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T. Martin Schmeing - Publications

Affiliations: 
Biochemistry McGill University, Montreal, QC, Canada 
Website:
https://www.mcgill.ca/biochemistry/about-us/department/faculty-members/schmeing
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82 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
2023 Markus LMD, Sharon I, Munro K, Grogg M, Hilvert D, Strauss M, Schmeing TM. Structure and function of a hexameric cyanophycin synthetase 2. Protein Science : a Publication of the Protein Society. e4685. PMID 37222490 DOI: 10.1002/pro.4685  0.367
2022 Sharon I, Grogg M, Hilvert D, Schmeing TM. Structure and Function of the β-Asp-Arg Polymerase Cyanophycin Synthetase 2. Acs Chemical Biology. PMID 35179888 DOI: 10.1021/acschembio.1c01007  0.333
2022 Fortinez CM, Bloudoff K, Harrigan C, Sharon I, Strauss M, Schmeing TM. Structures and function of a tailoring oxidase in complex with a nonribosomal peptide synthetase module. Nature Communications. 13: 548. PMID 35087027 DOI: 10.1038/s41467-022-28221-y  0.368
2021 Sharon I, Haque AS, Grogg M, Lahiri I, Seebach D, Leschziner AE, Hilvert D, Schmeing TM. Structures and function of the amino acid polymerase cyanophycin synthetase. Nature Chemical Biology. PMID 34385683 DOI: 10.1038/s41589-021-00854-y  0.672
2020 Robert F, Cencic R, Cai R, Schmeing TM, Pelletier J. RNA-tethering assay and eIF4G:eIF4A obligate dimer design uncovers multiple eIF4F functional complexes. Nucleic Acids Research. PMID 32749456 DOI: 10.1093/Nar/Gkaa646  0.447
2020 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility. Science (New York, N.Y.). 366. PMID 31699907 DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2019 Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility Science. 366: eaaw4388. DOI: 10.1126/science.aaw4388  0.325
2018 Reimer JM, Haque AS, Tarry MJ, Schmeing TM. Piecing together nonribosomal peptide synthesis. Current Opinion in Structural Biology. 49: 104-113. PMID 29444491 DOI: 10.1016/J.Sbi.2018.01.011  0.433
2017 Bloudoff K, Schmeing TM. Structural and functional aspects of the nonribosomal peptide synthetase condensation domain superfamily: discovery, dissection and diversity. Biochimica Et Biophysica Acta. PMID 28526268 DOI: 10.1016/J.Bbapap.2017.05.010  0.353
2017 Tarry MJ, Haque AS, Bui KH, Schmeing TM. X-Ray Crystallography and Electron Microscopy of Cross- and Multi-Module Nonribosomal Peptide Synthetase Proteins Reveal a Flexible Architecture. Structure (London, England : 1993). PMID 28434915 DOI: 10.1016/J.Str.2017.03.014  0.396
2016 Bloudoff K, Fage CD, Marahiel MA, Schmeing TM. Structural and mutational analysis of the nonribosomal peptide synthetase heterocyclization domain provides insight into catalysis. Proceedings of the National Academy of Sciences of the United States of America. PMID 27994138 DOI: 10.1073/Pnas.1614191114  0.448
2016 Schmeing TM. Visualizing A Natural Antibiotic Nanofactory. Clinical and Investigative Medicine. Medecine Clinique Et Experimentale. 39: E220-E226. PMID 27917781 DOI: 10.25011/Cim.V39I6.27490  0.378
2016 Bloudoff K, Alonzo DA, Schmeing TM. Chemical Probes Allow Structural Insight into the Condensation Reaction of Nonribosomal Peptide Synthetases. Cell Chemical Biology. 23: 331-9. PMID 26991102 DOI: 10.1016/J.Chembiol.2016.02.012  0.447
2016 Alonzo DA, Schmeing TM. Translation: Ribosomes make sweeping arrests. Nature Chemical Biology. 12: 127-8. PMID 26881763 DOI: 10.1038/Nchembio.2027  0.359
2016 Reimer JM, Aloise MN, Harrison PM, Schmeing TM. Synthetic cycle of the initiation module of a formylating nonribosomal peptide synthetase. Nature. 529: 239-42. PMID 26762462 DOI: 10.1038/Nature16503  0.452
2015 Alonzo DA, Magarvey NA, Schmeing TM. Characterization of cereulide synthetase, a toxin-producing macromolecular machine. Plos One. 10: e0128569. PMID 26042597 DOI: 10.1371/Journal.Pone.0128569  0.399
2015 Tarry MJ, Schmeing TM. Specific disulfide cross-linking to constrict the mobile carrier domain of nonribosomal peptide synthetases. Protein Engineering, Design & Selection : Peds. 28: 163-70. PMID 25713404 DOI: 10.1093/Protein/Gzv009  0.395
2014 Cencic R, Miura H, Malina A, Robert F, Ethier S, Schmeing TM, Dostie J, Pelletier J. Protospacer adjacent motif (PAM)-distal sequences engage CRISPR Cas9 DNA target cleavage. Plos One. 9: e109213. PMID 25275497 DOI: 10.1371/Journal.Pone.0109213  0.318
2014 Alonzo D, Reimer J, Magarvey N, Schmeing TM. Towards the structure of an unusual nonribosomal peptide synthetase Acta Crystallographica Section a Foundations and Advances. 70: C433-C433. DOI: 10.1107/S2053273314095667  0.405
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2014 Bloudoff K, Schmeing T. NRPS condensation domain–substrate studies using X-ray crystallography Acta Crystallographica Section a Foundations and Advances. 70: C438-C438. DOI: 10.1107/S2053273314095618  0.349
2013 Bloudoff K, Rodionov D, Schmeing TM. Crystal structures of the first condensation domain of CDA synthetase suggest conformational changes during the synthetic cycle of nonribosomal peptide synthetases. Journal of Molecular Biology. 425: 3137-50. PMID 23756159 DOI: 10.1016/j.jmb.2013.06.003  0.343
2013 Bloudoff K, Schmeing TM. Crystallization and preliminary crystallographic analysis of the first condensation domain of viomycin synthetase. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 69: 412-5. PMID 23545648 DOI: 10.1107/S1744309113004004  0.417
2011 Schmeing TM, Voorhees RM, Kelley AC, Ramakrishnan V. How mutations in tRNA distant from the anticodon affect the fidelity of decoding. Nature Structural & Molecular Biology. 18: 432-6. PMID 21378964 DOI: 10.1038/Nsmb.2003  0.56
2011 Voorhees RM, Schmeing TM, Kelley AC, Ramakrishnan V. Response to comment on "The mechanism for activation of GTP hydrolysis on the ribosome" Science. 333: 37b. DOI: 10.1126/Science.1202532  0.408
2010 Voorhees RM, Schmeing TM, Kelley AC, Ramakrishnan V. The mechanism for activation of GTP hydrolysis on the ribosome. Science (New York, N.Y.). 330: 835-8. PMID 21051640 DOI: 10.1126/Science.1194460  0.638
2009 Schmeing TM, Ramakrishnan V. What recent ribosome structures have revealed about the mechanism of translation. Nature. 461: 1234-42. PMID 19838167 DOI: 10.1038/Nature08403  0.606
2009 Schmeing TM, Voorhees RM, Kelley AC, Gao YG, Murphy FV, Weir JR, Ramakrishnan V. The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA. Science (New York, N.Y.). 326: 688-94. PMID 19833920 DOI: 10.1126/Science.1179700  0.729
2007 Passmore LA, Schmeing TM, Maag D, Applefield DJ, Acker MG, Algire MA, Lorsch JR, Ramakrishnan V. The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome. Molecular Cell. 26: 41-50. PMID 17434125 DOI: 10.1016/J.Molcel.2007.03.018  0.695
2005 Schmeing TM, Huang KS, Strobel SA, Steitz TA. An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature. 438: 520-4. PMID 16306996 DOI: 10.1038/Nature04152  0.592
2005 Schmeing TM, Huang KS, Kitchen DE, Strobel SA, Steitz TA. Structural insights into the roles of water and the 2' hydroxyl of the P site tRNA in the peptidyl transferase reaction. Molecular Cell. 20: 437-48. PMID 16285925 DOI: 10.1016/J.Molcel.2005.09.006  0.56
2003 Schmeing TM, Moore PB, Steitz TA. Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit. Rna (New York, N.Y.). 9: 1345-52. PMID 14561884 DOI: 10.1261/Rna.5120503  0.662
2002 Hansen JL, Schmeing TM, Moore PB, Steitz TA. Structural insights into peptide bond formation. Proceedings of the National Academy of Sciences of the United States of America. 99: 11670-5. PMID 12185246 DOI: 10.1073/pnas.172404099  0.707
2002 Schmeing TM, Seila AC, Hansen JL, Freeborn B, Soukup JK, Scaringe SA, Strobel SA, Moore PB, Steitz TA. A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits. Nature Structural Biology. 9: 225-30. PMID 11828326 DOI: 10.1038/Nsb758  0.71
2001 Hansen JL, Schmeing TM, Klein DJ, Ippolito JA, Ban N, Nissen P, Freeborn B, Moore PB, Steitz TA. Progress toward an understanding of the structure and enzymatic mechanism of the large ribosomal subunit. Cold Spring Harbor Symposia On Quantitative Biology. 66: 33-42. PMID 12762006 DOI: 10.1101/Sqb.2001.66.33  0.704
2001 Klein DJ, Schmeing TM, Moore PB, Steitz TA. The kink-turn: a new RNA secondary structure motif. The Embo Journal. 20: 4214-21. PMID 11483524 DOI: 10.1093/Emboj/20.15.4214  0.653
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