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Bryan F. Shaw, Ph.D. - Publications

Affiliations: 
2005 University of California, Los Angeles, Los Angeles, CA 
Area:
Copper-Zinc Superoxide Dismutase and ALS, Redox Balance, Oxidative Stress, and Metal Ion Metabolism in Eukaryotic Cells
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39 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
2022 Dashnaw CM, Zhang AY, Gonzalez M, Koone JC, Shaw BF. Metal migration and subunit swapping in ALS-linked SOD1: Zn transfer between mutant and wild-type occurs faster than the rate of heterodimerization. The Journal of Biological Chemistry. 298: 102610. PMID 36265587 DOI: 10.1016/j.jbc.2022.102610  0.302
2021 Dashnaw CM, Koone JC, Abdolvahabi A, Shaw BF. Measuring how two proteins affect each other's net charge in a crowded environment. Protein Science : a Publication of the Protein Society. PMID 33928693 DOI: 10.1002/pro.4092  0.759
2020 Zhang AY, Koone JC, Dashnaw CM, Zahler CT, Shaw BF. Complete Charge Regulation by a Redox Enzyme Upon Single Electron Transfer. Angewandte Chemie (International Ed. in English). PMID 32212239 DOI: 10.1002/Anie.202001452  0.432
2020 Baumer KM, Koone JC, Shaw BF. Kinetic variability in seeded formation of ALS-linked SOD1 fibrils across multiple generations. Acs Chemical Neuroscience. PMID 31895541 DOI: 10.1021/Acschemneuro.9B00464  0.384
2019 Zahler CT, Shaw BF. What are we missing by not measuring the net charge of proteins? Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 30779227 DOI: 10.1002/Chem.201900178  0.433
2019 Zahler CT, Shaw BF. Frontispiece: What Are We Missing by Not Measuring the Net Charge of Proteins? Chemistry – a European Journal. 25. DOI: 10.1002/Chem.201983261  0.373
2018 Rasouli S, Abdolvahabi A, Croom CM, Plewman D, Shi Y, Shaw BF. Glycerolipid headgroups control rate and mechanism of SOD1 aggregation and accelerate fibrillization of slowly aggregating ALS mutants. Acs Chemical Neuroscience. PMID 29649360 DOI: 10.1021/Acschemneuro.8B00086  0.781
2018 Zahler CT, Zhou H, Abdolvahabi A, Holden RL, Rasouli S, Tao P, Shaw B. Direct Measurement of Charge Regulation in Metalloprotein Electron Transfer. Angewandte Chemie (International Ed. in English). PMID 29451960 DOI: 10.1002/Anie.201712306  0.783
2018 Zahler CT, Zhou H, Abdolvahabi A, Holden RL, Rasouli S, Tao P, Shaw BF. Inside Back Cover: Direct Measurement of Charge Regulation in Metalloprotein Electron Transfer (Angew. Chem. Int. Ed. 19/2018) Angewandte Chemie International Edition. 57: 5555-5555. DOI: 10.1002/Anie.201803479  0.759
2018 Zahler CT, Zhou H, Abdolvahabi A, Holden RL, Rasouli S, Tao P, Shaw BF. Innenrücktitelbild: Direct Measurement of Charge Regulation in Metalloprotein Electron Transfer (Angew. Chem. 19/2018) Angewandte Chemie. 130: 5655-5655. DOI: 10.1002/Ange.201803479  0.76
2017 Rasouli S, Abdolvahabi A, Croom CM, Plewman DL, Shi Y, Ayers JI, Shaw BF. Lysine acylation in superoxide dismutase-1 electrostatically inhibits formation of fibrils with prion-like seeding. The Journal of Biological Chemistry. PMID 28974578 DOI: 10.1074/Jbc.M117.805283  0.785
2017 Abdolvahabi A, Shi Y, Rasouli S, Croom CM, Aliyan A, Marti AA, Shaw BF. Kaplan-Meier meets chemical kinetics: intrinsic rate of SOD1 amyloidogenesis decreased by subset of ALS mutations and cannot fully explain age of disease onset. Acs Chemical Neuroscience. PMID 28290665 DOI: 10.1021/Acschemneuro.7B00029  0.78
2017 Abdolvahabi A, Shi Y, Rasouli S, Croom CM, Chuprin A, Shaw BF. How Do Gyrating Beads Accelerate Amyloid Fibrillization? Biophysical Journal. 112: 250-264. PMID 28122213 DOI: 10.1016/J.Bpj.2016.12.004  0.775
2016 Shi Y, Acerson MJ, Abdolvahabi A, Mowery RA, Shaw BF. Gibbs energy of superoxide dismutase heterodimerization accounts for variable survival in amyotrophic lateral sclerosis. Journal of the American Chemical Society. PMID 27054659 DOI: 10.1021/Jacs.6B01742  0.796
2016 Abdolvahabi A, Shi Y, Chuprin A, Rasouli S, Shaw BF. Stochastic formation of fibrillar and amorphous superoxide dismutase oligomers linked to amyotrophic lateral sclerosis. Acs Chemical Neuroscience. PMID 26979728 DOI: 10.1021/Acschemneuro.6B00048  0.777
2015 Shi Y, Acerson MJ, Shuford KL, Shaw BF. Voltage-Induced Misfolding of Zinc-Replete ALS Mutant Superoxide Dismutase-1. Acs Chemical Neuroscience. PMID 26207449 DOI: 10.1021/Acschemneuro.5B00146  0.746
2015 Abdolvahabi A, Shi Y, Rhodes NR, Cook NP, Martí AA, Shaw BF. Arresting amyloid with coulomb's law: acetylation of ALS-linked SOD1 by aspirin impedes aggregation. Biophysical Journal. 108: 1199-212. PMID 25762331 DOI: 10.1016/J.Bpj.2015.01.014  0.82
2015 Sea K, Sohn SH, Durazo A, Sheng Y, Shaw BF, Cao X, Taylor AB, Whitson LJ, Holloway SP, Hart PJ, Cabelli DE, Gralla EB, Valentine JS. Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase. The Journal of Biological Chemistry. 290: 2405-18. PMID 25433341 DOI: 10.1074/Jbc.M114.588798  0.767
2014 Abdolvahabi A, Gober JL, Mowery RA, Shi Y, Shaw BF. Metal-ion-specific screening of charge effects in protein amide H/D exchange and the Hofmeister series. Analytical Chemistry. 86: 10303-10. PMID 25207790 DOI: 10.1021/Ac502714V  0.786
2014 Shi Y, Abdolvahabi A, Shaw BF. Protein charge ladders reveal that the net charge of ALS-linked superoxide dismutase can be different in sign and magnitude from predicted values. Protein Science : a Publication of the Protein Society. 23: 1417-33. PMID 25052939 DOI: 10.1002/Pro.2526  0.815
2013 Abdolvahabi A, Taylor BW, Holden RL, Shaw EV, Kentsis A, Rodriguez-Galindo C, Mukai S, Shaw BF. Colorimetric and longitudinal analysis of leukocoria in recreational photographs of children with retinoblastoma. Plos One. 8: e76677. PMID 24204654 DOI: 10.1371/Journal.Pone.0076677  0.707
2013 Shi Y, Rhodes NR, Abdolvahabi A, Kohn T, Cook NP, Marti AA, Shaw BF. Deamidation of asparagine to aspartate destabilizes Cu, Zn superoxide dismutase, accelerates fibrillization, and mirrors ALS-linked mutations. Journal of the American Chemical Society. 135: 15897-908. PMID 24066782 DOI: 10.1021/Ja407801X  0.81
2013 Shi Y, Mowery RA, Shaw BF. Effect of metal loading and subcellular pH on net charge of superoxide dismutase-1. Journal of Molecular Biology. 425: 4388-404. PMID 23871896 DOI: 10.1016/J.Jmb.2013.07.018  0.751
2013 Alves NJ, Champion MM, Stefanick JF, Handlogten MW, Moustakas DT, Shi Y, Shaw BF, Navari RM, Kiziltepe T, Bilgicer B. Selective photocrosslinking of functional ligands to antibodies via the conserved nucleotide binding site. Biomaterials. 34: 5700-10. PMID 23601661 DOI: 10.1016/J.Biomaterials.2013.03.082  0.664
2013 Krishnamurthy VM, Raman VS, Mowery RA, Hentz M, Baleja JD, Shaw BF, Kumar K. Ligand-induced protein mobility in complexes of carbonic anhydrase II and benzenesulfonamides with oligoglycine chains. Plos One. 8: e57629. PMID 23472094 DOI: 10.1371/Journal.Pone.0057629  0.314
2012 Shaw BF, Schneider GF, Whitesides GM. Effect of surfactant hydrophobicity on the pathway for unfolding of ubiquitin. Journal of the American Chemical Society. 134: 18739-45. PMID 23095057 DOI: 10.1021/Ja3079863  0.339
2012 Shi Y, Mowery RA, Ashley J, Hentz M, Ramirez AJ, Bilgicer B, Slunt-Brown H, Borchelt DR, Shaw BF. Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding. Protein Science : a Publication of the Protein Society. 21: 1197-209. PMID 22692797 DOI: 10.1002/Pro.2107  0.739
2011 Shaw BF, Schneider GF, Arthanari H, Narovlyansky M, Moustakas D, Durazo A, Wagner G, Whitesides GM. Complexes of native ubiquitin and dodecyl sulfate illustrate the nature of hydrophobic and electrostatic interactions in the binding of proteins and surfactants. Journal of the American Chemical Society. 133: 17681-95. PMID 21939262 DOI: 10.1021/Ja205735Q  0.743
2010 Shaw BF, Arthanari H, Narovlyansky M, Durazo A, Frueh DP, Pollastri MP, Lee A, Bilgicer B, Gygi SP, Wagner G, Whitesides GM. Neutralizing positive charges at the surface of a protein lowers its rate of amide hydrogen exchange without altering its structure or increasing its thermostability. Journal of the American Chemical Society. 132: 17411-25. PMID 21090618 DOI: 10.1021/Ja9067035  0.752
2010 Shaw BF, Moustakas DT, Whitelegge JP, Faull KF. Taking charge of proteins from neurodegeneration to industrial biotechnology. Advances in Protein Chemistry and Structural Biology. 79: 127-64. PMID 20621283 DOI: 10.1016/S1876-1623(10)79004-0  0.414
2009 Durazo A, Shaw BF, Chattopadhyay M, Faull KF, Nersissian AM, Valentine JS, Whitelegge JP. Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperature. The Journal of Biological Chemistry. 284: 34382-9. PMID 19805550 DOI: 10.1074/Jbc.M109.052076  0.757
2009 Oztug Durer ZA, Cohlberg JA, Dinh P, Padua S, Ehrenclou K, Downes S, Tan JK, Nakano Y, Bowman CJ, Hoskins JL, Kwon C, Mason AZ, Rodriguez JA, Doucette PA, Shaw BF, et al. Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase. Plos One. 4: e5004. PMID 19325915 DOI: 10.1371/Journal.Pone.0005004  0.81
2008 Schneider GF, Shaw BF, Lee A, Carillho E, Whitesides GM. Pathway for unfolding of ubiquitin in sodium dodecyl sulfate, studied by capillary electrophoresis. Journal of the American Chemical Society. 130: 17384-93. PMID 19035631 DOI: 10.1021/Ja804736T  0.315
2008 Shaw BF, Schneider GF, Bilgiçer B, Kaufman GK, Neveu JM, Lane WS, Whitelegge JP, Whitesides GM. Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation. Protein Science : a Publication of the Protein Society. 17: 1446-55. PMID 18451358 DOI: 10.1110/Ps.035154.108  0.366
2008 Shaw BF, Lelie HL, Durazo A, Nersissian AM, Xu G, Chan PK, Gralla EB, Tiwari A, Hayward LJ, Borchelt DR, Valentine JS, Whitelegge JP. Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1. The Journal of Biological Chemistry. 283: 8340-50. PMID 18192269 DOI: 10.1074/Jbc.M707751200  0.777
2007 Potter SZ, Zhu H, Shaw BF, Rodriguez JA, Doucette PA, Sohn SH, Durazo A, Faull KF, Gralla EB, Nersissian AM, Valentine JS. Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein. Journal of the American Chemical Society. 129: 4575-83. PMID 17381088 DOI: 10.1021/Ja066690+  0.717
2007 Shaw BF, Valentine JS. How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? Trends in Biochemical Sciences. 32: 78-85. PMID 17208444 DOI: 10.1016/J.Tibs.2006.12.005  0.616
2006 Shaw BF, Durazo A, Nersissian AM, Whitelegge JP, Faull KF, Valentine JS. Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry. The Journal of Biological Chemistry. 281: 18167-76. PMID 16644738 DOI: 10.1074/Jbc.M600623200  0.778
2005 Rodriguez JA, Shaw BF, Durazo A, Sohn SH, Doucette PA, Nersissian AM, Faull KF, Eggers DK, Tiwari A, Hayward LJ, Valentine JS. Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. Proceedings of the National Academy of Sciences of the United States of America. 102: 10516-21. PMID 16020530 DOI: 10.1073/Pnas.0502515102  0.783
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