Year |
Citation |
Score |
2020 |
Li Z, Mascarenhas R, Twahir UT, Kallon A, Deb A, Yaw M, Penner-Hahn JE, Koutmos M, Warncke K, Banerjee R. An interprotein Co-S coordination complex in the B12-trafficking pathway. Journal of the American Chemical Society. PMID 32871076 DOI: 10.1021/Jacs.0C06590 |
0.368 |
|
2017 |
Li Z, Shanmuganathan A, Ruetz M, Yamada K, Lesniak NA, Kraeutler B, Brunold TC, Koutmos M, Banerjee R. Coordination Chemistry Controls the Thiol Oxidase Activity of the B12 Trafficking Protein CblC. The Journal of Biological Chemistry. PMID 28442570 DOI: 10.1074/Jbc.M117.788554 |
0.306 |
|
2015 |
Karasik A, Shanmuganathan A, Howard MJ, Fierke CA, Koutmos M. Nuclear Protein-only ribonuclease P 2 Structure and Biochemical Characterization Provide Insight Into the Conserved Properties of tRNA 5'-end Processing Enzymes. Journal of Molecular Biology. PMID 26655022 DOI: 10.1016/J.Jmb.2015.11.025 |
0.312 |
|
2015 |
Yamada K, Gherasim C, Banerjee R, Koutmos M. Structure of Human B12 trafficking protein CblD reveals molecular mimicry and identifies a new subfamily of Nitro-FMN reductases. The Journal of Biological Chemistry. PMID 26364851 DOI: 10.1074/Jbc.M115.682435 |
0.327 |
|
2014 |
Mládková J, Hladílková J, Diamond CE, Tryon K, Yamada K, Garrow TA, Jungwirth P, Koutmos M, Jiráček J. Specific potassium ion interactions facilitate homocysteine binding to betaine-homocysteine S-methyltransferase. Proteins. 82: 2552-64. PMID 24895213 DOI: 10.1002/Prot.24619 |
0.3 |
|
2010 |
Koutmos M, Kabil O, Smith JL, Banerjee R. Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine {beta}-synthase. Proceedings of the National Academy of Sciences of the United States of America. 107: 20958-63. PMID 21081698 DOI: 10.1073/Pnas.1011448107 |
0.318 |
|
2010 |
Hsieh J, Koutmou KS, Rueda D, Koutmos M, Walter NG, Fierke CA. A divalent cation stabilizes the active conformation of the B. subtilis RNase P x pre-tRNA complex: a role for an inner-sphere metal ion in RNase P. Journal of Molecular Biology. 400: 38-51. PMID 20434461 DOI: 10.1016/J.Jmb.2010.04.050 |
0.326 |
|
2009 |
Koutmos M, Datta S, Pattridge KA, Smith JL, Matthews RG. Insights into the reactivation of cobalamin-dependent methionine synthase. Proceedings of the National Academy of Sciences of the United States of America. 106: 18527-32. PMID 19846791 DOI: 10.1073/Pnas.0906132106 |
0.344 |
|
2008 |
Datta S, Koutmos M, Pattridge KA, Ludwig ML, Matthews RG. A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor. Proceedings of the National Academy of Sciences of the United States of America. 105: 4115-20. PMID 18332423 DOI: 10.1073/Pnas.0800329105 |
0.308 |
|
2008 |
Koutmos M, Pejchal R, Bomer TM, Matthews RG, Smith JL, Ludwig ML. Metal active site elasticity linked to activation of homocysteine in methionine synthases. Proceedings of the National Academy of Sciences of the United States of America. 105: 3286-91. PMID 18296644 DOI: 10.1073/Pnas.0709960105 |
0.31 |
|
2008 |
Koutmos M, Georgakaki IP, Tsiolis P, Coucouvanis D. Synthesis and characterization of MoFe3S4 and Mo 2Fe2S4 single cubanes Zeitschrift Fur Anorganische Und Allgemeine Chemie. 634: 255-261. DOI: 10.1002/Zaac.200700419 |
0.623 |
|
2006 |
Xiao Y, Koutmos M, Case DA, Coucouvanis D, Wang H, Cramer SP. Dynamics of an [Fe4S4(SPh)4]2- cluster explored via IR, Raman, and nuclear resonance vibrational spectroscopy (NRVS)-analysis using 36S substitution, DFT calculations, and empirical force fields. Dalton Transactions (Cambridge, England : 2003). 2192-201. PMID 16673033 DOI: 10.1039/B513331A |
0.657 |
|
2006 |
Koutmos M, Georgakaki IP, Coucouvanis D. Borohydride, azide, and chloride anions as terminal ligands on Fe/Mo/S clusters. Synthesis, structure and characterization of [(Cl4-cat)(PPr3) MoFe3S4(X)2]2(Bu4N)4 and [(Cl4-cat)(PPr3)MoFe3S4 (PPr3)(X)]2(Bu4N)2 (X = N3-, BH4-, Cl-) double-fused cubanes. NMR reactivity studies of [(Cl4-cat)(PPr3) MoFe3S4(BH4)2]2(Bu4N)4. Inorganic Chemistry. 45: 3648-56. PMID 16634597 DOI: 10.1021/Ic052156B |
0.68 |
|
2006 |
Koutmos M, Coucouvanis D. Metal clusters as ligands. Substitution of fe ions in Fe/Mo/S clusters by thiophilic CuI ions. Inorganic Chemistry. 45: 1421-3. PMID 16471948 DOI: 10.1021/Ic051860P |
0.694 |
|
2005 |
Smith MC, Xiao Y, Wang H, George SJ, Coucouvanis D, Koutmos M, Sturhahn W, Alp EE, Zhao J, Cramer SP. Normal-mode analysis of FeCl4- and Fe2S2Cl42- via vibrational mössbauer, resonance Raman, and FT-IR spectroscopies. Inorganic Chemistry. 44: 5562-70. PMID 16060605 DOI: 10.1021/Ic0482584 |
0.634 |
|
2005 |
Koutmos M, Kalyvas H, Sanakis Y, Simopoulos A, Coucouvanis D. Systematic synthesis of heterometallic Ni/Fe/S and Cu/Fe/S clusters with a pentlandite-like M8S6 core. Journal of the American Chemical Society. 127: 3706-7. PMID 15771499 DOI: 10.1021/Ja042938O |
0.68 |
|
2005 |
Koutmos M, Coucouvanis D. Metal clusters as ligands: substitution of Fe ions in Fe/Mo/S clusters by thiophilic Cu(I) ions to give clusters with [Cu4Mo2Fe2S8]4+ and [Cu5Mo3Fe4S11]6+ cores. Angewandte Chemie (International Ed. in English). 44: 1971-4. PMID 15724256 DOI: 10.1002/Anie.200462596 |
0.678 |
|
2004 |
Koutmos M, Coucouvanis D. Borohydride anions as terminal ligands on a Fe/Mo/S cluster. Synthesis, structure, and characterization of the [(Cl4-cat)(PPr3)MoFe3S4(BH4)2]2(Bu4N)4 double-fused cubane. Inorganic Chemistry. 43: 6508-10. PMID 15476337 DOI: 10.1021/Ic049275W |
0.705 |
|
2004 |
Koutmos M, Coucouvanis D. Superclusters: a host-guest complex with a cyclic array of three bridged MoFe3S4 clusters. Angewandte Chemie (International Ed. in English). 43: 5023-5. PMID 15384123 DOI: 10.1002/Anie.200460154 |
0.625 |
|
2001 |
Han J, Koutmos M, Ahmad SA, Coucouvanis D. Rational synthesis of high nuclearity Mo/Fe/S clusters: the reductive coupling approach in the convenient synthesis of (Cl(4)-cat)(2)Mo(2)Fe(6)S(8)(PR(3))(6) [R = Et, (n)Pr, (n)Bu] and the new [(Cl(4)-cat)(2)Mo(2)Fe(2)S(3)O(PEt(3))(3)Cl]-1/2(Fe(PEt(3))(2)(MeCN)(4)) and (Cl(4)-cat)(2)Mo(2)Fe(3)S(5)(PEt(3))(5) clusters. Inorganic Chemistry. 40: 5985-99. PMID 11681915 DOI: 10.1021/Ic0104914 |
0.705 |
|
Low-probability matches (unlikely to be authored by this person) |
2008 |
Matthews RG, Koutmos M, Datta S. Cobalamin-dependent and cobamide-dependent methyltransferases. Current Opinion in Structural Biology. 18: 658-66. PMID 19059104 DOI: 10.1016/J.Sbi.2008.11.005 |
0.296 |
|
2013 |
Lofgren M, Koutmos M, Banerjee R. Autoinhibition and signaling by the switch II motif in the G-protein chaperone of a radical B12 enzyme. The Journal of Biological Chemistry. 288: 30980-9. PMID 23996001 DOI: 10.1074/Jbc.M113.499970 |
0.295 |
|
2012 |
Howard MJ, Lim WH, Fierke CA, Koutmos M. Mitochondrial ribonuclease P structure provides insight into the evolution of catalytic strategies for precursor-tRNA 5' processing. Proceedings of the National Academy of Sciences of the United States of America. 109: 16149-54. PMID 22991464 DOI: 10.1073/Pnas.1209062109 |
0.292 |
|
2016 |
Howard MJ, Karasik A, Klemm BP, Mei C, Shanmuganathan A, Fierke CA, Koutmos M. Differential substrate recognition by isozymes of plant protein-only Ribonuclease P. Rna (New York, N.Y.). PMID 26966150 DOI: 10.1261/Rna.055541.115 |
0.291 |
|
2013 |
Lofgren M, Padovani D, Koutmos M, Banerjee R. A switch III motif relays signaling between a B12 enzyme and its G-protein chaperone Nature Chemical Biology. 9: 535-541. PMID 23873214 DOI: 10.1038/Nchembio.1298 |
0.29 |
|
2013 |
Yadav PK, Yamada K, Chiku T, Koutmos M, Banerjee R. Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase. The Journal of Biological Chemistry. 288: 20002-13. PMID 23698001 DOI: 10.1074/Jbc.M113.466177 |
0.287 |
|
2017 |
Ruetz M, Shanmuganathan A, Gherasim C, Karasik A, Salchner R, Kieninger C, Wurst K, Banerjee R, Koutmos M, Kräutler B. Antivitamin B12 Inhibition of the Human B12 -Processing Enzyme CblC: Crystal Structure of an Inactive Ternary Complex with Glutathione as the Cosubstrate. Angewandte Chemie (International Ed. in English). PMID 28544088 DOI: 10.1002/Anie.201701583 |
0.286 |
|
2017 |
Klemm BP, Karasik A, Kaitany KJ, Shanmuganathan A, Henley MJ, Thelen AZ, Dewar AJ, Jackson ND, Koutmos M, Fierke CA. Molecular recognition of pre-tRNA by Arabidopsis protein-only Ribonuclease P. Rna (New York, N.Y.). PMID 28874505 DOI: 10.1261/Rna.061457.117 |
0.286 |
|
2019 |
Ruetz M, Campanello GC, Purchal M, Shen H, McDevitt L, Gouda H, Wakabayashi S, Zhu J, Rubin EJ, Warncke K, Mootha VK, Koutmos M, Banerjee R. Itaconyl-CoA forms a stable biradical in methylmalonyl-CoA mutase and derails its activity and repair. Science (New York, N.Y.). 366: 589-593. PMID 31672889 DOI: 10.1126/Science.Aay0934 |
0.285 |
|
2011 |
Koutmos M, Gherasim C, Smith JL, Banerjee R. Structural basis of multifunctionality in a vitamin B12-processing enzyme. The Journal of Biological Chemistry. 286: 29780-7. PMID 21697092 DOI: 10.1074/Jbc.M111.261370 |
0.281 |
|
2013 |
Howard MJ, Liu X, Lim WH, Klemm BP, Fierke CA, Koutmos M, Engelke DR. RNase P enzymes: divergent scaffolds for a conserved biological reaction. Rna Biology. 10: 909-14. PMID 23595059 DOI: 10.4161/Rna.24513 |
0.28 |
|
2009 |
Vanek V, Budesínský M, Kabeleová P, Sanda M, Kozísek M, Hanclová I, Mládková J, Brynda J, Rosenberg I, Koutmos M, Garrow TA, Jirácek J. Structure-activity study of new inhibitors of human betaine-homocysteine S-methyltransferase. Journal of Medicinal Chemistry. 52: 3652-65. PMID 19534555 DOI: 10.1021/Jm8015798 |
0.279 |
|
2018 |
Yamada K, Koutmos M. The folate-binding module of Thermus thermophilus cobalamin-dependent methionine synthase displays a distinct variation of the classical TIM barrel: a TIM barrel with a `twist'. Acta Crystallographica. Section D, Structural Biology. 74: 41-51. PMID 29372898 DOI: 10.1107/S2059798317018290 |
0.273 |
|
2008 |
Szegedi SS, Castro CC, Koutmos M, Garrow TA. Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-homocysteine methyltransferase. The Journal of Biological Chemistry. 283: 8939-45. PMID 18230605 DOI: 10.1074/Jbc.M710449200 |
0.257 |
|
2019 |
Karasik A, Fierke CA, Koutmos M. Interplay between substrate recognition, 5' end tRNA processing and methylation activity of human mitochondrial RNase P. Rna (New York, N.Y.). PMID 31455609 DOI: 10.1261/Rna.069310.118 |
0.248 |
|
2011 |
Koutmos M, Kabil O, Smith JL, Banerjee R. Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine β-synthase (Proceedings of the National Academy of Sciences of the United States of America (2010) 107, 49 (20958-20963) DOI: 10.1073/pnas.1011448107) Proceedings of the National Academy of Sciences of the United States of America. 108: 4512. DOI: 10.1073/Pnas.1102185108 |
0.234 |
|
2013 |
Ganu R, Garrow T, Koutmos M, Rund L, Schook LB. Splicing variants of the porcine betaine-homocysteine S-methyltransferase gene: implications for mammalian metabolism. Gene. 529: 228-37. PMID 23948084 DOI: 10.1016/J.Gene.2013.07.103 |
0.234 |
|
2015 |
Ganu RS, Ishida Y, Koutmos M, Kolokotronis SO, Roca AL, Garrow TA, Schook LB. Evolutionary Analyses and Natural Selection of Betaine-Homocysteine S-Methyltransferase (BHMT) and BHMT2 Genes. Plos One. 10: e0134084. PMID 26213999 DOI: 10.1371/Journal.Pone.0134084 |
0.229 |
|
2016 |
Sen A, Karasik A, Shanmuganathan A, Mirkovic E, Koutmos M, Cox RT. Loss of the mitochondrial protein-only ribonuclease P complex causes aberrant tRNA processing and lethality in Drosophila. Nucleic Acids Research. PMID 27131785 DOI: 10.1093/Nar/Gkw338 |
0.226 |
|
2017 |
Ruetz M, Shanmuganathan A, Gherasim C, Karasik A, Salchner R, Kieninger C, Wurst K, Banerjee R, Koutmos M, Kräutler B. Inhibierung des humanen B12-verarbeitenden Enzyms CblC durch Antivitamine B12- Kristallstruktur des inaktiven ternären Komplexes mit dem Kosubstrat Glutathion Angewandte Chemie. 129: 7493-7498. DOI: 10.1002/Ange.201701583 |
0.22 |
|
2020 |
Mascarenhas R, Ruetz M, McDevitt L, Koutmos M, Banerjee R. Mobile loop dynamics in adenosyltransferase control binding and reactivity of coenzyme B. Proceedings of the National Academy of Sciences of the United States of America. PMID 33199623 DOI: 10.1073/pnas.2007332117 |
0.2 |
|
2022 |
Yamada K, Mendoza J, Koutmos M. 5-Formyltetrahydrofolate promotes conformational remodeling in a methylenetetrahydrofolate reductase active site and inhibits its activity. The Journal of Biological Chemistry. 299: 102855. PMID 36592927 DOI: 10.1016/j.jbc.2022.102855 |
0.196 |
|
2022 |
Wu Meyers N, Karasik A, Kaitany K, Fierke CA, Koutmos M. Gambogic acid and juglone inhibit RNase P through distinct mechanisms. The Journal of Biological Chemistry. 102683. PMID 36370850 DOI: 10.1016/j.jbc.2022.102683 |
0.167 |
|
2023 |
Wilhelm CA, Mallik L, Kelly AL, Brotzman S, Mendoza J, Anders AG, Leskaj S, Castillo C, Ruotolo BT, Cianfrocco MA, Koutmos M. Bacterial RNA-free RNase P: structural and functional characterization of multiple oligomeric forms of a minimal protein-only ribonuclease P. The Journal of Biological Chemistry. 105327. PMID 37806495 DOI: 10.1016/j.jbc.2023.105327 |
0.162 |
|
2021 |
Gouda H, Mascarenhas R, Pillay S, Ruetz M, Koutmos M, Banerjee R. Patient mutations in human ATP:cob(I)alamin adenosyltransferase differentially affect its catalytic versus chaperone functions. The Journal of Biological Chemistry. 101373. PMID 34757128 DOI: 10.1016/j.jbc.2021.101373 |
0.146 |
|
2020 |
Lukowski AL, Mallik L, Hinze ME, Carlson BM, Ellinwood DC, Pyser JB, Koutmos M, Narayan ARH. Substrate Promiscuity of a Paralytic Shellfish Toxin Amidinotransferase. Acs Chemical Biology. PMID 32058687 DOI: 10.1021/acschembio.9b00964 |
0.144 |
|
2023 |
Mendoza J, Purchal M, Yamada K, Koutmos M. Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured in crystallo. Nature Communications. 14: 6365. PMID 37821448 DOI: 10.1038/s41467-023-42037-4 |
0.14 |
|
2022 |
Purchal MK, Eyler DE, Tardu M, Franco MK, Korn MM, Khan T, McNassor R, Giles R, Lev K, Sharma H, Monroe J, Mallik L, Koutmos M, Koutmou KS. Pseudouridine synthase 7 is an opportunistic enzyme that binds and modifies substrates with diverse sequences and structures. Proceedings of the National Academy of Sciences of the United States of America. 119. PMID 35058356 DOI: 10.1073/pnas.2109708119 |
0.127 |
|
2024 |
Wilhelm CA, Kaitany K, Kelly A, Yacoub M, Koutmos M. The protein-only RNase Ps, endonucleases that cleave pre-tRNA: Biological relevance, molecular architectures, substrate recognition and specificity, and protein interactomes. Wiley Interdisciplinary Reviews. Rna. 15: e1836. PMID 38453211 DOI: 10.1002/wrna.1836 |
0.12 |
|
2022 |
Ruetz M, Koutmos M, Kräutler B. Antivitamins B: Synthesis and application as inhibitory ligand of the B-tailoring enzyme CblC. Methods in Enzymology. 668: 157-178. PMID 35589193 DOI: 10.1016/bs.mie.2021.12.016 |
0.118 |
|
2020 |
Karasik A, Wilhelm CA, Fierke CA, Koutmos M. Disease-associated mutations in mitochondrial precursor tRNAs affect binding, m1R9 methylation and tRNA processing by mtRNase P. Rna (New York, N.Y.). PMID 33380464 DOI: 10.1261/rna.077198.120 |
0.105 |
|
2020 |
Miller NA, Kaneshiro AK, Konar A, Alonso-Mori R, Britz A, Deb A, Glownia JM, Koralek JD, Mallik L, Meadows JH, Michocki LB, van Driel TB, Koutmos M, Padmanabhan S, Elías-Arnanz M, et al. The Photoactive Excited State of the B-Based Photoreceptor CarH. The Journal of Physical Chemistry. B. PMID 33174757 DOI: 10.1021/acs.jpcb.0c09428 |
0.102 |
|
2024 |
Tidwell ED, Kilde IR, Leskaj S, Koutmos M. Fluorescent Ligand Equilibrium Displacement: A High-Throughput Method for Identification of FMN Riboswitch-Binding Small Molecules. International Journal of Molecular Sciences. 25. PMID 38255809 DOI: 10.3390/ijms25020735 |
0.095 |
|
2024 |
Anders AG, Tidwell ED, Gadkari VV, Koutmos M, Ruotolo BT. Collision-Induced Unfolding Reveals Disease-Associated Stability Shifts in Mitochondrial Transfer Ribonucleic Acids. Journal of the American Chemical Society. 146: 4412-4420. PMID 38329282 DOI: 10.1021/jacs.3c09230 |
0.093 |
|
2005 |
Demadis KD, Katarachia SD, Koutmos M. Crystal growth and characterization of zinc-(amino-tris- (methylenephosphonate)) organic-inorganic hybrid networks and their inhibiting effect on metallic corrosion Inorganic Chemistry Communications. 8: 254-258. DOI: 10.1016/j.inoche.2004.12.019 |
0.062 |
|
2023 |
DeAngelo SL, Győrffy B, Koutmos M, Shah YM. Selenoproteins and tRNA-Sec: regulators of cancer redox homeostasis. Trends in Cancer. PMID 37716885 DOI: 10.1016/j.trecan.2023.08.003 |
0.061 |
|
Hide low-probability matches. |