Chemist
Chemist

Biography

  

Research and Professional Experience: 

Professional Experience:

1990 Postdoctoral Scientist, Laboratoire des Lesions des Acides Nucléique, Centre d’Etudes Nucléaires de Grenoble, Grenoble, France.

1991 - 1993 Postdoctoral Scientist, Radiobiology, Cross Cancer Institute, Edmonton, Alberta, Canada.

1993 – 1995 Postdoctoral Scientist, Institute of Molecular Biology and Biochemistry, Simon Fraser University, British Columbia, Canada.

1995-1999 Postdoctoral Scientist, Pacific Northwest National Laboratory, Richland, Washington, USA.

1999  Research Associate, Department of Radiology, Duke University Medical Center, Durham, North Carolina, USA.

2000  Research Associate, Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, Vermont, USA.

2001 – Present  Senior Research Scientist, Biological Sciences Division and Seattle Structural Genomics Center for Infectious Disease, Pacific Northwest National Laboratory, Richland, Washington, USA.

2017 – Present  Associate Professor, School of Molecular Biosciences, Washington State University, Pullman, Washington, USA.

Synopsis:

I have been a Senior Research Scientist at Pacific Northwest National Laboratory (PNNL) since 2000 and recently accepted a Joint Appointment as an Associate Professor in the School of Molecular Biosciences at Washington State University in 2017. I have 35+ years of experience as a physical biochemist with specializations in protein chemistry, structural biology, and NMR spectroscopy. Over my career I have published over 150 peer-reviewed papers and personally deposited more than 50 protein structures into the PDB. The past 15 years has been devoted heavily on an NIH-funded biomineralization project and an NIAID-funded structural genomics project (Seattle Structural Genomics Center for Infectious Diseases, SSGCID). As one of the four founding SSGCID PIs, my primary role has been to determine structures of proteins recalcitrant to forming well-diffracting crystals using solution-state NMR methods and publish (36 SSGCID-associated publications). The biomineralization project involves understanding how the intrinsically disordered protein amelogenin orchestrates the formation of the hardest tissue in the human body, tooth enamel. 

Research Interests

  • Structural Biology
  • NMR spectroscopy
  • Protein chemistry
  • Protein expression
  • Infectious diseases
  • Biomineralization

Education

  • Doctor of Philosophy in Chemistry,
  • Master of Science in Chemistry, McMaster University
  • Bachelor of Science in Biochemistry,

Affiliations and Professional Service

  • Associate Professor, School of Molecular Biosciences, WSU
  • Seattle Structural Genomics Center for Infectious Diseases
  • The Protein Society
  • International Association for Dental Research

Awards and Recognitions

  • Outstanding Performance Award, PNNL (2008, 2010, 2015)
  • International Workshop on Radiation Damage in DNA Travel Award, 1994
  • BC and Yukon Heart and Stroke Research Fellowship, 1993-1995
  • Alberta Cancer Board Research Fellowship, 1991-1992
  • Travel Award, American Association of Cancer Research, 1991
  • France-Canada Postdoctoral Fellowship, Government of France, 1990
  • Travel Award, A.N. Campbell, 1989

Publications

2026

  • Buchko, G., L. Liu, K. Battaile, J. Craig, E. Harmon, W. VanVoorhis, P. Myler, and S. Lovell. 2026. A Trichomonas vaginalis C2-XYPPX-repeat protein with a structured C2 domain displaying dampened flexibility upon binding calcium. Biochimie. doi:10.1016/j.biochi.2025.11.011
  • Teptarakulkarn, P., R. Treviño, A. Hansen, J. Laureanti, G. Buchko, W. Shaw, and H. Shafaat. 2026. Correlating Protein Dynamics and Catalytic Activity of a Model Hydrogenase Using Paramagnetic and Biological Nuclear Magnetic Resonance Spectroscopy. Journal of the American Chemical Society 148(2), 2351-2364. doi:10.1021/jacs.5c15958

2025

  • Dahiya, D., Z. Péter-Szabó, M. Senanayake, S. Pingali, W. Leite, J. Byrnes, G. Buchko, P. Sivan, F. Vilaplana, E. Master, and H. O’Neill. 2025. SANS investigation of fungal loosenins reveals substrate-dependent impacts of protein action on the inter-microfibril arrangement of cellulosic substrates. Biotechnology for Biofuels and Bioproducts 18(1). doi:10.1186/s13068-025-02618-5
  • Buchko, G., N. Kegulian, and J. Moradian-Oldak. 2025. Ameloblastin binding to biomimetic models of cell membranes – A continuum of intrinsic disorder. Archives of Oral Biology 169, 106124. doi:10.1016/j.archoralbio.2024.106124

2024

  • Godwin, J., A. Djami-Tchatchou, S. Velivelli, M. Tetorya, R. Kalunke, A. Pokhrel, M. Zhou, G. Buchko, K. Czymmek, and D. Shah. 2024. Chickpea NCR13 disulfide cross-linking variants exhibit profound differences in antifungal activity and modes of action. PLOS Pathogens 20(12), e1012745. doi:10.1371/journal.ppat.1012745 doi:10.1101/2024.08.09.607347
  • Mergelsberg, S., H. Kim, G. Buchko, and B. Ginovska. 2024. SAXS of murine amelogenin identifies a persistent dimeric species from pH 5.0 to 8.0. Journal of Structural Biology 216(4), 108131. doi:10.1016/j.jsb.2024.108131
  • Haddad Momeni, M., A. Zitting, V. Jäämuru, R. Turunen, P. Penttilä, G. Buchko, S. Hiltunen, N. Maiorova, A. Koivula, J. Sapkota, K. Marjamaa, and E. Master. 2024. Insights into the action of phylogenetically diverse microbial expansins on the structure of cellulose microfibrils. Biotechnology for Biofuels and Bioproducts 17(1). doi:10.1186/s13068-024-02500-w

2023

  • 2023. Plant defensin MtDef4‐derived antifungal peptide with multiple modes of action and potential as a bio‐inspired fungicide. Molecular Plant Pathology. doi:10.1111/mpp.13336
  • Taylor, S., J. Tao, Y. Shin, G. Buchko, A. Dohnalkova, J. Grimm, B. Tarasevich, B. Ginovska, W. Shaw, and A. Devaraj. 2023. Resolving protein-mineral interfacial interactions during in vitro mineralization by atom probe tomography. Materials Today Advances 18, 100378. doi:10.1016/j.mtadv.2023.100378
  • Gu, Y., M. Liu, B. Staker, G. Buchko, and R. Quinn. 2023. Drug-Repurposing Screening Identifies a Gallic Acid Binding Site on SARS-CoV-2 Non-structural Protein 7. ACS Pharmacology & Translational Science 6(4), 578-586. doi:10.1021/acsptsci.2c00225
  • 2023. High‐yield recombinant bacterial expression of 13C‐, 15N‐labeled, serine‐16 phosphorylated, murine amelogenin using a modified third generation genetic code expansion protocol. Protein Science. doi:10.1002/pro.4560

2022

  • 2022. Residue-Specific Insights into the Intermolecular Protein–Protein Interfaces Driving Amelogenin Self-Assembly in Solution. Biochemistry. doi:10.1021/acs.biochem.2c00522
  • Tao, J., E. Hanson, A. Dohnalkova, G. Buchko, B. Jin, W. Shaw, and B. Tarasevich. 2022. Changes in the C-terminal, N-terminal, and histidine regions of amelogenin reveal the role of oligomer quaternary structure on adsorption and hydroxyapatite mineralization. Frontiers in Physiology 13. doi:10.3389/fphys.2022.1034662
  • 2022. Plant defensin MtDef4-derived antifungal peptide with multiple modes of action and potential as a bioinspired fungicide. doi:10.1101/2022.10.02.510465
  • 2022. Structural characterization of a soil viral auxiliary metabolic gene product – a functional chitosanase. Nature Communications. doi:10.1038/s41467-022-32993-8
  • 2022. Understanding Proton Movement in [Fe-Fe] Hydrogenases. doi:10.2172/1983356
  • Mandel, C., H. Yang, G. Buchko, J. Abendroth, N. Grieshaber, T. Chiarelli, S. Grieshaber, and A. Omsland. 2022. Expression and structure of the Chlamydia trachomatis DksA ortholog. Pathogens and Disease 80(1). doi:10.1093/femspd/ftac007
  • Abendroth, J., G. Buchko, F. Liew, J. Nguyen, and H. Kim. 2022. Structural Characterization of Cytochrome c′β‐Met from an Ammonia-Oxidizing Bacterium. Biochemistry 61(7), 563-574. doi:10.1021/acs.biochem.1c00640

2021

  • Choi, R., M. Zhou, R. Shek, J. Wilson, L. Tillery, J. Craig, I. Salukhe, S. Hickson, N. Kumar, R. James, G. Buchko, R. Wu, S. Huff, T. Nguyen, B. Hurst, S. Cherry, L. Barrett, J. Hyde, and W. Van Voorhis. 2021. High-throughput screening of the ReFRAME, Pandemic Box, and COVID Box drug repurposing libraries against SARS-CoV-2 nsp15 endoribonuclease to identify small-molecule inhibitors of viral activity. PLOS ONE 16(4), e0250019. doi:10.1371/journal.pone.0250019
  • 2021. Backbone chemical shift assignments for the SARS-CoV-2 non-structural protein Nsp9: intermediate (ms – μs) dynamics in the C-terminal helix at the dimer interface. Biomolecular NMR Assignments. doi:10.1007/s12104-020-09992-1

2020

  • 2020. Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite. Journal of Structural Biology. doi:10.1016/j.jsb.2020.107630
  • 2020. Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection. Proceedings of the National Academy of Sciences. doi:10.1073/pnas.2003526117
  • Elnaas, A., D. Grice, J. Han, Y. Feng, A. Capua, T. Mak, J. Laureanti, G. Buchko, P. Myler, G. Cook, R. Quinn, and M. Liu. 2020. Discovery of a Natural Product That Binds to the Mycobacterium tuberculosis Protein Rv1466 Using Native Mass Spectrometry. Molecules 25(10), 2384. doi:10.3390/molecules25102384
  • 2020. A Positive Charge in the Outer Coordination Sphere of an Artificial Enzyme Increases CO2 Hydrogenation. Organometallics. doi:10.1021/acs.organomet.9b00843
  • Xie, Y., Y. Feng, A. Di Capua, T. Mak, G. Buchko, P. Myler, M. Liu, and R. Quinn. 2020. A Phenotarget Approach for Identifying an Alkaloid Interacting with the Tuberculosis Protein Rv1466. Marine Drugs 18(3), 149. doi:10.3390/md18030149
  • 2020. Solution structure for an Encephalitozoon cuniculi adrenodoxin‐like protein in the oxidized state. Protein Science. doi:10.1002/pro.3818
  • 2020. Structural diversity in the Mycobacteria DUF3349 superfamily. Protein Science. doi:10.1002/pro.3758
  • Ma, Z., J. Abendroth, G. Buchko, K. Rohde, and V. Davidson. 2020. Crystal structure of a hemerythrin-like protein from Mycobacterium kansasii and homology model of the orthologous Rv2633c protein of M. tuberculosis. Biochemical Journal 477(2), 567-581. doi:10.1042/bcj20190827

2019

  • 2019. The energetic basis for hydroxyapatite mineralization by amelogenin variants provides insights into the origin of amelogenesis imperfecta. Proceedings of the National Academy of Sciences. doi:10.1073/pnas.1815654116
  • Laureanti, J., G. Buchko, S. Katipamula, Q. Su, J. Linehan, O. Zadvornyy, J. Peters, and M. O’Hagan. 2019. Protein Scaffold Activates Catalytic CO 2 Hydrogenation by a Rhodium Bis(diphosphine) Complex. ACS Catalysis 9(1), 620-625. doi:10.1021/acscatal.8b02615

2018

  • 2018. Identification of major matrix metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rich amelogenin peptide using a nuclear magnetic resonance spectroscopy based method. Archives of Oral Biology. doi:10.1016/j.archoralbio.2018.06.001
  • 2018. Solution NMR structures of oxidized and reduced Ehrlichia chaffeensis thioredoxin: NMR-invisible structure owing to backbone dynamics. Acta Crystallographica Section F Structural Biology Communications. doi:10.1107/S2053230X1701799X
  • Buchko, G., S. Pulavarti, V. Ovchinnikov, E. Shaw, S. Rettie, P. Myler, M. Karplus, T. Szyperski, D. Baker, and C. Bahl. 2018. Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide-rich de novo designed peptides. Protein Science 27(9), 1611-1623. doi:10.1002/pro.3453
  • Arachchige, R., S. Burton, J. Lu, B. Ginovska, L. Harding, M. Taylor, J. Tao, A. Dohnalkova, B. Tarasevich, G. Buchko, and W. Shaw. 2018. Solid-State NMR Identification of Intermolecular Interactions in Amelogenin Bound to Hydroxyapatite. Biophysical Journal 115(9), 1666-1672. doi:10.1016/j.bpj.2018.08.027
  • 2018. Structure flexibility controls the adsorption and digestion kinetics of point mutant amelogenin on hydroxyapatite (100). Abstracts of Papers of the American Chemical Society.
  • Mori, S., K. Green, R. Choi, G. Buchko, M. Fried, and S. Garneau‐Tsodikova. 2018. Using MbtH-Like Proteins to Alter the Substrate Profile of a Nonribosomal Peptide Adenylation Enzyme. Chembiochem 19(20), 2186-2194. doi:10.1002/cbic.201800240

2017

  • Zerfaß, C., G. Buchko, W. Shaw, S. Hobe, and H. Paulsen. 2017. Secondary structure and dynamics study of the intrinsically disordered silica‐mineralizing peptide P5S3 during silicic acid condensation and silica decondensation. Proteins: Structure, Function, and Bioinformatics 85(11), 2111-2126. doi:10.1002/prot.25366
  • 2017. Structural and Biophysical Characterization of the Mycobacterium tuberculosis Protein Rv0577, a Protein Associated with Neutral Red Staining of Virulent Tuberculosis Strains and Homologue of the Streptomyces coelicolor Protein KbpA. Biochemistry. doi:10.1021/acs.biochem.7b00511
  • Buchko, G., M. Clifton, E. Wallace, K. Atkins, and P. Myler. 2017. Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus. Biomolecular NMR Assignments 11(1), 51-56. doi:10.1007/s12104-016-9719-2
  • Boralugodage, N., R. Arachchige, A. Dutta, G. Buchko, and W. Shaw. 2017. Evaluating the role of acidic, basic, and polar amino acids and dipeptides on a molecular electrocatalyst for H2 oxidation. Catalysis Science and Technology 7(5), 1108-1121. doi:10.1039/c6cy02579j

2016

  • Bhardwaj, G., V. Mulligan, C. Bahl, J. Gilmore, P. Harvey, O. Cheneval, G. Buchko, S. Pulavarti, Q. Kaas, A. Eletsky, P. Huang, W. Johnsen, P. Greisen, G. Rocklin, Y. Song, T. Linsky, A. Watkins, S. Rettie, X. Xu, L. Carter, R. Bonneau, J. Olson, E. Coutsias, C. Correnti, T. Szyperski, D. Craik, and D. Baker. 2016. Accurate de novo design of hyperstable constrained peptides. Nature 538(7625), 329-335. doi:10.1038/nature19791
  • Priyadarshani, N., A. Dutta, B. Ginovska, G. Buchko, M. O’Hagan, S. Raugei, and W. Shaw. 2016. Achieving Reversible H2/H+ Interconversion at Room Temperature with Enzyme-Inspired Molecular Complexes: A Mechanistic Study. ACS Catalysis 6(9), 6037-6049. doi:10.1021/acscatal.6b01433
  • Buchko, G., A. Perkins, D. Parsonage, L. Poole, and P. Karplus. 2016. Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics. Biomolecular Nmr Assignments 10(1), 57-61. doi:10.1007/s12104-015-9637-8
  • Reback, M., B. Ginovska, G. Buchko, A. Dutta, N. Priyadarshani, B. Kier, M. Helm, S. Raugei, and W. Shaw. 2016. Investigating the role of chain and linker length on the catalytic activity of an H2 production catalyst containing a β-hairpin peptide. Journal of Coordination Chemistry 69(11-13), 1730-1747. doi:10.1080/00958972.2016.1188924

2015

  • Buchko, G., T. Edwards, S. Hewitt, I. Phan, W. Van Voorhis, S. Miller, and P. Myler. 2015. Backbone chemical shift assignments for the sensor domain of the Burkholderia pseudomallei histidine kinase RisS: “missing” resonances at the dimer interface. Biomol NMR Assign 9(2), 381-385. doi:10.1007/s12104-015-9614-2
  • Buchko, G., A. Yee, A. Semesi, P. Myler, C. Arrowsmith, and R. Hui. 2015. Solution-state NMR structure of the putative morphogene protein BolA (PFE0790c) from Plasmodium falciparum. Acta Crystallogr Sect F Struct Biol Cryst Commun 71(5), 514-521. doi:10.1107/s2053230x1402799x
  • Buchko, G., J. Abendroth, M. Clifton, H. Robinson, Y. Zhang, S. Hewitt, B. Staker, T. Edwards, W. Van Voorhis, and P. Myler. 2015. Structure of a CutA1 divalent-cation tolerance protein from Cryptosporidium parvum , the protozoal parasite responsible for cryptosporidiosis. Acta Crystallogr Sect F Struct Biol Cryst Commun 71(5), 522-530. doi:10.1107/s2053230x14028210
  • Tarasevich, B., J. Philo, N. Maluf, S. Krueger, G. Buchko, G. Lin, and W. Shaw. 2015. The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution. Journal of Structural Biology 190(1), 81-91. doi:10.1016/j.jsb.2014.10.007
  • Buchko, G. and W. Shaw. 2015. Improved protocol to purify untagged amelogenin – Application to murine amelogenin containing the equivalent P70→T point mutation observed in human amelogenesis imperfecta. Protein Expression and Purification 105, 14-22. doi:10.1016/j.pep.2014.09.020
  • Baugh, L., I. Phan, D. Begley, M. Clifton, B. Armour, D. Dranow, B. Taylor, M. Muruthi, J. Abendroth, J. Fairman, D. Fox, S. Dieterich, B. Staker, A. Gardberg, R. Choi, S. Hewitt, A. Napuli, J. Myers, L. Barrett, Y. Zhang, M. Ferrell, E. Mundt, K. Thompkins, N. Tran, S. Lyons-Abbott, A. Abramov, A. Sekar, D. Serbzhinskiy, D. Lorimer, G. Buchko, R. Stacy, L. Stewart, T. Edwards, W. Van Voorhis, and P. Myler. 2015. Increasing the structural coverage of tuberculosis drug targets. Tuberculosis 95(2), 142-148. doi:10.1016/j.tube.2014.12.003
  • Staker, B., G. Buchko, and P. Myler. 2015. Recent contributions of structure-based drug design to the development of antibacterial compounds. Current Opinion in Microbiology 27, 133-138. doi:10.1016/j.mib.2015.09.003
  • Tao, J., G. Buchko, W. Shaw, J. De Yoreo, and B. Tarasevich. 2015. Sequence-Defined Energetic Shifts Control the Disassembly Kinetics and Microstructure of Amelogenin Adsorbed onto Hydroxyapatite (100). Langmuir 31(38), 10451-10460. doi:10.1021/acs.langmuir.5b02549

2014

  • Reback, M., G. Buchko, B. Kier, B. Ginovska‐Pangovska, Y. Xiong, S. Lense, J. Hou, J. Roberts, C. Sorensen, S. Raugei, T. Squier, and W. Shaw. 2014. Enzyme Design from the Bottom Up: An Active Nickel Electrocatalyst with a Structured Peptide Outer Coordination Sphere. Chemistry-a European Journal 20(6), 1510-1514. doi:10.1002/chem.201303976
  • Zhang, Y., Y. Zheng, L. Qin, S. Wang, G. Buchko, and R. Garavito. 2014. Structural characterization of a beta-hydroxyacid dehydrogenase from Geobacter sulfurreducens and Geobacter metallireducens with succinic semialdehyde reductase activity. Biochimie 104, 61-69. doi:10.1016/j.biochi.2014.05.002
  • Lu, J., S. Burton, Y. Xu, G. Buchko, and W. Shaw. 2014. The flexible structure of the K24S28 region of Leucine-Rich Amelogenin Protein (LRAP) bound to apatites as a function of surface type, calcium, mutation, and ionic strength. Frontiers in Physiology 5. doi:10.3389/fphys.2014.00254

2013

  • Buchko, G., G. Lin, B. Tarasevich, and W. Shaw. 2013. A solution NMR investigation into the impaired self-assembly properties of two murine amelogenins containing the point mutations T21 -> I or P41 -> T. Archives of Biochemistry and Biophysics 537(2), 217-224. doi:10.1016/j.abb.2013.07.015
  • Baugh, L., L. Gallagher, R. Patrapuvich, M. Clifton, A. Gardberg, T. Edwards, B. Armour, D. Begley, S. Dieterich, D. Dranow, J. Abendroth, J. Fairman, D. Fox, B. Staker, I. Phan, A. Gillespie, R. Choi, S. Nakazawa-Hewitt, M. Nguyen, A. Napuli, L. Barrett, G. Buchko, R. Stacy, P. Myler, L. Stewart, C. Manoil, and W. Van Voorhis. 2013. Combining Functional and Structural Genomics to Sample the Essential Burkholderia Structome. Plos One 8(1), e53851. doi:10.1371/journal.pone.0053851
  • Buchko, G., J. Abendroth, H. Robinson, Y. Zhang, S. Hewitt, T. Edwards, W. Van Voorhis, and P. Myler. 2013. Crystal structure of a macrophage migration inhibitory factor from Giardia lamblia. Journal of structural and functional genomics 14(2), 47-57. doi:10.1007/s10969-013-9155-9
  • Lu, J., Y. Xu, G. Buchko, and W. Shaw. 2013. Mineral Association Changes the Secondary Structure and Dynamics of Murine Amelogenin. Journal of Dental Research 92(11), 1000-1004. doi:10.1177/0022034513504929
  • Buchko, G., S. Hewitt, W. Van Voorhis, and P. Myler. 2013. Solution structure of a putative FKBP-type peptidyl-propyl cis-trans isomerase from Giardia lamblia. Journal of Biomolecular Nmr 57(4), 369-374. doi:10.1007/s10858-013-9797-8
  • Sagaram, U., K. El-Mounadi, G. Buchko, H. Berg, J. Kaur, R. Pandurangi, T. Smith, and D. Shah. 2013. Structural and Functional Studies of a Phosphatidic Acid-Binding Antifungal Plant Defensin MtDef4: Identification of an RGFRRR Motif Governing Fungal Cell Entry. Plos One 8(12), e82485. doi:10.1371/journal.pone.0082485
  • Buchko, G., A. Jain, M. Reback, and W. Shaw. 2013. Structural characterization of the model amphipathic peptide Ac-LKKLLKLLKKLLKL-NH2 in aqueous solution and with 2,2,2-trifluoroethanol and 1,1,1,3,3,3-hexafluoroisopropanol. Canadian Journal of Chemistry-Revue Canadienne De Chimie 91(6), 406-413. doi:10.1139/cjc-2012-0429
  • Zhang, Y., A. Gardberg, T. Edwards, B. Sankaran, H. Robinson, S. Varnum, and G. Buchko. 2013. Structural insights into the functional role of the Hcn sub-domain of the receptor-binding domain of the botulinum neurotoxin mosaic serotype C/D. Biochimie 95(7), 1379-1385. doi:10.1016/j.biochi.2013.03.006

2012

  • Jain, A., G. Buchko, M. Reback, M. O’Hagan, B. Ginovska-Pangovska, J. Linehan, and W. Shaw. 2012. Active Hydrogenation Catalyst with a Structured, Peptide-Based Outer-Coordination Sphere. Acs Catalysis 2(10), 2114-2118. doi:10.1021/cs3004177
  • Buchko, G., H. Kim, P. Myler, T. Terwilliger, and C. Kim. 2012. Chemical shift assignments for Rv0577, a putative glyoxylase associated with virulence from Mycobacterium tuberculosis. Biomolecular Nmr Assignments 6(1), 43-46. doi:10.1007/s12104-011-9322-5
  • Buchko, G. and H. Robinson. 2012. Crystal structure of cce_0566 from Cyanothece 51142, a protein associated with nitrogen fixation in the DUF269 family. Febs Letters 586(4), 350-355. doi:10.1016/j.febslet.2012.01.037
  • Jin, H., Y. Zhang, G. Buchko, S. Varnum, H. Robinson, T. Squier, and P. Long. 2012. Structure Determination and Functional Analysis of a Chromate Reductase from Gluconacetobacter hansenii. Plos One 7(8), e42432. doi:10.1371/journal.pone.0042432

2011

  • Zhang, Y., G. Buchko, L. Qin, H. Robinson, and S. Varnum. 2011. Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions. Biochemical and Biophysical Research Communications 404(1), 407-412. doi:10.1016/j.bbrc.2010.11.134
  • Buchko, G., I. Phan, P. Myler, T. Terwilliger, and C. Kim. 2011. Inaugural structure from the DUF3349 superfamily of proteins, Mycobacterium tuberculosis Rv0543c. Archives of Biochemistry and Biophysics 506(2), 150-156. doi:10.1016/j.abb.2010.12.001
  • Buchko, G., S. Hewitt, A. Napuli, W. Van Voorhis, and P. Myler. 2011. Solution structure of an arsenate reductase-related protein, YffB, from Brucella melitensis, the etiological agent responsible for brucellosis. Acta Crystallographica Section F-Structural Biology and Crystallization Communications 67(9), 1129-1136. doi:10.1107/S1744309111006336
  • Buchko, G., S. Hewitt, A. Napuli, W. Van Voorhis, and P. Myler. 2011. Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis. Acta Crystallographica Section F-Structural Biology and Crystallization Communications 67(9), 1148-1153. doi:10.1107/S1744309111008189
  • Buchko, G. 2011. Structural Genomics-A Goldmine of Blueprints for Structure-Based Drug Design. J Postgenom Drug Biomark Develop 01(02). doi:10.4172/2153-0769.1000104e
  • Stacy, R., D. Begley, I. Phan, B. Staker, W. Van Voorhis, G. Varani, G. Buchko, L. Stewart, and P. Myler. 2011. Structural genomics of infectious disease drug targets: the SSGCID introduction. Acta Crystallographica Section F-Structural Biology and Crystallization Communications 67(9), 979-984. doi:10.1107/S1744309111029204
  • Buchko, G., T. Edwards, J. Abendroth, T. Arakaki, L. Law, A. Napuli, S. Hewitt, W. Van Voorhis, L. Stewart, B. Staker, and P. Myler. 2011. Structure of a Nudix hydrolase (MutT) in the Mg2+-bound state from Bartonella henselae, the bacterium responsible for cat scratch fever. Acta Crystallographica Section F-Structural Biology and Crystallization Communications 67(9), 1078-1083. doi:10.1107/S1744309111011559

2010

  • W. Buchko, G. 2010. Circular Dichroism Studies on the Deinococcus radiodurans Nudix Hydrolase DR_0079: An Atypical Thermal Melt. PPL 17(7), 831-835. doi:10.2174/092986610791306689
  • Buchko, G., G. Niemann, E. Baker, M. Belov, R. Smith, F. Heffron, J. Adkins, and J. McDermott. 2010. A multi-pronged search for a common structural motif in the secretion signal of Salmonella enterica serovar Typhimurium type III effector proteins. Molecular Biosystems 6(12), 2448. doi:10.1039/c0mb00097c
  • Buchko, G., B. Tarasevich, J. Roberts, M. Snead, and W. Shaw. 2010. A solution NMR investigation into the murine amelogenin splice-variant LRAP (Leucine-Rich Amelogenin Protein). Biochimica Et Biophysica Acta-Proteins and Proteomics 1804(9), 1768-1774. doi:10.1016/j.bbapap.2010.03.006
  • Tang, Z., H. Wu, J. Cort, G. Buchko, Y. Zhang, Y. Shao, I. Aksay, J. Liu, and Y. Lin. 2010. Constraint of DNA on Functionalized Graphene Improves its Biostability and Specificity. Small 6(11), 1205-1209. doi:10.1002/smll.201000024
  • Zhang, Y., X. Gao, L. Qin, G. Buchko, H. Robinson, and S. Varnum. 2010. High-level expression, purification, crystallization and preliminary X-ray crystallographic studies of the receptor-binding domain of botulinum neurotoxin serotype D. Acta Crystallographica Section F-Structural Biology and Crystallization Communications 66(12), 1610-1613. doi:10.1107/S1744309110039874
  • Buchko, G., C. Kim, T. Terwilliger, and P. Myler. 2010. Solution structure of Rv2377c-founding member of the MbtH-like protein family. Tuberculosis 90(4), 245-251. doi:10.1016/j.tube.2010.04.002
  • Zhang, Y., G. Buchko, L. Qin, H. Robinson, and S. Varnum. 2010. Structural analysis of the receptor binding domain of botulinum neurotoxin serotype D. Biochemical and Biophysical Research Communications 401(4), 498-503. doi:10.1016/j.bbrc.2010.09.063
  • Buchko, G., H. Robinson, J. Abendroth, B. Staker, and P. Myler. 2010. Structural characterization of Burkholderia pseudomallei adenylate kinase (Adk): Profound asymmetry in the crystal structure of the 'open' state. Biochemical and Biophysical Research Communications 394(4), 1012-1017. doi:10.1016/j.bbrc.2010.03.112

2009

  • 2009. A BAYESIAN INTEGRATION MODEL OF HIGH-THROUGHPUT PROTEOMICS AND METABOLOMICS DATA FOR IMPROVED EARLY DETECTION OF MICROBIAL INFECTIONS. Pacific Symposium on Biocomputing 2009.
  • Buchko, G., S. Hewitt, A. Napuli, W. Van Voorhis, and P. Myler. 2009. Backbone and side chain H-1, C-13, and N-15 NMR assignments for the organic hydroperoxide resistance protein (Ohr) from Burkholderia pseudomallei. Biomolecular Nmr Assignments 3(2), 163-166. doi:10.1007/s12104-009-9165-5
  • 2009. Pentapeptide repeat proteins and cyanobacteria. Handbook on Cyanobacteria: Biochemistry, Biotechnology and Applications.
  • Buchko, G., H. Robinson, and A. Addlagatta. 2009. Structural characterization of the protein cce_0567 from Cyanothece 51142, a metalloprotein associated with nitrogen fixation in the DUF683 family. Biochimica Et Biophysica Acta-Proteins and Proteomics 1794(4), 627-633. doi:10.1016/j.bbapap.2009.01.002
  • 2009. The Seattle Structural Genomics Center for Infectious Disease (SSGCID). Infectious disorders drug targets.
  • Myler, P., R. Stacy, L. Stewart, B. Staker, W. Van Voorhis, G. Varani, and G. Buchko. 2009. The seattle structural genomics center for infectious disease (SSGCID). Infectious Disorders - Drug Targets 9(5), 493-506. doi:10.2174/187152609789105687
  • Harvey, S., G. Buchko, R. Lucke, C. Wright, A. Melville, A. Scott, and B. Wright. 2009. The structure and purity of a reference dye standard used for quantification of CI Solvent Red 164 in fuels. Dyes and Pigments 82(3), 307-315. doi:10.1016/j.dyepig.2009.01.015

2008

  • Buchko, G., B. Tarasevich, J. Bekhazi, M. Snead, and W. Shaw. 2008. A Solution NMR Investigation into the Early Events of Amelogenin Nanosphere Self-Assembly Initiated with Sodium Chloride or Calcium Chloride. Biochemistry 47(50), 13215-13222. doi:10.1021/bi8018288
  • Buchko, G. and H. Sofia. 2008. Backbone (1)H, (13)C, and (15)N NMR assignments for the Cyanothece 51142 protein cce_0567: a protein associated with nitrogen fixation in the DUF683 family. Biomolecular Nmr Assignments 2(1), 25-28. doi:10.1007/s12104-007-9075-3
  • Buchko, G., O. Litvinova, H. Robinson, A. Yakunin, and M. Kennedy. 2008. Functional and structural characterization of DR_0079 from Deinococcus radiodurans, a novel Nudix hydrolase with a preference for cytosine (deoxy)ribonucleoside 5 '-di- and triphosphates. Biochemistry 47(25), 6571-6582. doi:10.1021/bi800099d
  • Buchko, G., J. Bekhazi, J. Cort, N. Valentine, M. Snead, and W. Shaw. 2008. H-1, C-13, and N-15 resonance assignments of murine amelogenin, an enamel biomineralization protein. Biomolecular Nmr Assignments 2(1), 89-91. doi:10.1007/s12104-008-9092-x
  • Buchko, G., H. Robinson, H. Pakrasi, and M. Kennedy. 2008. Insights into the structural variation between pentapeptide repeat proteins - Crystal structure of Rfr23 from Cyanothece 51142. Journal of Structural Biology 162(1), 184-192. doi:10.1016/j.jsb.2007.11.008

2007

  • Buchko, G., S. Ni, N. Lourette, R. Reeves, and M. Kennedy. 2007. NMR resonance assignments of the human high mobility group protein HMGA1. Journal of Biomolecular Nmr 38(2), 185-185. doi:10.1007/s10858-006-9116-8

2006

  • Buchko, G., S. Ni, H. Robinson, E. Welsh, H. Pakrasi, and M. Kennedy. 2006. Characterization of two potentially universal turn motifs that shape the repeated five-residues fold - Crystal structure of a lumenal pentapeptide repeat protein from Cyanothece 51142. Protein Science 15(11), 2579-2595. doi:10.1110/ps.062407506
  • Buchko, G., H. Robinson, S. Ni, H. Pakrasi, and M. Kennedy. 2006. Cloning, expression, crystallization and preliminary crystallographic analysis of a pentapeptide-repeat protein (Rfr23) from the bacterium Cyanothece 51142. Acta Crystallographica Section F-Structural Biology and Crystallization Communications 62(12), 1251-1254. doi:10.1107/S174430910604663X
  • Buchko, G. and J. Cadet. 2006. Identification of the alpha and beta anomers of 1-(2-deoxy-D-erythro-pentofuranosyl)-oxaluric acid at the site of riboflavin-mediated photooxidation of guanine in 2 '-deoxyguanosine and thymidylyl-(3 '-5 ')2 '-deoxyguanosine. Photochemistry and Photobiology 82(1), 191. doi:10.1562/2005-06-01-RA-562
  • Buchko, G., C. Kim, T. Terwilliger, and M. Kennedy. 2006. Solution structure of the conserved hypothetical protein Rv2302 from Mycobacterium tuberculosis. Journal of Bacteriology 188(16), 5993-6001. doi:10.1128/JB.00460-06

2005

  • Buchko, G., K. McAteer, S. Wallace, and M. Kennedy. 2005. Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): a dynamic description of the DNA/protein interface. DNA Repair 4(3), 327-339. doi:10.1016/j.dnarep.2004.09.012

2004

  • McAteer, K., A. Aceves‐Gaona, R. Michalczyk, G. Buchko, N. Isern, L. Silks, J. Miller, and M. Kennedy. 2004. Compensating bends in a 16-base-pair DNA oligomer containing a T(3)A(3) segment: A NMR study of global DNA curvature. Biopolymers 75(6), 497-511. doi:10.1002/bip.20168
  • Buchko, G., S. Ni, S. Holbrook, and M. Kennedy. 2004. Solution structure of hypothetical Nudix hydrolase DR0079 from extremely radiation-resistant Deinococcus radiodurans bacterium. Proteins-Structure Function and Bioinformatics 56(1), 28-39. doi:10.1002/prot.20082

2003

  • Daughdrill, G. 2003. Chemical shift changes provide evidence for overlapping single-stranded DNA- and XPA-binding sites on the 70 kDa subunit of human replication protein A. Nucleic Acids Research 31(14), 4176-4183. doi:10.1093/nar/gkg451
  • Buchko, G., S. Ni, S. Holbrook, and M. Kennedy. 2003. H-1, C-13, and N-15 NMR assignments of the hypothetical Nudix protein DR0079 from the extremely radiation-resistant bacterium Deinococcus radiodurans. Journal of Biomolecular Nmr 25(2), 169-170. doi:10.1023/A:1022243724501
  • Holbrook, E., U. Schulze-Gahmen, G. Buchko, S. Ni, M. Kennedy, and S. Holbrook. 2003. Purification, crystallization and preliminary X-ray analysis of two nudix hydrolases from Deninococcus radiodurans. Acta Crystallographica Section D-Biological Crystallography 59(4), 737-740. doi:10.1107/S0907444903002671

2002

  • Buchko, G. and M. Weinfeld. 2002. DNA-targeted 2-nitroimidazoles: Studies of the influence of the phenanthridine-linked nitroimidazoles, 2-NLP-3 and 2-NLP-4, on DNA damage induced by ionizing radiation. Radiation Research 158(3), 302-310. doi:10.1667/0033-7587(2002)158[0302:DTNSOT]2.0.CO;2
  • Buchko, G., S. Wallace, and M. Kennedy. 2002. Letter to the Editor: Base excision repair: NMR backbone assignments of Escherichia coli formamidopyrimidine-DNA glycosylase. Journal of Biomolecular Nmr 22(3), 301-302. doi:10.1023/A:1014903518628

2001

  • 2001. DNA-XPA interactions: A 31P NMR and molecular modeling study of dCCAATAACC association with the minimal DNA-binding domain (M98-F219) of the nucleotide excision repair protein XPA. Nucleic Acids Research.
  • Buchko, G. 2001. DNA-XPA interactions: a P-31 NMR and molecular modeling study of dCCAATAACC association with the minimal DNA-binding domain (M98-F219) of the nucleotide excision repair protein XPA. Nucleic Acids Research 29(12), 2635-2643. doi:10.1093/nar/29.12.2635
  • Buchko, G., N. Isern, L. Spicer, and M. Kennedy. 2001. Human nucleotide excision repair protein XPA: NMR spectroscopic studies of an XPA fragment containing the ERCC1-binding region and the minimal DNA-binding domain (M59-F219). Mutation Research-DNA Repair 486(1), 1-10. doi:10.1016/S0921-8777(01)00072-6
  • Buchko, G. and M. Kennedy. 2001. Hydroxyapatite elution behavior of human nucleotide excision repair protein XPA and fragments of XPA. Protein and Peptide Letters 8(5), 357-365. doi:10.2174/0929866013409300
  • Lipton, A., G. Buchko, J. Sears, M. Kennedy, and P. Ellis. 2001. Zn-67 solid-state NMR spectroscopy of the minimal DNA binding domain of human nucleotide excision repair protein XPA. Journal of the American Chemical Society 123(5), 992-993. doi:10.1021/ja003720e

2000

  • 2000. Cadmium mutagenicity and human nucleotide excision repair protein XPA: CD, EXAFS and 1H/15N-NMR spectroscopic studies on the zinc(II)- and cadmium(II)-associated minimal DNA-binding domain (M98-F219). Carcinogenesis.
  • Buchko, G. 2000. Cadmium mutagenicity and human nucleotide excision repair protein XPA: CD, EXAFS and H-1/N-15-NMR spectroscopic studies on the zinc(II)- and cadmium(II)-associated minimal DNA-binding domain (M98-F219). Carcinogenesis 21(5), 1051-1057. doi:10.1093/carcin/21.5.1051
  • 2000. Human nucleotide excision repair protein XPA: Summary of exafs studies on the Zn (II), Co (II) and Cd (II) associated minimal DNA-binding domain. Protein and Peptide Letters.
  • Buchko, G., N. Hess, V. Bandaru, S. Wallace, and M. Kennedy. 2000. Spectroscopic studies of zinc(II)- and cobalt(II)-associated Escherichia coli formamidopyrimidine-DNA glycosylase: Extended X-ray absorption fine structure evidence for a metal-binding domain. Biochemistry 39(40), 12441-12449. doi:10.1021/bi001377k
  • 2000. Structural studies of a baboon (Papio sp.) plasma protein inhibitor of cholesteryl ester transferase. Protein Science.

1999

  • Buchko, G., L. Iakoucheva, M. Kennedy, E. Ackerman, and N. Hess. 1999. Extended X-ray absorption fine structure evidence for a single metal binding domain in Xenopus laevis nucleotide excision repair protein XPA. Biochemical and Biophysical Research Communications 254(1), 109-113. doi:10.1006/bbrc.1998.9890
  • Buchko, G., G. Daughdrill, R. de Lorimier, . Sudha Rao B. K.,, N. Isern, J. Lingbeck, J. Taylor, M. Wold, M. Gochin, L. Spicer, D. Lowry, and M. Kennedy. 1999. Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: Chemical shift mapping and N-15 NMR relaxation studies. Biochemistry 38(46), 15116-15128. doi:10.1021/bi991755p

1998

  • 1998. Human nucleotide excision repair protein XPA: Extended X-ray absorption fine-structure evidence for a metal-binding domain. Protein Science.
  • Buchko, G. 1998. Structural features of the minimal DNA binding domain (M98-F219) of human nucleotide excision repair protein XPA. Nucleic Acids Research 26(11), 2779-2788. doi:10.1093/nar/26.11.2779
  • Buchko, G., A. Rozek, D. W. Hoyt, R. Cushley, and M. Kennedy. 1998. The use of sodium dodecyl sulfate to model the apolipoprotein environment. Evidence for peptide-SDS complexes using pulsed-field-gradient NMR spectroscopy. Biochimica Et Biophysica Acta-Lipids and Lipid Metabolism 1392(1), 101-108. doi:10.1016/S0005-2760(98)00028-9

1997

  • 1997. Conformational studies of the N-terminal lipid-associating domain of human apolipoprotein C-I by CD and H-1 NMR spectroscopy. Protein Science.
  • 1997. High resolution 1H NMR spectra of human apolipoprotein C-III2 using DPC to model the lipoprotein environment. Protein and Peptide Letters.
  • 1997. High resolution H-1 NMR spectra of human apolipoprotein C-III2 using DPC to model the lipoprotein environment. Protein and Peptide Letters.
  • 1997. Human nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a synthetic peptide fragment corresponding to the zinc-binding domain (101-141). Journal of Biomolecular Structure and Dynamics.
  • Buchko, G., S. Ni, B. Thrall, and M. Kennedy. 1997. Human nucleotide excision repair protein XPA: Expression and NMR backbone assignments of the 14.7 kDa minimal damaged DNA binding domain (Met(98)-Phe(219)). Journal of Biomolecular Nmr 10(3), 313-314. doi:10.1023/A:1018321319578
  • 1997. Human nucleotide excision repair protein XPA: Expression and NMR backbone assignments of the 14.7 kDa minimal damaged DNA binding domain (Met98-Phe219). Journal of Biomolecular NMR.
  • 1997. Human nucleotide excision repair protein XPA: H-1 NMR and CD solution studies of a synthetic peptide fragment corresponding to the zinc-binding domain (101-141). Journal of Biomolecular Structure & Dynamics.
  • Shaw, R., G. Buchko, G. Wang, A. Rozek, W. Treleaven, H. Mantsch, and R. Cushley. 1997. Infrared spectroscopy of human apolipoprotein fragments in SDS/D2O: Relative lipid-binding affinities and a novel amide I assignment. Biochemistry 36(47), 14531-14538. doi:10.1021/bi970558s

1996

  • 1996. 1H, 13C and 15N Nuclear magnetic resonance analysis and chemical features of the two main radical oxidation products of 2′-deoxyguanosine: Oxazolone and imidazolone nucleosides. Journal of the Chemical Society. Perkin Transactions 2.
  • 1996. Conformational studies of an amphipathic peptide corresponding to human apolipoprotein A-II residues 18-30 with a C-terminal lipid binding motif EWLNS. International Journal of Peptide and Protein Research.
  • Raoul, S., M. Berger, G. Buchko, P. Joshi, B. Morin, M. Weinfeld, and J. Cadet. 1996. H-1, C-13 and N-15 nuclear magnetic resonance analysis and chemical features of the two main radical oxidation products of 2'-deoxyguanosine: Oxazolone and imidazolone nucleosides. Journal of the Chemical Society-Perkin Transactions 2(3), 371-381. doi:10.1039/p29960000371
  • 1996. Structural studies of a peptide activator of human lecithin-cholesterol acyltransferase. Journal of Biological Chemistry.

1995

  • 1995. A STRUCTURAL COMPARISON OF 2 PEPTIDES CORRESPONDING TO HUMAN AND BABOON APOLIPOPROTEIN-C-1 RESIDUES 1-38. Journal of Cellular Biochemistry.
  • Rozek, A., G. Buchko, and R. Cushley. 1995. CONFORMATION OF 2 PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN-C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYL-SULFATE BY CD AND NMR-SPECTROSCOPY. Biochemistry 34(22), 7401-7408. doi:10.1021/bi00022a013
  • 1995. Hydroxyl and one-electron oxidation mediated reactions of the purine bases of DNA and model compounds: Mechanistic aspects. Radiation Damage in DNA: Structure/function Relationships At Early Times.
  • Buchko, G., J. Wagner, J. Cadet, S. Raoul, and M. Weinfeld. 1995. METHYLENE BLUE-MEDIATED PHOTOOXIDATION OF 7,8-DIHYDRO-8-OXO-2'-DEOXYGUANOSINE. Biochimica Et Biophysica Acta-Gene Structure and Expression 1263(1), 17-24. doi:10.1016/0167-4781(95)00078-U
  • 1995. NMR structural studies of amphipathic helices. Bulletin of Magnetic Resonance, Vol 17, Nos 1-4, December 1995.
  • Buchko, G., J. Cadet, B. Morin, and M. Weinfeld. 1995. PHOTOOXIDATION OF D(TPG) BY RIBOFLAVIN AND METHYLENE-BLUE - ISOLATION AND CHARACTERIZATION OF THYMIDYLYL-(3',5')-2-AMINO-5-[(2-DEOXY-BETA-D-ERYTHRO-PENTOFURANOSYL)AMINO]-4H-IMIDAZOL-4-ONE AND ITS PRIMARY DECOMPOSITION PRODUCT THYMIDYLYL-(3',5')-2,2-DIAMINO-4-[(2-DEOXY-BETA-D-ERYTHRO-PENTOFURANOSYL)AMINO]-5(2H)-OXAZOLONE. Nucleic Acids Research 23(19), 3954-3961. doi:10.1093/nar/23.19.3954
  • 1995. Photochemical and radical induced damage to DNA. Ozone Sun Cancer.
  • 1995. SEQUENCE-SPECIFIC H-1-NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF A LIPID-ASSOCIATING PEPTIDE FROM HUMAN APOC-I - AN NMR-STUDY OF AN AMPHIPATHIC HELIX MOTIF. Peptide Research.
  • 1995. Sequence-specific 1H NMR assignments and secondary structure of a lipid-associating peptide from human ApoC-I: An NMR study of an amphipathic helix motif. Peptide Research.
  • 1995. The use of photosensitizers to selectively generate radiation-induced guanine decomposition products. Radiation Damage in DNA: Structure/function Relationships At Early Times.

1994

  • Cadet, J., M. Berger, G. Buchko, P. Joshi, S. Raoul, and J. Ravanat. 1994. 2,2-DIAMINO-4-[(3,5-DI-O-ACETYL-2-DEOXY-BETA-D-ERYTHROPENTOFURANOSYL) AMINO]-5-(2H)-OXAZOLONE - A NOVEL AND PREDOMINANT RADICAL OXIDATION-PRODUCT OF 3',5'-DI-O-ACETYL-2'-DEOXYGUANOSINE. Journal of the American Chemical Society 116(16), 7403-7404. doi:10.1021/ja00095a052
  • 1994. 2,2-Diamino-4-[(3,5-di-O-acetyl-2-deoxy-β-D-erythro- pentofuranosyl)amino]-5-(2H)-oxazolone: A novel and predominant radical oxidation product of 3',5'-Di-O-acetyl-2'-deoxyguanosine. Journal of the American Chemical Society.
  • 1994. SINGLET OXYGEN DNA-DAMAGE - CHROMATOGRAPHIC AND MASS-SPECTROMETRIC ANALYSIS OF DAMAGE PRODUCTS. Oxygen Radicals in Biological Systems, Pt D.
  • Cadet, J., J. Ravanat, G. Helen, H. Yeo, and B. Ames. 1994. Singlet oxygen DNA damage: Chromatographic and mass spectrometric analysis of damage products. Methods in Enzymology, 79-88. doi:10.1016/0076-6879(94)34079-X

1993

  • Buchko, G. and M. Weinfeld. 1993. Influence of nitrogen, oxygen, and nitroimidazole radiosensitizers on DNA damage induced by ionizing radiation. Biochemistry 32(9), 2186-2193. doi:10.1021/bi00060a009
  • 1993. CHARACTERIZATION OF GAMMA-RADIATION INDUCED DECOMPOSITION PRODUCTS OF THYMIDINE-CONTAINING DINUCLEOSIDE MONOPHOSPHATES BY NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY. Journal of Biomolecular Structure & Dynamics.
  • Baleja, J., G. Buchko, M. Weinfeld, and B. Sykes. 1993. Characterization of y-radiation induced decomposition products of thymidine-containing dinucleoside monophosphates by nuclear magnetic resonance spectroscopy. Journal of Biomolecular Structure and Dynamics 10(4), 747-762. doi:10.1080/07391102.1993.10508004
  • Weinfeld, M., K. Soderlind, and G. Buchko. 1993. INFLUENCE OF NUCLEIC-ACID BASE AROMATICITY ON SUBSTRATE REACTIVITY WITH ENZYMES ACTING ON SINGLE-STRANDED-DNA. Nucleic Acids Research 21(3), 621-626. doi:10.1093/nar/21.3.621
  • Buchko, G., J. Cadet, J. Ravanat, and P. Labataille. 1993. ISOLATION AND CHARACTERIZATION OF A NEW PRODUCT PRODUCED BY IONIZING IRRADIATION AND TYPE-I PHOTOSENSITIZATION OF 2'-DEOXYGUANOSINE IN OXYGEN-SATURATED AQUEOUS-SOLUTION - (2S)-2,5'-ANHYDRO-1-(2'-DEOXY-BETA-D-ERYTHRO-PENTOFURANOSYL)-5-GUANIDINYLIDENE-2-HYDROXY-4-OXOIMIDAZOLIDINE. International Journal of Radiation Biology 63(6), 669-676. doi:10.1080/09553009314552061
  • 1993. PHOTOOXIDATION REACTIONS OF NUCLEIC-ACIDS. Frontiers of Photobiology.
  • 1993. Postlabelling methods for the detection of apurinic sites and radiation-induced DNA damage. IARC scientific publications.

1992

  • Buchko, G. and J. Cadet. 1992. IDENTIFICATION OF 2-DEOXY-D-RIBONO-1,4-LACTONE AT THE SITE OF BENZOPHENONE PHOTOSENSITIZED RELEASE OF GUANINE IN 2'-DEOXYGUANOSINE AND THYMIDYLYL-(3'-5')-2'-DEOXYGUANOSINE. Canadian Journal of Chemistry-Revue Canadienne De Chimie 70(6), 1827-1832. doi:10.1139/v92-226
  • Buchko, G., J. Cadet, M. Berger, and J. Revant. 1992. PHOTOOXIDATION OF D(TPG) BY PHTHALOCYANINES AND RIBOFLAVIN - ISOLATION AND CHARACTERIZATION OF DINUCLEOSIDE MONOPHOSPHATES CONTAINING THE 4R-ASTERISK AND 4S-ASTERISK DIASTEREOISOMERS OF 4,8-DIHYDRO-4-HYDROXY-8-OXO-2'-DEOXYGUANOSINE. Nucleic Acids Research 20(18), 4847-4851. doi:10.1093/nar/20.18.4847
  • Lafortune, F., G. Buchko, F. Hruska, K. Sadana, K. Standing, and J. Westmore. 1992. TIME-OF-FLIGHT SECONDARY ION MASS-SPECTROMETRY OF ISOMERIC O-ALKYLTHYMIDINES. Nucleosides & Nucleotides 11(7), 1305-1324. doi:10.1080/07328319208021175

1991

  • 1991. PHOTOOXIDATION OF 2'-DEOXYGUANOSINE BY PHTHALOCYANINES AND NAPHTHALOCYANINES - DETERMINATION OF THE RATIO OF TYPE-I AND TYPE-II MECHANISMS. Journal De Chimie Physique Et De Physico-Chimie Biologique.

1990

  • Buchko, G., F. Hruska, and K. Sadana. 1990. SYNTHESIS AND PROPERTIES OF DNA OLIGOMERS CONTAINING AN O4-ETHYLATED THYMINE - D(E4TPA), D(APE4T), D(APE4TPA), AND D(TPE4TPT)1. Canadian Journal of Chemistry-Revue Canadienne De Chimie 68(11), 2011-2021. doi:10.1139/v90-308
  • 1990. Synthesis and properties of DNA oligomers containing an O4-ethylated thymine. d(e4TpA), d(Ape4T), d(Ape4TpA), and d(Tpe4TpT). Canadian Journal of Chemistry.

1989

  • Buchko, G., F. Hruska, and K. Sadana. 1989. AN NMR-STUDY OF DINUCLEOSIDE MONOPHOSPHATES WITH AN O4-ETHYLATED THYMINE - D(E4TPT) AND D(TPE4T). Canadian Journal of Chemistry-Revue Canadienne De Chimie 67(1), 109-119. doi:10.1139/v89-019
  • 1989. An NMR study of dinucleoside monophosphates with an O4-ethylated thymine. d(e4TpT) and d(Tpe4T). Canadian Journal of Chemistry.
  • Buchko, G., F. Hruska, and K. Sadana. 1989. STRUCTURAL STUDIES OF OLIGONUCLEOTIDES WITH AN O4-ISOPROPYLATED THYMINE - D(I4TPT), D(TPI4T), AND D(TPI4TPT). Canadian Journal of Chemistry-Revue Canadienne De Chimie 67(8), 1344-1353. doi:10.1139/v89-206

1988

  • Birnbaum, G., K. Sadana, M. Razi, T. Lee, R. Sebastian, G. Buchko, and F. Hruska. 1988. CARCINOGENIC ALKYLATION OF NUCLEIC-ACID BASES - SOLID-STATE AND SOLUTION STUDIES OF 0-2-ISOPROPYL-2'-DEOXYTHYMIDINE. Canadian Journal of Chemistry-Revue Canadienne De Chimie 66(7), 1628-1634. doi:10.1139/v88-264