal parameters using a nonbonded dummy model. The Journal of Physical Chemistry. B. 118: 4351-62. PMID 24670003 DOI: 10.1021/jp501737x  1
2014 Duarte F, Gronert S, Kamerlin SC. Concerted or stepwise: how much do free-energy landscapes tell us about the mechanisms of elimination reactions? The Journal of Organic Chemistry. 79: 1280-8. PMID 24404911 DOI: 10.1021/jo402702m  1
2014 Duarte F, Geng T, Marloie G, Al Hussain AO, Williams NH, Kamerlin SC. The alkaline hydrolysis of sulfonate esters: challenges in interpreting experimental and theoretical data. The Journal of Organic Chemistry. 79: 2816-28. PMID 24279349 DOI: 10.1021/jo402420t  1
2013 Duarte F, Amrein BA, Kamerlin SC. Modeling catalytic promiscuity in the alkaline phosphatase superfamily. Physical Chemistry Chemical Physics : Pccp. 15: 11160-77. PMID 23728154 DOI: 10.1039/c3cp51179k  1
2013 Wallin G, Kamerlin SC, Aqvist J. Energetics of activation of GTP hydrolysis on the ribosome. Nature Communications. 4: 1733. PMID 23591900 DOI: 10.1038/ncomms2741  1
2013 Luo J, Yu CH, Yu H, Borstnar R, Kamerlin SC, Gräslund A, Abrahams JP, Wärmländer SK. Cellular polyamines promote amyloid-beta (Aβ) peptide fibrillation and modulate the aggregation pathways. Acs Chemical Neuroscience. 4: 454-62. PMID 23509981 DOI: 10.1021/cn300170x  1
2013 Kamerlin SC, Sharma PK, Prasad RB, Warshel A. Why nature really chose phosphate. Quarterly Reviews of Biophysics. 46: 1-132. PMID 23318152 DOI: 10.1017/S0033583512000157  1
2012 Borštnar R, Repič M, Kamerlin SC, Vianello R, Mavri J. Computational Study of the pKa Values of Potential Catalytic Residues in the Active Site of Monoamine Oxidase B. Journal of Chemical Theory and Computation. 8: 3864-70. PMID 26593027 DOI: 10.1021/ct300119u  1
2012 Barrozo A, Borstnar R, Marloie G, Kamerlin SC. Computational protein engineering: bridging the gap between rational design and laboratory evolution. International Journal of Molecular Sciences. 13: 12428-60. PMID 23202907 DOI: 10.3390/ijms131012428  1
2012 Kudavalli JS, Rao SN, Bean DE, Sharma ND, Boyd DR, Fowler PW, Gronert S, Kamerlin SC, Keeffe JR, More O'Ferrall RA. Base-catalyzed dehydration of 3-substituted benzene cis-1,2-dihydrodiols: stabilization of a cyclohexadienide anion intermediate by negative aromatic hyperconjugation. Journal of the American Chemical Society. 134: 14056-69. PMID 22830996 DOI: 10.1021/ja304366j  1
2012 Luo J, van Loo B, Kamerlin SC. Catalytic promiscuity in Pseudomonas aeruginosa arylsulfatase as an example of chemistry-driven protein evolution. Febs Letters. 586: 1622-30. PMID 22673572 DOI: 10.1016/j.febslet.2012.04.012  1
2012 Luo J, van Loo B, Kamerlin SC. Examining the promiscuous phosphatase activity of Pseudomonas aeruginosa arylsulfatase: a comparison to analogous phosphatases. Proteins. 80: 1211-26. PMID 22275090 DOI: 10.1002/prot.24020  1
2012 Borštnar R, Repi? M, Kamerlin SCL, Vianello R, Mavri J. Computational study of the pK a values of potential catalytic residues in the active site of monoamine oxidase B Journal of Chemical Theory and Computation. 8: 3864-3870. DOI: 10.1021/ct300119u  1
2012 Prasad BR, Kamerlin SCL, Florián J, Warshel A. Prechemistry barriers and checkpoints do not contribute to fidelity and catalysis as long as they are not rate limiting Theoretical Chemistry Accounts. 131: 1-15. DOI: 10.1007/s00214-012-1288-6  1
2011 Kamerlin SC. Theoretical comparison of p-nitrophenyl phosphate and sulfate hydrolysis in aqueous solution: implications for enzyme-catalyzed sulfuryl transfer. The Journal of Organic Chemistry. 76: 9228-38. PMID 21981415 DOI: 10.1021/jo201104v  0.01
2011 Adamczyk AJ, Cao J, Kamerlin SC, Warshel A. Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions. Proceedings of the National Academy of Sciences of the United States of America. 108: 14115-20. PMID 21831831 DOI: 10.1073/pnas.1111252108  1
2011 Kamerlin SC, Wilkie J. The effect of leaving group on mechanistic preference in phosphate monoester hydrolysis. Organic & Biomolecular Chemistry. 9: 5394-406. PMID 21655563 DOI: 10.1039/c0ob01210f  1
2011 Plotnikov NV, Kamerlin SC, Warshel A. Paradynamics: an effective and reliable model for ab initio QM/MM free-energy calculations and related tasks. The Journal of Physical Chemistry. B. 115: 7950-62. PMID 21618985 DOI: 10.1021/jp201217b  1
2011 Kamerlin SC, Warshel A. Multiscale modeling of biological functions. Physical Chemistry Chemical Physics : Pccp. 13: 10401-11. PMID 21526232 DOI: 10.1039/c0cp02823a  1
2011 Kamerlin SC, Vicatos S, Dryga A, Warshel A. Coarse-grained (multiscale) simulations in studies of biophysical and chemical systems. Annual Review of Physical Chemistry. 62: 41-64. PMID 21034218 DOI: 10.1146/annurev-physchem-032210-103335  1
2011 Kamerlin SCL, Warshel A. The empirical valence bond model: Theory and applications Wiley Interdisciplinary Reviews: Computational Molecular Science. 1: 30-45. DOI: 10.1002/wcms.10  1
2010 Kamerlin SC, Warshel A. The EVB as a quantitative tool for formulating simulations and analyzing biological and chemical reactions. Faraday Discussions. 145: 71-106. PMID 25285029 DOI: 10.1039/B907354J  1
2010 Kamerlin SC, Warshel A. An Analysis of All the Relevant Facts and Arguments Indicates that Enzyme Catalysis Does Not Involve Large Contributions from Nuclear Tunneling. Journal of Physical Organic Chemistry. 23: 677-684. PMID 21494414 DOI: 10.1002/poc.1620  1
2010 Kamerlin SC, Chu ZT, Warshel A. On catalytic preorganization in oxyanion holes: highlighting the problems with the gas-phase modeling of oxyanion holes and illustrating the need for complete enzyme models. The Journal of Organic Chemistry. 75: 6391-401. PMID 20825150 DOI: 10.1021/jo100651s  1
2010 Kamerlin SC, Mavri J, Warshel A. Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issues. Febs Letters. 584: 2759-66. PMID 20433839 DOI: 10.1016/j.febslet.2010.04.062  1
2010 Kamerlin SC, Sharma PK, Chu ZT, Warshel A. Ketosteroid isomerase provides further support for the idea that enzymes work by electrostatic preorganization. Proceedings of the National Academy of Sciences of the United States of America. 107: 4075-80. PMID 20150513 DOI: 10.1073/pnas.0914579107  1
2010 Kamerlin SC, Warshel A. At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis? Proteins. 78: 1339-75. PMID 20099310 DOI: 10.1002/prot.22654  1
2010 Kamerlin SCL, Warshel A. Reply to Karplus: Conformational dynamics have no role in the chemical step Proceedings of the National Academy of Sciences of the United States of America. 107: E72. DOI: 10.1073/pnas.1002658107  1
2010 Alkherraz A, Kamerlin SCL, Feng G, Sheikh QI, Warshel A, Williams NH. Phosphate ester analogues as probes for understanding enzyme catalysed phosphoryl transfer Faraday Discussions. 145: 281-299. DOI: 10.1039/b908398g  1
2009 Kamerlin SC, Warshel A. On the energetics of ATP hydrolysis in solution. The Journal of Physical Chemistry. B. 113: 15692-8. PMID 19888735 DOI: 10.1021/jp907223t  1
2009 Pisliakov AV, Cao J, Kamerlin SC, Warshel A. Enzyme millisecond conformational dynamics do not catalyze the chemical step. Proceedings of the National Academy of Sciences of the United States of America. 106: 17359-64. PMID 19805169 DOI: 10.1073/pnas.0909150106  1
2009 Kamerlin SC, Cao J, Rosta E, Warshel A. On unjustifiably misrepresenting the EVB approach while simultaneously adopting it. The Journal of Physical Chemistry. B. 113: 10905-15. PMID 19606825 DOI: 10.1021/jp901709f  1
2009 Kamerlin SC, McKenna CE, Goodman MF, Goondman MF, Warshel A. A computational study of the hydrolysis of dGTP analogues with halomethylene-modified leaving groups in solution: implications for the mechanism of DNA polymerases. Biochemistry. 48: 5963-71. PMID 19391628 DOI: 10.1021/bi900140c  1
2009 Kamerlin SC, Haranczyk M, Warshel A. Are mixed explicit/implicit solvation models reliable for studying phosphate hydrolysis? A comparative study of continuum, explicit and mixed solvation models. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 10: 1125-34. PMID 19301306 DOI: 10.1002/cphc.200800753  1
2009 Kamerlin SC, Haranczyk M, Warshel A. Progress in ab initio QM/MM free-energy simulations of electrostatic energies in proteins: accelerated QM/MM studies of pKa, redox reactions and solvation free energies. The Journal of Physical Chemistry. B. 113: 1253-72. PMID 19055405 DOI: 10.1021/jp8071712  1
2009 Kamerlin SCL, McKenna CE, Goodman MF, Warshel A. Correction to a computational study of the hydrolysis of dGTP analogues with halomethylene-modified leaving groups in solution: Implications for the mechanism of DNA polymerases (Biochemistry (2009) 48, (5963) DOI: 10.1021/bi900140c) Biochemistry. 48: 7776. DOI: 10.1021/bi901141c  1
2008 Kamerlin SC, Williams NH, Warshel A. Dineopentyl phosphate hydrolysis: evidence for stepwise water attack. The Journal of Organic Chemistry. 73: 6960-9. PMID 18729515 DOI: 10.1021/jo801207q  1
2008 Kamerlin SC, Florián J, Warshel A. Associative versus dissociative mechanisms of phosphate monoester hydrolysis: on the interpretation of activation entropies. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 9: 1767-73. PMID 18666265 DOI: 10.1002/cphc.200800356  1
2008 Rosta E, Kamerlin SC, Warshel A. On the interpretation of the observed linear free energy relationship in phosphate hydrolysis: a thorough computational study of phosphate diester hydrolysis in solution. Biochemistry. 47: 3725-35. PMID 18307312 DOI: 10.1021/bi702106m  1
2007 Kamerlin SC, Wilkie J. The role of metal ions in phosphate ester hydrolysis. Organic & Biomolecular Chemistry. 5: 2098-108. PMID 17581653 DOI: 10.1039/b701274h  1
2007 Kamerlin SC, Rucker R, Boresch S. A molecular dynamics study of WPD-loop flexibility in PTP1B. Biochemical and Biophysical Research Communications. 356: 1011-6. PMID 17408595 DOI: 10.1016/j.bbrc.2007.03.093  1
2006 Kamerlin SC, Rucker R, Boresch S. A targeted molecular dynamics study of WPD loop movement in PTP1B. Biochemical and Biophysical Research Communications. 345: 1161-6. PMID 16713994 DOI: 10.1016/j.bbrc.2006.04.181  1
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