| Year |
Citation |
Score |
| 2022 |
Stiers KM, Owuocha LF, Beamer LJ. Effects of the T337M and G391V disease-related variants on human phosphoglucomutase 1: structural disruptions large and small. Acta Crystallographica. Section F, Structural Biology Communications. 78: 200-209. PMID 35506765 DOI: 10.1107/S2053230X22004174 |
0.389 |
|
| 2020 |
Beamer LJ. Enzyme dysfunction at atomic resolution: Disease-associated variants of human phosphoglucomutase-1. Biochimie. PMID 32898648 DOI: 10.1016/J.Biochi.2020.08.017 |
0.482 |
|
| 2020 |
Korasick DA, Kandoth PK, Tanner JJ, Mitchum MG, Beamer LJ. Impaired folate binding of serine hydroxymethyltransferase 8 from soybean underlies resistance to the soybean cyst nematode. The Journal of Biological Chemistry. PMID 32014996 DOI: 10.1074/jbc.RA119.012256 |
0.305 |
|
| 2019 |
Zhu JS, Stiers KM, Soleimani E, Groves BR, Beamer LJ, Jakeman DL. Inhibitory Evaluation of αPMM/PGM from : Chemical Synthesis, Enzyme Kinetics, and Protein Crystallographic Study. The Journal of Organic Chemistry. PMID 31264865 DOI: 10.1021/Acs.Joc.9B01305 |
0.516 |
|
| 2019 |
Stiers KM, Graham AC, Zhu JS, Jakeman DL, Nix JC, Beamer LJ. Structural and dynamical description of the enzymatic reaction of a phosphohexomutase. Structural Dynamics (Melville, N.Y.). 6: 024703. PMID 31041362 DOI: 10.1063/1.5092803 |
0.521 |
|
| 2018 |
Stiers KM, Beamer LJ. Assessment and Impacts of Phosphorylation on Protein Flexibility of the α-d-Phosphohexomutases. Methods in Enzymology. 607: 241-267. PMID 30149860 DOI: 10.1016/bs.mie.2018.04.003 |
0.439 |
|
| 2018 |
Stiers KM, Beamer LJ. A Hotspot for Disease-Associated Variants of Human PGM1 Is Associated with Impaired Ligand Binding and Loop Dynamics. Structure (London, England : 1993). PMID 30122451 DOI: 10.1016/j.str.2018.07.005 |
0.382 |
|
| 2017 |
Stiers KM, Xu J, Lee Y, Addison ZR, Van Doren SR, Beamer LJ. Phosphorylation-Dependent Effects on the Structural Flexibility of Phosphoglucosamine Mutase from . Acs Omega. 2: 8445-8452. PMID 31457382 DOI: 10.1021/acsomega.7b01490 |
0.467 |
|
| 2017 |
Muenks AG, Stiers KM, Beamer LJ. Sequence-structure relationships, expression profiles, and disease-associated mutations in the paralogs of phosphoglucomutase 1. Plos One. 12: e0183563. PMID 28837627 DOI: 10.1371/journal.pone.0183563 |
0.372 |
|
| 2017 |
Xu J, Sarma AVS, Wei Y, Beamer LJ, Van Doren SR. Multiple Ligand-Bound States of a Phosphohexomutase Revealed by Principal Component Analysis of NMR Peak Shifts. Scientific Reports. 7: 5343. PMID 28706231 DOI: 10.1038/s41598-017-05557-w |
0.421 |
|
| 2017 |
Stiers KM, Muenks AG, Beamer LJ. Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily. Advances in Protein Chemistry and Structural Biology. 109: 265-304. PMID 28683921 DOI: 10.1016/bs.apcsb.2017.04.005 |
0.433 |
|
| 2017 |
Korasick D, Gamage TT, Christgen S, Stiers KM, Beamer LJ, Henzl MT, Becker DF, Tanner JJ. Structure and characterization of a class 3B proline utilization A: ligand-induced dimerization and importance of the C-terminal domain for catalysis. The Journal of Biological Chemistry. PMID 28420730 DOI: 10.1074/Jbc.M117.786855 |
0.418 |
|
| 2017 |
Stiers KM, Graham AC, Kain BN, Beamer LJ. Asp263 missense variants perturb the active site of human phosphoglucomutase 1 (PGM1). The Febs Journal. PMID 28117557 DOI: 10.1111/febs.14025 |
0.433 |
|
| 2017 |
Lee Y, Furdui C, Beamer LJ. Data on the phosphorylation state of the catalytic serine of enzymes in the α-D-phosphohexomutase superfamily. Data in Brief. 10: 398-405. PMID 28050582 DOI: 10.1016/J.Dib.2016.12.017 |
0.506 |
|
| 2016 |
Stiers KM, Kain BN, Graham AC, Beamer LJ. Induced Structural Disorder as a Molecular Mechanism for Enzyme Dysfunction in Phosphoglucomutase 1 Deficiency. Journal of Molecular Biology. PMID 26972339 DOI: 10.1016/j.jmb.2016.02.032 |
0.41 |
|
| 2015 |
Beamer LJ. Mutations in hereditary phosphoglucomutase 1 deficiency map to key regions of enzyme structure and function. Journal of Inherited Metabolic Disease. 38: 243-56. PMID 25168163 DOI: 10.1007/S10545-014-9757-9 |
0.454 |
|
| 2014 |
Lee Y, Stiers KM, Kain BN, Beamer LJ. Compromised catalysis and potential folding defects in in vitro studies of missense mutants associated with hereditary phosphoglucomutase 1 deficiency. The Journal of Biological Chemistry. 289: 32010-9. PMID 25288802 DOI: 10.1074/Jbc.M114.597914 |
0.432 |
|
| 2014 |
Lee Y, Villar MT, Artigues A, Beamer LJ. Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase. The Journal of Biological Chemistry. 289: 4674-82. PMID 24403075 DOI: 10.1074/Jbc.M113.532226 |
0.57 |
|
| 2014 |
Wei Y, Marcink TC, Xu J, Sirianni AG, Sarma AV, Prior SH, Beamer LJ, Van Doren SR. Chemical shift assignments of domain 4 from the phosphohexomutase from Pseudomonas aeruginosa suggest that freeing perturbs its coevolved domain interface. Biomolecular Nmr Assignments. 8: 329-33. PMID 23893395 DOI: 10.1007/S12104-013-9511-5 |
0.396 |
|
| 2013 |
Hu L, Magesh S, Chen L, Wang L, Lewis TA, Chen Y, Khodier C, Inoyama D, Beamer LJ, Emge TJ, Shen J, Kerrigan JE, Kong AN, Dandapani S, Palmer M, et al. Discovery of a small-molecule inhibitor and cellular probe of Keap1-Nrf2 protein-protein interaction. Bioorganic & Medicinal Chemistry Letters. 23: 3039-43. PMID 23562243 DOI: 10.1016/J.Bmcl.2013.03.013 |
0.333 |
|
| 2013 |
Lee Y, Mehra-Chaudhary R, Furdui C, Beamer LJ. Identification of an essential active-site residue in the α-D-phosphohexomutase enzyme superfamily. The Febs Journal. 280: 2622-32. PMID 23517223 DOI: 10.1111/Febs.12249 |
0.596 |
|
| 2012 |
Luebbering EK, Mick J, Singh RK, Tanner JJ, Mehra-Chaudhary R, Beamer LJ. Conservation of functionally important global motions in an enzyme superfamily across varying quaternary structures. Journal of Molecular Biology. 423: 831-46. PMID 22935436 DOI: 10.1016/J.Jmb.2012.08.013 |
0.504 |
|
| 2012 |
Lee Y, Mick J, Furdui C, Beamer LJ. A coevolutionary residue network at the site of a functionally important conformational change in a phosphohexomutase enzyme family. Plos One. 7: e38114. PMID 22685552 DOI: 10.1371/Journal.Pone.0038114 |
0.495 |
|
| 2012 |
Sarma AV, Anbanandam A, Kelm A, Mehra-Chaudhary R, Wei Y, Qin P, Lee Y, Berjanskii MV, Mick JA, Beamer LJ, Van Doren SR. Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect. Biochemistry. 51: 807-19. PMID 22242625 DOI: 10.1021/Bi201609N |
0.445 |
|
| 2011 |
Mehra-Chaudhary R, Mick J, Tanner JJ, Beamer LJ. Quaternary structure, conformational variability and global motions of phosphoglucosamine mutase. The Febs Journal. 278: 3298-307. PMID 21767345 DOI: 10.1111/J.1742-4658.2011.08246.X |
0.447 |
|
| 2011 |
Mehra-Chaudhary R, Mick J, Beamer LJ. Crystal structure of Bacillus anthracis phosphoglucosamine mutase, an enzyme in the peptidoglycan biosynthetic pathway. Journal of Bacteriology. 193: 4081-7. PMID 21685296 DOI: 10.1128/Jb.00418-11 |
0.592 |
|
| 2011 |
Mehra-Chaudhary R, Mick J, Tanner JJ, Henzl MT, Beamer LJ. Crystal structure of a bacterial phosphoglucomutase, an enzyme involved in the virulence of multiple human pathogens. Proteins. 79: 1215-29. PMID 21246636 DOI: 10.1002/Prot.22957 |
0.587 |
|
| 2010 |
Chuang GY, Mehra-Chaudhary R, Ngan CH, Zerbe BS, Kozakov D, Vajda S, Beamer LJ. Domain motion and interdomain hot spots in a multidomain enzyme. Protein Science : a Publication of the Protein Society. 19: 1662-72. PMID 20589904 DOI: 10.1002/Pro.446 |
0.518 |
|
| 2010 |
Schramm AM, Karr D, Mehra-Chaudhary R, Van Doren SR, Furdui CM, Beamer LJ. Breaking the covalent connection: Chain connectivity and the catalytic reaction of PMM/PGM. Protein Science : a Publication of the Protein Society. 19: 1235-42. PMID 20512975 DOI: 10.1002/Pro.402 |
0.461 |
|
| 2009 |
Mehra-Chaudhary R, Neace CE, Beamer LJ. Crystallization and initial crystallographic analysis of phosphoglucosamine mutase from Bacillus anthracis. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 65: 733-5. PMID 19574653 DOI: 10.1107/S1744309109023409 |
0.555 |
|
| 2008 |
Schramm AM, Mehra-Chaudhary R, Furdui CM, Beamer LJ. Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa. Biochemistry. 47: 9154-62. PMID 18690721 DOI: 10.1021/Bi8005219 |
0.549 |
|
| 2006 |
Lo SC, Li X, Henzl MT, Beamer LJ, Hannink M. Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling. The Embo Journal. 25: 3605-17. PMID 16888629 DOI: 10.1038/Sj.Emboj.7601243 |
0.395 |
|
| 2006 |
Regni C, Shackelford GS, Beamer LJ. Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62: 722-6. PMID 16880541 DOI: 10.1107/S1744309106025887 |
0.775 |
|
| 2006 |
Regni C, Schramm AM, Beamer LJ. The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme. The Journal of Biological Chemistry. 281: 15564-71. PMID 16595672 DOI: 10.1074/Jbc.M600590200 |
0.778 |
|
| 2005 |
Beamer LJ, Li X, Bottoms CA, Hannink M. Conserved solvent and side-chain interactions in the 1.35 Angstrom structure of the Kelch domain of Keap1. Acta Crystallographica. Section D, Biological Crystallography. 61: 1335-42. PMID 16204884 DOI: 10.1107/S0907444905022626 |
0.409 |
|
| 2004 |
Li X, Zhang D, Hannink M, Beamer LJ. Crystallization and initial crystallographic analysis of the Kelch domain from human Keap1. Acta Crystallographica. Section D, Biological Crystallography. 60: 2346-8. PMID 15583386 DOI: 10.1107/S0907444904024825 |
0.406 |
|
| 2004 |
Li X, Zhang D, Hannink M, Beamer LJ. Crystal structure of the Kelch domain of human Keap1. The Journal of Biological Chemistry. 279: 54750-8. PMID 15475350 DOI: 10.1074/Jbc.M410073200 |
0.417 |
|
| 2004 |
Shackelford GS, Regni CA, Beamer LJ. Evolutionary trace analysis of the alpha-D-phosphohexomutase superfamily. Protein Science : a Publication of the Protein Society. 13: 2130-8. PMID 15238632 DOI: 10.1110/Ps.04801104 |
0.776 |
|
| 2004 |
Regni C, Naught L, Tipton PA, Beamer LJ. Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa. Structure (London, England : 1993). 12: 55-63. PMID 14725765 DOI: 10.1016/J.Str.2003.11.015 |
0.79 |
|
| 2004 |
Beamer LJ. Structure of human BPI (bactericidal/permeability-increasing protein) and implications for related proteins. Biochemical Society Transactions. 31: 791-4. PMID 12887307 DOI: 10.1042/Bst0310791 |
0.338 |
|
| 2004 |
Regni C, Tipton PA, Beamer LJ. Structural basis of diverse substrate recognition by PMM/PGM fromP. aeruginosa Acta Crystallographica Section a Foundations of Crystallography. 60: s28-s28. DOI: 10.1107/S0108767304099453 |
0.758 |
|
| 2003 |
Naught LE, Regni C, Beamer LJ, Tipton PA. Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase. Biochemistry. 42: 9946-51. PMID 12924943 DOI: 10.1021/Bi034673G |
0.776 |
|
| 2003 |
Snook CF, Tipton PA, Beamer LJ. Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate biosynthesis in P. aeruginosa. Biochemistry. 42: 4658-68. PMID 12705829 DOI: 10.1021/Bi027328K |
0.618 |
|
| 2002 |
Naught LE, Gilbert S, Imhoff R, Snook C, Beamer L, Tipton P. Allosterism and cooperativity in Pseudomonas aeruginosa GDP-mannose dehydrogenase Biochemistry. 41: 9637-9645. PMID 12135385 DOI: 10.1021/Bi025862M |
0.434 |
|
| 2002 |
Regni C, Tipton PA, Beamer LJ. Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors. Structure (London, England : 1993). 10: 269-79. PMID 11839312 DOI: 10.1016/S0969-2126(02)00705-0 |
0.772 |
|
| 2000 |
Kleiger G, Beamer LJ, Grothe R, Mallick P, Eisenberg D. The 1.7 A crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold. Journal of Molecular Biology. 299: 1019-34. PMID 10843855 DOI: 10.1006/Jmbi.2000.3805 |
0.381 |
|
| 2000 |
Regni CA, Tipton PA, Beamer LJ. Crystallization and initial crystallographic analysis of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa. Acta Crystallographica. Section D, Biological Crystallography. 56: 761-2. PMID 10818357 DOI: 10.1107/S0907444900004431 |
0.756 |
|
| 1999 |
Beamer LJ, Carroll SF, Eisenberg D. The three-dimensional structure of human bactericidal/permeability-increasing protein: implications for understanding protein-lipopolysaccharide interactions. Biochemical Pharmacology. 57: 225-9. PMID 9890549 DOI: 10.1016/S0006-2952(98)00279-2 |
0.355 |
|
| 1998 |
Bruce C, Beamer LJ, Tall AR. The implications of the structure of the bactericidal/permeability-increasing protein on the lipid-transfer function of the cholesteryl ester transfer protein. Current Opinion in Structural Biology. 8: 426-34. PMID 9729732 DOI: 10.1016/S0959-440X(98)80118-8 |
0.339 |
|
| 1998 |
Beamer LJ, Fischer D, Eisenberg D. Detecting distant relatives of mammalian LPS-binding and lipid transport proteins. Protein Science : a Publication of the Protein Society. 7: 1643-6. PMID 9684900 DOI: 10.1002/Pro.5560070721 |
0.34 |
|
| 1998 |
Beamer LJ, Carroll SF, Eisenberg D. The BPI/LBP family of proteins: a structural analysis of conserved regions. Protein Science : a Publication of the Protein Society. 7: 906-14. PMID 9568897 DOI: 10.1002/Pro.5560070408 |
0.43 |
|
| 1997 |
Beamer LJ, Carroll SF, Eisenberg D. Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution. Science (New York, N.Y.). 276: 1861-4. PMID 9188532 DOI: 10.1126/Science.276.5320.1861 |
0.389 |
|
| 1996 |
Vrielink A, Beamer L, Le T, Eisenberg D. Crystallization of the chaperone protein SecB. Protein Science : a Publication of the Protein Society. 4: 1651-3. PMID 8520492 DOI: 10.1002/Pro.5560040824 |
0.322 |
|
| 1996 |
Beamer LJ, Carroll SF, Eisenberg D. Crystal structure of BPI, the human bactericidal/permeability-increasing protein Acta Crystallographica Section a Foundations of Crystallography. 52: C166-C166. DOI: 10.1107/S0108767396092628 |
0.339 |
|
| 1992 |
Beamer LJ, Pabo CO. Refined 1.8 A crystal structure of the lambda repressor-operator complex. Journal of Molecular Biology. 227: 177-96. PMID 1387915 DOI: 10.1016/0022-2836(92)90690-L |
0.389 |
|
| 1991 |
Clarke ND, Beamer LJ, Goldberg HR, Berkower C, Pabo CO. The DNA binding arm of lambda repressor: critical contacts from a flexible region. Science (New York, N.Y.). 254: 267-70. PMID 1833818 DOI: 10.1126/Science.1833818 |
0.393 |
|
| 1990 |
Pabo CO, Aggarwal AK, Jordan SR, Beamer LJ, Obeysekare UR, Harrison SC. Conserved residues make similar contacts in two repressor-operator complexes. Science (New York, N.Y.). 247: 1210-3. PMID 2315694 DOI: 10.1126/Science.2315694 |
0.396 |
|
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