Year |
Citation |
Score |
2016 |
Zhou YF, Metcalf MC, Garman SC, Edmunds T, Qiu H, Wei RR. Human acid sphingomyelinase structures provide insight to molecular basis of Niemann-Pick disease. Nature Communications. 7: 13082. PMID 27725636 DOI: 10.1038/Ncomms13082 |
0.452 |
|
2016 |
Taabazuing CY, Fermann J, Garman S, Knapp MJ. Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH. Biochemistry. PMID 26727884 DOI: 10.1021/Acs.Biochem.5B01003 |
0.359 |
|
2016 |
Deming DT, Garman SC. The molecular basis of Pompe disease: Crystal structure of acid alpha glucosidase Molecular Genetics and Metabolism. 117: S40-S41. DOI: 10.1016/J.Ymgme.2015.12.239 |
0.463 |
|
2015 |
Ryan KC, Guce AI, Johnson OE, Brunold TC, Cabelli DE, Garman SC, Maroney MJ. Nickel superoxide dismutase: structural and functional roles of His1 and its H-bonding network. Biochemistry. 54: 1016-27. PMID 25580509 DOI: 10.1021/Bi501258U |
0.746 |
|
2015 |
Ferreira S, Ortiz A, Germain DP, Viana-Baptista M, Caldeira-Gomes A, Camprecios M, Fenollar-Cortés M, Gallegos-Villalobos Á, Garcia D, García-Robles JA, Egido J, Gutiérrez-Rivas E, Herrero JA, Mas S, Oancea R, ... ... Garman SC, et al. The alpha-galactosidase A p.Arg118Cys variant does not cause a Fabry disease phenotype: data from individual patients and family studies. Molecular Genetics and Metabolism. 114: 248-58. PMID 25468652 DOI: 10.1016/J.Ymgme.2014.11.004 |
0.414 |
|
2015 |
Metcalf MC, Garman S. Characterization of a potential next generation enzyme replacement molecule for the treatment of Fabry disease Molecular Genetics and Metabolism. 114: S80. DOI: 10.1016/J.Ymgme.2014.12.176 |
0.361 |
|
2015 |
Garman SC, Metcalf MC. Pharmacological chaperoning in Fabry and Schindler diseases Molecular Genetics and Metabolism. 114: S45. DOI: 10.1016/J.Ymgme.2014.12.086 |
0.304 |
|
2014 |
Molla MR, Marcinko T, Prasad P, Deming D, Garman SC, Thayumanavan S. Unlocking a caged lysosomal protein from a polymeric nanogel with a pH trigger. Biomacromolecules. 15: 4046-53. PMID 25291086 DOI: 10.1021/Bm501091P |
0.311 |
|
2014 |
Kolli N, Garman SC. Proteolytic activation of human cathepsin A. The Journal of Biological Chemistry. 289: 11592-600. PMID 24599961 DOI: 10.1074/Jbc.M113.524280 |
0.377 |
|
2013 |
Mohr BG, Dobson CM, Garman SC, Muthukumar M. Electrostatic origin of in vitro aggregation of human γ-crystallin Journal of Chemical Physics. 139. PMID 24089726 DOI: 10.1063/1.4816367 |
0.477 |
|
2013 |
Garman S, Guce AI, Clark NE, Rogich JJ. The molecular basis of pharmacological chaperoning in human alpha-galactosidase Molecular Genetics and Metabolism. 108: S41-S42. DOI: 10.1016/J.Ymgme.2012.11.091 |
0.752 |
|
2013 |
Garman S, Clark NE, Metcalf MC. Pharmacological chaperones for human alpha-N-acetylgalactosaminidase Molecular Genetics and Metabolism. 108: S41. DOI: 10.1016/J.Ymgme.2012.11.090 |
0.708 |
|
2013 |
Rivera-Colon Y, Schutsky EK, Garman SC. Crystal structure of N-acetylgalactosamine-6-sulfatase: The molecular basis for Mucopolysaccharidosis IVA Molecular Genetics and Metabolism. 108: S79. DOI: 10.1016/J.Bpj.2012.11.3143 |
0.798 |
|
2012 |
Clark NE, Metcalf MC, Best D, Fleet GW, Garman SC. Pharmacological chaperones for human α-N-acetylgalactosaminidase. Proceedings of the National Academy of Sciences of the United States of America. 109: 17400-5. PMID 23045655 DOI: 10.1073/Pnas.1203924109 |
0.712 |
|
2012 |
Rivera-Colón Y, Schutsky EK, Kita AZ, Garman SC. The structure of human GALNS reveals the molecular basis for mucopolysaccharidosis IV A. Journal of Molecular Biology. 423: 736-51. PMID 22940367 DOI: 10.1016/J.Jmb.2012.08.020 |
0.797 |
|
2012 |
Rood KL, Clark NE, Stoddard PR, Garman SC, Chien P. Adaptor-dependent degradation of a cell-cycle regulator uses a unique substrate architecture. Structure (London, England : 1993). 20: 1223-32. PMID 22682744 DOI: 10.1016/J.Str.2012.04.019 |
0.656 |
|
2011 |
Guce AI, Clark NE, Rogich JJ, Garman SC. The molecular basis of pharmacological chaperoning in human α-galactosidase. Chemistry & Biology. 18: 1521-6. PMID 22195554 DOI: 10.1016/J.Chembiol.2011.10.012 |
0.748 |
|
2011 |
Caciotti A, Garman SC, Rivera-Colón Y, Procopio E, Catarzi S, Ferri L, Guido C, Martelli P, Parini R, Antuzzi D, Battini R, Sibilio M, Simonati A, Fontana E, Salviati A, et al. GM1 gangliosidosis and Morquio B disease: an update on genetic alterations and clinical findings. Biochimica Et Biophysica Acta. 1812: 782-90. PMID 21497194 DOI: 10.1016/J.Bbadis.2011.03.018 |
0.311 |
|
2010 |
Tomasic IB, Metcalf MC, Guce AI, Clark NE, Garman SC. Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases. The Journal of Biological Chemistry. 285: 21560-6. PMID 20444686 DOI: 10.1074/Jbc.M110.118588 |
0.76 |
|
2010 |
Filoni C, Caciotti A, Carraresi L, Cavicchi C, Parini R, Antuzzi D, Zampetti A, Feriozzi S, Poisetti P, Garman SC, Guerrini R, Zammarchi E, Donati MA, Morrone A. Functional studies of new GLA gene mutations leading to conformational fabry disease Biochimica Et Biophysica Acta - Molecular Basis of Disease. 1802: 247-252. PMID 19941952 DOI: 10.1016/J.Bbadis.2009.11.003 |
0.379 |
|
2010 |
Guce AI, Clark NE, Salgado EN, Ivanen DR, Kulminskaya AA, Brumer H, Garman SC. Catalytic mechanism of human alpha-galactosidase. The Journal of Biological Chemistry. 285: 3625-32. PMID 19940122 DOI: 10.1074/Jbc.M109.060145 |
0.779 |
|
2010 |
Guce AI, Garman SC. The structure of human α-galactosidase a and implications for fabry disease Fabry Disease. 21-38. DOI: 10.1007/978-90-481-9033-1_2 |
0.793 |
|
2009 |
Clark NE, Garman SC. The 1.9 a structure of human alpha-N-acetylgalactosaminidase: The molecular basis of Schindler and Kanzaki diseases. Journal of Molecular Biology. 393: 435-47. PMID 19683538 DOI: 10.1016/J.Jmb.2009.08.021 |
0.768 |
|
2009 |
Herbst RW, Guce A, Bryngelson PA, Higgins KA, Ryan KC, Cabelli DE, Garman SC, Maroney MJ. Role of conserved tyrosine residues in NiSOD catalysis: a case of convergent evolution. Biochemistry. 48: 3354-69. PMID 19183068 DOI: 10.1021/Bi802029T |
0.77 |
|
2007 |
Ishii S, Chang HH, Kawasaki K, Yasuda K, Wu HL, Garman SC, Fan JQ. Mutant alpha-galactosidase A enzymes identified in Fabry disease patients with residual enzyme activity: biochemical characterization and restoration of normal intracellular processing by 1-deoxygalactonojirimycin. The Biochemical Journal. 406: 285-95. PMID 17555407 DOI: 10.1042/Bj20070479 |
0.489 |
|
2007 |
Garman SC. Structure-function relationships in alpha-galactosidase A. Acta Paediatrica (Oslo, Norway : 1992). 96: 6-16. PMID 17391432 DOI: 10.1111/J.1651-2227.2007.00198.X |
0.453 |
|
2006 |
Garman SC. Structural studies on α-GAL and α-NAGAL: The atomic basis of Fabry and Schindler diseases Biocatalysis and Biotransformation. 24: 129-136. DOI: 10.1080/10242420600598194 |
0.411 |
|
2005 |
Hebert DN, Garman SC, Molinari M. The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends in Cell Biology. 15: 364-70. PMID 15939591 DOI: 10.1016/J.Tcb.2005.05.007 |
0.319 |
|
2005 |
Ries M, Gupta S, Moore DF, Sachdev V, Quirk JM, Murray GJ, Rosing DR, Robinson C, Schaefer E, Gal A, Dambrosia JM, Garman SC, Brady RO, Schiffmann R. Pediatric Fabry disease. Pediatrics. 115: e344-55. PMID 15713906 DOI: 10.1542/Peds.2004-1678 |
0.391 |
|
2004 |
Yu Z, Theoret MR, Touloukian CE, Surman DR, Garman SC, Feigenbaum L, Baxter TK, Baker BM, Restifo NP. Poor immunogenicity of a self/tumor antigen derives from peptide-MHC-I instability and is independent of tolerance. The Journal of Clinical Investigation. 114: 551-9. PMID 15314692 DOI: 10.1172/Jci21695 |
0.482 |
|
2004 |
Garman SC, Garboczi DN. The molecular defect leading to Fabry disease: structure of human alpha-galactosidase. Journal of Molecular Biology. 337: 319-35. PMID 15003450 DOI: 10.1016/J.Jmb.2004.01.035 |
0.556 |
|
2003 |
Garman SC, Simcoke WN, Stowers AW, Garboczi DN. Structure of the C-terminal domains of merozoite surface protein-1 from Plasmodium knowlesi reveals a novel histidine binding site. The Journal of Biological Chemistry. 278: 7264-9. PMID 12493733 DOI: 10.1074/Jbc.M210716200 |
0.34 |
|
2002 |
Garman SC, Garboczi DN. Structural basis of Fabry disease. Molecular Genetics and Metabolism. 77: 3-11. PMID 12359124 DOI: 10.1016/S1096-7192(02)00151-8 |
0.517 |
|
2002 |
Garman SC, Hannick L, Zhu A, Garboczi DN. The 1.9 A structure of alpha-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases. Structure (London, England : 1993). 10: 425-34. PMID 12005440 DOI: 10.1016/S0969-2126(02)00726-8 |
0.516 |
|
2002 |
Garman SC, Hannick L, Zhu A, Garboczi DN. The 1.9 Å structure of α-N-acetylgalactosaminidase: molecular basis of glycosidase deficiency diseases Acta Crystallographica Section A. 58: 271-271. DOI: 10.1107/S0108767302095818 |
0.393 |
|
2001 |
Garman SC, Sechi S, Kinet JP, Jardetzky TS. The analysis of the human high affinity IgE receptor FcεRIα from multiple crystal forms Journal of Molecular Biology. 311: 1049-1062. PMID 11531339 DOI: 10.1006/Jmbi.2001.4929 |
0.649 |
|
2000 |
Wurzburg BA, Garman SC, Jardetzky TS. Structure of the human IgE-Fc Cε3-Cε4 reveals conformational flexibility in the antibody effector domains Immunity. 13: 375-385. PMID 11021535 DOI: 10.1016/S1074-7613(00)00037-6 |
0.598 |
|
2000 |
Garman SC, Wurzburg BA, Tarchevskaya SS, Klnet JP, Jardetzky TS. Structure of the Fc fragment of human IgE bound to its high-affinity receptor FcεRIα Nature. 406: 259-266. PMID 10917520 DOI: 10.1038/35018500 |
0.618 |
|
1999 |
Garman SC, Kinet JP, Jardetzky TS. The crystal structure of the human high-affinity IgE receptor (FcεRIα) Annual Review of Immunology. 17: 973-976. PMID 10358779 DOI: 10.1146/Annurev.Immunol.17.1.973 |
0.579 |
|
1998 |
Garman SC, Kinet JP, Jardetzky TS. Crystal structure of the human high-affinity IgE receptor Cell. 95: 951-961. PMID 9875849 DOI: 10.1016/S0092-8674(00)81719-5 |
0.599 |
|
1991 |
Down JA, Garman SC, Gurnett AM, Turner MJ, Wiley DC. Crystallization and preliminary X-ray analysis of an intact soluble-form variant surface glycoprotein from the African trypanosome, Trypanosoma brucei Journal of Molecular Biology. 218: 679-683. PMID 2023242 DOI: 10.1016/0022-2836(91)90254-4 |
0.484 |
|
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