Albert Lau, PhD - Publications

Affiliations: 
Biophysics and Biophysical Chemistry Johns Hopkins University, Baltimore, MD 
Website:
http://pmcb.jhu.edu/faculty/lau-profile.html

23 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
2017 Yu A, Salazar H, Plested AJR, Lau AY. Neurotransmitter Funneling Optimizes Glutamate Receptor Kinetics. Neuron. PMID 29249286 DOI: 10.1016/j.neuron.2017.11.024  0.44
2016 Baranovic J, Chebli M, Salazar H, Carbone AL, Faelber K, Lau AY, Daumke O, Plested AJ. Dynamics of the Ligand Binding Domain Layer during AMPA Receptor Activation. Biophysical Journal. 110: 896-911. PMID 26910426 DOI: 10.1016/j.bpj.2015.12.033  0.44
2016 Yu A, Wied T, Belcher J, Lau AY. Computing conformational free energies of iGluR Ligand-binding domains Neuromethods. 106: 119-132. DOI: 10.1007/978-1-4939-2812-5_9  1
2013 Yao Y, Belcher J, Berger AJ, Mayer ML, Lau AY. Conformational analysis of NMDA receptor GluN1, GluN2, and GluN3 ligand-binding domains reveals subtype-specific characteristics. Structure (London, England : 1993). 21: 1788-99. PMID 23972471 DOI: 10.1016/j.str.2013.07.011  1
2013 Lau AY, Salazar H, Blachowicz L, Ghisi V, Plested AJ, Roux B. A conformational intermediate in glutamate receptor activation. Neuron. 79: 492-503. PMID 23931998 DOI: 10.1016/j.neuron.2013.06.003  1
2011 Lau AY, Roux B. Structural biology: One domain, multiple conformations. Nature Chemical Biology. 7: 130-1. PMID 21321548 DOI: 10.1038/nchembio.527  1
2011 Lau AY, Roux B. The hidden energetics of ligand binding and activation in a glutamate receptor. Nature Structural & Molecular Biology. 18: 283-7. PMID 21317895 DOI: 10.1038/nsmb.2010  1
2010 Contreras JE, Chen J, Lau AY, Jogini V, Roux B, Holmgren M. Voltage profile along the permeation pathway of an open channel. Biophysical Journal. 99: 2863-9. PMID 21044583 DOI: 10.1016/j.bpj.2010.08.053  1
2009 Kollewe A, Lau AY, Sullivan A, Roux B, Goldstein SA. A structural model for K2P potassium channels based on 23 pairs of interacting sites and continuum electrostatics. The Journal of General Physiology. 134: 53-68. PMID 19564427 DOI: 10.1085/jgp.200910235  1
2009 Numano R, Szobota S, Lau AY, Gorostiza P, Volgraf M, Roux B, Trauner D, Isacoff EY. Nanosculpting reversed wavelength sensitivity into a photoswitchable iGluR. Proceedings of the National Academy of Sciences of the United States of America. 106: 6814-9. PMID 19342491 DOI: 10.1073/pnas.0811899106  1
2008 Park S, Lau AY, Roux B. Computing conformational free energy by deactivated morphing. The Journal of Chemical Physics. 129: 134102. PMID 19045073 DOI: 10.1063/1.2982170  1
2007 Lau AY, Roux B. The free energy landscapes governing conformational changes in a glutamate receptor ligand-binding domain. Structure (London, England : 1993). 15: 1203-14. PMID 17937910 DOI: 10.1016/j.str.2007.07.015  1
2004 Ramachandran N, Hainsworth E, Bhullar B, Eisenstein S, Rosen B, Lau AY, Walter JC, LaBaer J. Self-assembling protein microarrays. Science (New York, N.Y.). 305: 86-90. PMID 15232106 DOI: 10.1126/science.1097639  1
2004 Lau AY, Chasman DI. Functional classification of proteins and protein variants. Proceedings of the National Academy of Sciences of the United States of America. 101: 6576-81. PMID 15087495 DOI: 10.1073/pnas.0305043101  1
2003 Williams RS, Chasman DI, Hau DD, Hui B, Lau AY, Glover JN. Detection of protein folding defects caused by BRCA1-BRCT truncation and missense mutations. The Journal of Biological Chemistry. 278: 53007-16. PMID 14534301 DOI: 10.1074/jbc.M310182200  1
2001 Hollis T, Lau A, Ellenberger T. Crystallizing thoughts about DNA base excision repair Progress in Nucleic Acid Research and Molecular Biology. 68: 305-314. PMID 11554308  1
2001 Abner CW, Lau AY, Ellenberger T, Bloom LB. Base excision and DNA binding activities of human alkyladenine DNA glycosylase are sensitive to the base paired with a lesion. The Journal of Biological Chemistry. 276: 13379-87. PMID 11278716 DOI: 10.1074/jbc.M010641200  1
2001 Lau AY, Waytt MD, Glassner BJ, Samson LD, Ellenberger T, Guliaev AB, Singer B. Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG Chemtracts. 14: 142-147.  1
2000 Lau AY, Wyatt MD, Glassner BJ, Samson LD, Ellenberger T. Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG. Proceedings of the National Academy of Sciences of the United States of America. 97: 13573-8. PMID 11106395 DOI: 10.1073/pnas.97.25.13573  1
2000 Hollis T, Lau A, Ellenberger T. Structural studies of human alkyladenine glycosylase and E. coli 3-methyladenine glycosylase Mutation Research - Dna Repair. 460: 201-210. PMID 10946229 DOI: 10.1016/S0921-8777(00)00027-6  1
1999 Wyatt MD, Allan JM, Lau AY, Ellenberger TE, Samson LD. 3-methyladenine DNA glycosylases: structure, function, and biological importance. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 21: 668-76. PMID 10440863 DOI: 10.1002/(SICI)1521-1878(199908)21:8<668::AID-BIES6>3.0.CO;2-D  1
1998 Chin DN, Lau AY, Whitesides GM. Studying how different terminal groups change the motion of H2NSO2C6H4CONH(EG)3R when bound to the active site of human carbonic anhydrase II. The Journal of Organic Chemistry. 63: 938-45. PMID 14994755  1
1998 Lau AY, Schärer OD, Samson L, Verdine GL, Ellenberger T. Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision. Cell. 95: 249-58. PMID 9790531 DOI: 10.1016/S0092-8674(00)81755-9  1
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