| Year |
Citation |
Score |
| 2023 |
Martinez Grundman JE, Johnson EA, Lecomte JTJ. Architectural digest: Thermodynamic stability and domain structure of a consensus monomeric globin. Biophysical Journal. PMID 37353934 DOI: 10.1016/j.bpj.2023.06.016 |
0.389 |
|
| 2021 |
Julió Plana L, Martinez Grundman JE, Estrin DA, Lecomte JTJ, Capece L. Distal lysine (de)coordination in the algal hemoglobin THB1: A combined computer simulation and experimental study. Journal of Inorganic Biochemistry. 220: 111455. PMID 33882423 DOI: 10.1016/j.jinorgbio.2021.111455 |
0.376 |
|
| 2019 |
Nye DB, Johnson EA, Mai MH, Lecomte JTJ. Replacement of the heme axial lysine as a test of conformational adaptability in the truncated hemoglobin THB1. Journal of Inorganic Biochemistry. 201: 110824. PMID 31514090 DOI: 10.1016/j.jinorgbio.2019.110824 |
0.375 |
|
| 2018 |
Nye D, Preimesberger M, Majumdar A, Lecomte J. A Histidine-Lysine Axial Ligand Switch in a Hemoglobin Biophysical Journal. 114: 405a. DOI: 10.1016/J.Bpj.2017.11.2246 |
0.323 |
|
| 2017 |
Nye DB, Preimesberger MR, Majumdar A, Lecomte JTJ. Histidine-Lysine Axial Ligand Switching in a Hemoglobin: A Role for Heme Propionates. Biochemistry. PMID 29271191 DOI: 10.1021/acs.biochem.7b01155 |
0.371 |
|
| 2016 |
Preimesberger MR, Majumdar A, Lecomte JT. The dynamics of lysine as a heme axial ligand: NMR analysis of the Chlamydomonas reinhardtii hemoglobin THB1. Biochemistry. PMID 28032976 DOI: 10.1021/acs.biochem.6b00926 |
0.367 |
|
| 2015 |
Rice SL, Boucher LE, Schlessman JL, Preimesberger MR, Bosch J, Lecomte JT. Structure of Chlamydomonas reinhardtii THB1, a group 1 truncated hemoglobin with a rare histidine-lysine heme ligation. Acta Crystallographica. Section F, Structural Biology Communications. 71: 718-25. PMID 26057801 DOI: 10.1107/S2053230X15006949 |
0.371 |
|
| 2015 |
Nye D, Preimesberger M, Kougentakis C, Rice S, Lecomte J. Heme Coordination Versatility in a Truncated Hemoglobin Biophysical Journal. 108: 213a. DOI: 10.1016/J.Bpj.2014.11.1177 |
0.474 |
|
| 2014 |
Rice SL, Preimesberger MR, Johnson EA, Lecomte JT. Introduction of a covalent histidine-heme linkage in a hemoglobin: a promising tool for heme protein engineering. Journal of Inorganic Biochemistry. 141: 198-207. PMID 25304367 DOI: 10.1016/j.jinorgbio.2014.09.009 |
0.388 |
|
| 2014 |
Johnson EA, Rice SL, Preimesberger MR, Nye DB, Gilevicius L, Wenke BB, Brown JM, Witman GB, Lecomte JT. Characterization of THB1, a Chlamydomonas reinhardtii truncated hemoglobin: linkage to nitrogen metabolism and identification of lysine as the distal heme ligand. Biochemistry. 53: 4573-89. PMID 24964018 DOI: 10.1021/bi5005206 |
0.345 |
|
| 2014 |
Wenke BB, Lecomte JT, Héroux A, Schlessman JL. The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: comparison of X-ray and NMR structures. Proteins. 82: 528-34. PMID 23999883 DOI: 10.1002/prot.24409 |
0.334 |
|
| 2013 |
Dellarole M, Roumestand C, Royer C, Lecomte JT. Volumetric properties underlying ligand binding in a monomeric hemoglobin: a high-pressure NMR study. Biochimica Et Biophysica Acta. 1834: 1910-22. PMID 23619242 DOI: 10.1016/J.Bbapap.2013.04.016 |
0.355 |
|
| 2013 |
Preimesberger MR, Wenke BB, Gilevicius L, Pond MP, Lecomte JT. Facile heme vinyl posttranslational modification in a hemoglobin. Biochemistry. 52: 3478-88. PMID 23607716 DOI: 10.1021/Bi400289E |
0.78 |
|
| 2012 |
Pond MP, Wenke BB, Preimesberger MR, Rice SL, Lecomte JT. 3-Fluorotyrosine as a complementary probe of hemoglobin structure and dynamics: a (19)F-NMR study of Synechococcus sp. PCC 7002 GlbN. Chemistry & Biodiversity. 9: 1703-17. PMID 22976963 DOI: 10.1002/Cbdv.201100448 |
0.778 |
|
| 2012 |
Pond MP, Majumdar A, Lecomte JT. Influence of heme post-translational modification and distal ligation on the backbone dynamics of a monomeric hemoglobin. Biochemistry. 51: 5733-47. PMID 22775272 DOI: 10.1021/Bi300624A |
0.772 |
|
| 2012 |
Preimesberger MR, Pond MP, Majumdar A, Lecomte JT. Electron self-exchange and self-amplified posttranslational modification in the hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 17: 599-609. PMID 22349976 DOI: 10.1007/S00775-012-0880-5 |
0.768 |
|
| 2012 |
Lecomte J, Pond M, Majumdar A. Backbone dynamics of the truncated (2/2) hemoglobin from Synechococcus sp. PCC 7002 (ferric form with heme PTM, cyanide complex) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr18423 |
0.76 |
|
| 2012 |
Lecomte J, Pond M, Majumdar A. Backbone dynamics of the truncated (2/2) hemoglobin from Synechococcus sp. PCC 7002 (ferrous form with heme PTM, carbonmonoxy complex) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr18422 |
0.759 |
|
| 2012 |
Lecomte J, Preimesberger M, Pond M, Majumdar A. Partial backbone 1H assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferrous bis-histidine state Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17947 |
0.752 |
|
| 2011 |
Nothnagel HJ, Winer BY, Vuletich DA, Pond MP, Lecomte JTJ. Structural properties of 2/2 hemoglobins: The group III protein from Helicobacter hepaticus Iubmb Life. 63: 197-205. PMID 21445851 DOI: 10.1002/Iub.430 |
0.764 |
|
| 2011 |
Nothnagel HJ, Preimesberger MR, Pond MP, Winer BY, Adney EM, Lecomte JTJ. Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: Covalent heme attachment and bishistidine coordination Journal of Biological Inorganic Chemistry. 16: 539-552. PMID 21240532 DOI: 10.1007/S00775-011-0754-2 |
0.78 |
|
| 2011 |
Preimesberger MR, Nothnagel HJ, Adney EM, Pond MP, Winer BY, Lecomte JT. Proposed Mechanism for Reductively Driven Hybrid b/c Heme Formation in Synechocystis and Synechococcus Hemoglobins Biophysical Journal. 100: 222a. DOI: 10.1016/J.Bpj.2010.12.1425 |
0.777 |
|
| 2011 |
Pond MP, Vuletich DA, Majumdar A, Falzone CJ, Lecomte JT. The Influence of the Heme Sixth Ligand on the Backbone Dynamics of an Endogenously Hexacoordinate Hemoglobin Biophysical Journal. 100: 220a-221a. DOI: 10.1016/J.Bpj.2010.12.1417 |
0.792 |
|
| 2010 |
Scott NL, Xu Y, Shen G, Vuletich DA, Falzone CJ, Li Z, Ludwig M, Pond MP, Preimesberger MR, Bryant DA, Lecomte JT. Functional and structural characterization of the 2/2 hemoglobin from Synechococcus sp. PCC 7002. Biochemistry. 49: 7000-11. PMID 20669934 DOI: 10.1021/Bi100463D |
0.74 |
|
| 2009 |
Pond MP, Vuletich DA, Falzone CJ, Majumdar A, Lecomte JT. (1)H, (15)N, and (13)C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state. Biomolecular Nmr Assignments. 3: 211-4. PMID 19888693 DOI: 10.1007/S12104-009-9177-1 |
0.764 |
|
| 2009 |
Nothnagel HJ, Love N, Lecomte JTJ. The role of the heme distal ligand in the post-translational modification of Synechocystis hemoglobin Journal of Inorganic Biochemistry. 103: 107-116. PMID 18992944 DOI: 10.1016/J.Jinorgbio.2008.09.009 |
0.808 |
|
| 2008 |
Davis RB, Lecomte JT. Structural propensities in the heme binding region of apocytochrome b5. II. Heme conjugates. Biopolymers. 90: 556-66. PMID 18398854 DOI: 10.1002/bip.20995 |
0.314 |
|
| 2008 |
Lecomte JT, Mukhopadhyay K, Pond MP. Structural and thermodynamic encoding in the sequence of rat microsomal cytochrome b(5). Biopolymers. 89: 428-42. PMID 18041061 DOI: 10.1002/Bip.20892 |
0.751 |
|
| 2007 |
Landfried DA, Vuletich DA, Pond MP, Lecomte JT. Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins. Gene. 398: 12-28. PMID 17550789 DOI: 10.1016/J.Gene.2007.02.046 |
0.699 |
|
| 2007 |
Knappenberger JA, Lecomte JT. Loop anchor modification causes the population of an alternative native state in an SH3-like domain. Protein Science : a Publication of the Protein Society. 16: 863-79. PMID 17456740 DOI: 10.1110/Ps.062469507 |
0.323 |
|
| 2006 |
Vuletich DA, Falzone CJ, Lecomte JT. Structural and dynamic repercussions of heme binding and heme-protein cross-linking in Synechococcus sp. PCC 7002 hemoglobin. Biochemistry. 45: 14075-84. PMID 17115702 DOI: 10.1021/bi061532g |
0.412 |
|
| 2006 |
Knappenberger JA, Kuriakose SA, Christie Vu B, Nothnagel HJ, Vuletich DA, Lecomte JTJ. Proximal influences in two-on-two globins: Effect of the Ala69Ser replacement on Synechocystis sp. PCC 6803 hemoglobin Biochemistry. 45: 11401-11413. PMID 16981700 DOI: 10.1021/Bi060691X |
0.806 |
|
| 2005 |
Lecomte JT, Vu BC, Falzone CJ. Structural and dynamic properties of Synechocystis sp. PCC 6803 Hb revealed by reconstitution with Zn-protoporphyrin IX. Journal of Inorganic Biochemistry. 99: 1585-92. PMID 15961161 DOI: 10.1016/j.jinorgbio.2005.04.018 |
0.422 |
|
| 2005 |
Bevilacqua PC, Brown TS, Chadalavada D, Lecomte J, Moody E, Nakano SI. Linkage between proton binding and folding in RNA: implications for RNA catalysis. Biochemical Society Transactions. 33: 466-70. PMID 15916542 DOI: 10.1042/Bst0330466 |
0.323 |
|
| 2004 |
Knappenberger JA, Kraemer-Pecore CM, Lecomte JT. Insertion of the cytochrome b5 heme-binding loop into an SH3 domain. Effects on structure and stability, and clues about the cytochrome's architecture. Protein Science : a Publication of the Protein Society. 13: 2899-908. PMID 15459337 DOI: 10.1110/Ps.04902704 |
0.381 |
|
| 2004 |
Vu BC, Nothnagel HJ, Vuletich DA, Falzone CJ, Lecomte JTJ. Cyanide binding to hexacoordinate cyanobacterial hemoglobins: Hydrogen-bonding network and heme pocket rearrangement in ferric H117A Synechocystis hemoglobin Biochemistry. 43: 12622-12633. PMID 15449952 DOI: 10.1021/Bi048726L |
0.812 |
|
| 2004 |
Mukhopadhyay K, Lecomte JT. A relationship between heme binding and protein stability in cytochrome b5. Biochemistry. 43: 12227-36. PMID 15379561 DOI: 10.1021/bi0488956 |
0.347 |
|
| 2004 |
Lecomte JT, Vuletich DA, Vu BC, Kuriakose SA, Scott NL, Falzone CJ. Structural properties of cyanobacterial hemoglobins: the unusual heme-protein cross-link of Synechocystis sp. PCC 6803 Hb and Synechococcus sp. PCC 7002 Hb. Micron (Oxford, England : 1993). 35: 71-2. PMID 15036295 DOI: 10.1016/j.micron.2003.10.020 |
0.385 |
|
| 2004 |
Vu BC, Vuletich DA, Kuriakose SA, Falzone CJ, Lecomte JT. Characterization of the heme-histidine cross-link in cyanobacterial hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 183-94. PMID 14727166 DOI: 10.1007/s00775-003-0512-1 |
0.504 |
|
| 2002 |
Falzone CJ, Christie Vu B, Scott NL, Lecomte JT. The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state. Journal of Molecular Biology. 324: 1015-29. PMID 12470956 DOI: 10.1016/S0022-2836(02)01093-8 |
0.434 |
|
| 2002 |
Vu BC, Jones AD, Lecomte JT. Novel histidine-heme covalent linkage in a hemoglobin. Journal of the American Chemical Society. 124: 8544-5. PMID 12121092 DOI: 10.1021/Ja026569C |
0.383 |
|
| 2002 |
Scott NL, Falzone CJ, Vuletich DA, Zhao J, Bryant DA, Lecomte JT. Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein. Biochemistry. 41: 6902-10. PMID 12033922 DOI: 10.1021/Bi025609M |
0.396 |
|
| 2001 |
Lecomte JTJ, Scott NL, Christie Vu B, Falzone CJ. Binding of ferric heme by the recombinant globin from the cyanobacterium Synechocystis sp. PCC 6803 Biochemistry. 40: 6541-6552. PMID 11371218 DOI: 10.1021/bi010226u |
0.423 |
|
| 2001 |
Falzone CJ, Wang Y, Vu BC, Scott NL, Bhattacharya S, Lecomte JTJ. Structural and dynamic perturbations induced by heme binding in cytochrome b5 Biochemistry. 40: 4879-4891. PMID 11294656 DOI: 10.1021/bi002681g |
0.438 |
|
| 2000 |
Scott NL, Lecomte JTJ. Cloning, expression, purification, and preliminary characterization of a putative hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 Protein Science. 9: 587-597. PMID 10752621 DOI: 10.1110/PS.9.3.587 |
0.443 |
|
| 1999 |
Lecomte JT, Sukits SF, Bhattacharya S, Falzone CJ. Conformational properties of native sperm whale apomyoglobin in solution. Protein Science : a Publication of the Protein Society. 8: 1484-91. PMID 10422837 DOI: 10.1110/ps.8.7.1484 |
0.357 |
|
| 1994 |
Cocco MJ, Lecomte JTJ. The native state of apomyoglobin described by proton NMR spectroscopy: Interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANS Protein Science. 3: 267-281. PMID 8003963 DOI: 10.1002/Pro.5560030211 |
0.346 |
|
| 1993 |
Moore CD, Lecomte JT. Characterization of an independent structural unit in apocytochrome b5. Biochemistry. 32: 199-207. PMID 8418838 DOI: 10.1021/bi00052a026 |
0.387 |
|
| 1992 |
Cocco MJ, Kao YH, Phillips AT, Lecomte JTJ. Structural comparison of apomyoglobin and metaquomyoglobin: pH titration of histidines by NMR spectroscopy Biochemistry. 31: 6481-6491. PMID 1633160 DOI: 10.1021/Bi00143A018 |
0.321 |
|
| 1991 |
Moore CD, al-Misky ON, Lecomte JT. Similarities in structure between holocytochrome b5 and apocytochrome b5: NMR studies of the histidine residues. Biochemistry. 30: 8357-65. PMID 1883823 DOI: 10.1021/bi00098a012 |
0.395 |
|
| 1990 |
Moore CD, Lecomte JT. Structural properties of apocytochrome b5: presence of a stable native core. Biochemistry. 29: 1984-9. PMID 2328231 DOI: 10.1021/bi00460a004 |
0.315 |
|
| 1990 |
Cocco MJ, Lecomte JTJ. Characterization of hydrophobic cores in apomyoglobin: A proton NMR spectroscopy study Biochemistry. 29: 11067-11072. PMID 2176892 DOI: 10.1021/Bi00502A008 |
0.312 |
|
| 1990 |
Lecomte JTJ, Cocco MJ. Structural features of the protoporphyrin-apomyoglobin complex: A proton NMR spectroscopy study Biochemistry. 29: 11057-11067. PMID 2176891 DOI: 10.1021/Bi00502A007 |
0.382 |
|
| 1989 |
Lecomte JT, Smit JD, Winterhalter KH, La Mar GN. Structural and electronic properties of the liver fluke heme cavity by nuclear magnetic resonance and optical spectroscopy. Evidence for a distal tyrosine residue in a normally functioning hemoglobin. Journal of Molecular Biology. 209: 235-47. PMID 2555518 DOI: 10.1016/0022-2836(89)90275-1 |
0.334 |
|
| 1988 |
LECOMTE JTJ, LA MAR GN. ChemInform Abstract: 1H NMR Probe for Hydrogen Bonding of Distal Residues to Bound Ligands in Heme Proteins: Isotope Effect on Heme Electronic Structure of Myoglobin. Cheminform. 19. DOI: 10.1002/chin.198810361 |
0.343 |
|
| 1987 |
Lecomte JTJ, Kaplan D, Llinás M, Thunberg E, Samuelsson G. Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin Biochemistry. 26: 1187-1194. PMID 3567163 DOI: 10.1021/Bi00378A029 |
0.353 |
|
| 1987 |
Lecomte JTJ, La Mar GN. Proton NMR probe for hydrogen bonding of distal residues to bound ligands in heme proteins: isotope effect on heme electronic structure of myoglobin Journal of the American Chemical Society. 109: 7219-7220. DOI: 10.1021/ja00257a068 |
0.33 |
|
| 1986 |
Mar GL, Emerson S, Lecomte J, Pande U, Smith K, Craig G, Kehres L. Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements Journal of Back and Musculoskeletal Rehabilitation. 108: 5568-5573. DOI: 10.13018/Bmr2434 |
0.336 |
|
| 1985 |
Lecomte JTJ, La Mar GN. 1H NMR study of labile proton exchange in the heme cavity as a probe for the potential ligand entry channel in myoglobin Biochemistry. 24: 7388-7395. PMID 4084588 |
0.337 |
|
| 1985 |
Lecomte JT, Johnson RD, La Mar GN. Characterization of heme orientational disorder in myoglobin by proton nuclear Overhauser effects. Biochimica Et Biophysica Acta. 829: 268-74. PMID 2986702 DOI: 10.1016/0167-4838(85)90197-9 |
0.309 |
|
| 1984 |
Lecomte J, La Mar GN, Winterhalter KH, Smit JDG. Proton nuclear magnetic resonance investigation of the heme cavity structure of liver fluke (Dirocoelium dendriticum) methemoglobin Journal of Molecular Biology. 180: 357-370. PMID 6096565 DOI: 10.1016/S0022-2836(84)80008-X |
0.405 |
|
| 1982 |
Lecomte JTJ, Jones BL, Llinás M. Proton magnetic resonance studies of barley and wheat thionins: Structural homology with crambin Biochemistry. 21: 4843-4849. PMID 6291592 DOI: 10.1021/Bi00263A003 |
0.338 |
|
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