Karen Anderson, PhD
Research & Publications
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Research Summary
The primary emphasis focuses on developing an understanding of enzymatic reactions and receptor-ligand interactions at a molecular level. The approach is to use a combination of structural techniques including rapid transient kinetics, NMR, and xRay crystallography. This allows a quantitative and structural basis for understanding how proteins work at a molecular level.
Our ultimate goal in this research is to develop an in-depth mechanistic understanding of how enzymes function and thereby provide a more effective means of modulating their function. This approach has been used to examine a number of enzyme mechanisms including EPSP synthase, tryptophan synthase, PABA synthase, LAR-tyrosine phosphatase, and HIV reverse transcriptase. We have recently uncovered some interesting mechanistic features of HIV reverse transcriptase which may ultimately aid in the design of better therapeutic agents for the treatment of AIDS.
Specialized Terms: Enzyme function; Anti-viral agents
Extensive Research Description
Also ongoing are studies to understanding the molecular mechanisms of normal and aberrant protein signaling and the effects of selectively guided anticancer drugs such as Iressa and Gleevec. Important molecular targets include EGFR, HER-2, PDGFRb, and c-kit receptor tyrosine kinases. Another area of focus involves investigating the mechanisms of HIV reverse transcriptase as well as drug resistance and toxicity that may ultimately aid in the design of better therapeutic agents for the treatment of AIDS.
Coauthors
Research Interests
Molecular Biology; Pharmacology; Anti-Retroviral Agents; HIV Reverse Transcriptase; Multifunctional Enzymes
Selected Publications
- Proof-of-concept studies with a computationally designed Mpro inhibitor as a synergistic combination regimen alternative to PaxlovidPapini C, Ullah I, Ranjan A, Zhang S, Wu Q, Spasov K, Zhang C, Mothes W, Crawford J, Lindenbach B, Uchil P, Kumar P, Jorgensen W, Anderson K. Proof-of-concept studies with a computationally designed Mpro inhibitor as a synergistic combination regimen alternative to Paxlovid. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2320713121. PMID: 38621119, PMCID: PMC11046628, DOI: 10.1073/pnas.2320713121.
- Exploring novel HIV‐1 reverse transcriptase inhibitors with drug‐resistant mutants: A double mutant surpriseHollander K, Chan A, Frey K, Hunker O, Ippolito J, Spasov K, Yeh Y, Jorgensen W, Ho Y, Anderson K. Exploring novel HIV‐1 reverse transcriptase inhibitors with drug‐resistant mutants: A double mutant surprise. Protein Science 2023, 32: e4814. PMID: 37861472, PMCID: PMC10659932, DOI: 10.1002/pro.4814.
- A High-Throughput, High-Containment Human Primary Epithelial Airway Organ-on-Chip Platform for SARS-CoV-2 Therapeutic ScreeningFisher C, Medie F, Luu R, Gaibler R, Mulhern T, Miller C, Zhang C, Rubio L, Marr E, Vijayakumar V, Gabriel E, Quezada L, Zhang C, Anderson K, Jorgensen W, Alladina J, Medoff B, Borenstein J, Gard A. A High-Throughput, High-Containment Human Primary Epithelial Airway Organ-on-Chip Platform for SARS-CoV-2 Therapeutic Screening. Cells 2023, 12: 2639. PMID: 37998374, PMCID: PMC10669988, DOI: 10.3390/cells12222639.
- Covalent and noncovalent strategies for targeting Lys102 in HIV-1 reverse transcriptasePrucha G, Henry S, Hollander K, Carter Z, Spasov K, Jorgensen W, Anderson K. Covalent and noncovalent strategies for targeting Lys102 in HIV-1 reverse transcriptase. European Journal Of Medicinal Chemistry 2023, 262: 115894. PMID: 37883896, PMCID: PMC10872499, DOI: 10.1016/j.ejmech.2023.115894.
- Noncanonical HPV carcinogenesis drives radiosensitization of head and neck tumorsSchrank T, Kothari A, Weir W, Stepp W, Rehmani H, Liu X, Wang X, Sewell A, Li X, Tasoulas J, Kim S, Yarbrough G, Xie Y, Flamand Y, Marur S, Hayward M, Wu D, Burtness B, Anderson K, Baldwin A, Yarbrough W, Issaeva N. Noncanonical HPV carcinogenesis drives radiosensitization of head and neck tumors. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2216532120. PMID: 37523561, PMCID: PMC10410762, DOI: 10.1073/pnas.2216532120.
- Tackling FGFR3-driven bladder cancer with a promising synergistic FGFR/HDAC targeted therapyWang Z, Muthusamy V, Petrylak D, Anderson K. Tackling FGFR3-driven bladder cancer with a promising synergistic FGFR/HDAC targeted therapy. Npj Precision Oncology 2023, 7: 70. PMID: 37479885, PMCID: PMC10362036, DOI: 10.1038/s41698-023-00417-5.
- Design, synthesis, and biological testing of biphenylmethyloxazole inhibitors targeting HIV-1 reverse transcriptaseCarter Z, Hollander K, Spasov K, Anderson K, Jorgensen W. Design, synthesis, and biological testing of biphenylmethyloxazole inhibitors targeting HIV-1 reverse transcriptase. Bioorganic & Medicinal Chemistry Letters 2023, 84: 129216. PMID: 36871704, PMCID: PMC10278203, DOI: 10.1016/j.bmcl.2023.129216.
- Yale Cancer Center Precision Medicine Tumor Board: one tumour, multiple targetsStewart T, Finberg K, Walther Z, Sklar JL, Hafez N, Eder JP, Anderson K, Wilson F, Goldberg SB. Yale Cancer Center Precision Medicine Tumor Board: one tumour, multiple targets. The Lancet Oncology 2018, 19: 1567-1568. PMID: 32956641, DOI: 10.1016/s1470-2045(18)30759-9.
- APOBEC as an Endogenous Mutagen in Cancers of the Head and NeckSasaki T, Issaeva N, Yarbrough W, Anderson K. APOBEC as an Endogenous Mutagen in Cancers of the Head and Neck. 2018, 275-292. DOI: 10.1007/978-3-319-78762-6_10.
- Understanding the molecular mechanism of substrate channeling and domain communication in protozoal bifunctional TS-DHFRAnderson K. Understanding the molecular mechanism of substrate channeling and domain communication in protozoal bifunctional TS-DHFR. Protein Engineering Design And Selection 2017, 30: 253-261. PMID: 28338744, PMCID: PMC6438133, DOI: 10.1093/protein/gzx004.
- Data publication with the structural biology data grid supports live analysisMeyer PA, Socias S, Key J, Ransey E, Tjon EC, Buschiazzo A, Lei M, Botka C, Withrow J, Neau D, Rajashankar K, Anderson KS, Baxter RH, Blacklow SC, Boggon TJ, Bonvin AM, Borek D, Brett TJ, Caflisch A, Chang CI, Chazin WJ, Corbett KD, Cosgrove MS, Crosson S, Dhe-Paganon S, Di Cera E, Drennan CL, Eck MJ, Eichman BF, Fan QR, Ferré-D'Amaré AR, Christopher Fromme J, Garcia KC, Gaudet R, Gong P, Harrison SC, Heldwein EE, Jia Z, Keenan RJ, Kruse AC, Kvansakul M, McLellan JS, Modis Y, Nam Y, Otwinowski Z, Pai EF, Pereira PJ, Petosa C, Raman CS, Rapoport TA, Roll-Mecak A, Rosen MK, Rudenko G, Schlessinger J, Schwartz TU, Shamoo Y, Sondermann H, Tao YJ, Tolia NH, Tsodikov OV, Westover KD, Wu H, Foster I, Fraser JS, Maia FR, Gonen T, Kirchhausen T, Diederichs K, Crosas M, Sliz P. Data publication with the structural biology data grid supports live analysis. Nature Communications 2016, 7: 10882. PMID: 26947396, PMCID: PMC4786681, DOI: 10.1038/ncomms10882.
- Abstract 2436: Understanding the molecular mechanism of targeted kinase inhibitor resistance mediated by the FGFR1 gatekeeper mutationSohl C, Ryan M, Luo B, Frey K, Anderson K. Abstract 2436: Understanding the molecular mechanism of targeted kinase inhibitor resistance mediated by the FGFR1 gatekeeper mutation. Cancer Research 2015, 75: 2436-2436. DOI: 10.1158/1538-7445.am2015-2436.
- Human PrimPol: A Novel Mechanism of Antiviral ToxicityMislak A, Anderson K. Human PrimPol: A Novel Mechanism of Antiviral Toxicity. The FASEB Journal 2015, 29 DOI: 10.1096/fasebj.29.1_supplement.710.23.
- Biochemical and Functional Characterization of the Mutagenic Cytidine Deaminase, APOBEC3BSasaki T, Anderson K. Biochemical and Functional Characterization of the Mutagenic Cytidine Deaminase, APOBEC3B. The FASEB Journal 2015, 29 DOI: 10.1096/fasebj.29.1_supplement.573.48.
- Recent Findings on the Mechanisms Involved in Tenofovir ResistanceIyidogan P, Anderson K. Recent Findings on the Mechanisms Involved in Tenofovir Resistance. Antiviral Chemistry And Chemotherapy 2014, 23: 217-222. PMID: 23744599, PMCID: PMC4077986, DOI: 10.3851/imp2628.
- Current Perspectives on HIV-1 Antiretroviral Drug ResistanceIyidogan P, Anderson K. Current Perspectives on HIV-1 Antiretroviral Drug Resistance. Viruses 2014, 6: 4095-4139. PMID: 25341668, PMCID: PMC4213579, DOI: 10.3390/v6104095.
- Temporal resolution of protein signaling (473.1)Anderson K, Sohl C, Luo B, Mo S, Kim Y, Apetri M, Lew E, Furdui C, Schlessinger J. Temporal resolution of protein signaling (473.1). The FASEB Journal 2014, 28 DOI: 10.1096/fasebj.28.1_supplement.473.1.
- Correction to Bifunctional Inhibition of Human Immunodeficiency Virus Type 1 Reverse Transcriptase: Mechanism and Proof-of-Concept as a Novel Therapeutic Design StrategyBailey C, Sullivan T, Iyidogan P, Tirado-Rives J, Chung R, Ruiz-Caro J, Mohamed E, Jorgensen W, Hunter R, Anderson K. Correction to Bifunctional Inhibition of Human Immunodeficiency Virus Type 1 Reverse Transcriptase: Mechanism and Proof-of-Concept as a Novel Therapeutic Design Strategy. Journal Of Medicinal Chemistry 2013, 56: 8953-8953. PMCID: PMC4301842, DOI: 10.1021/jm401535f.
- Design, Synthesis, and Antiviral Evaluation of Chimeric Inhibitors of HIV Reverse TranscriptaseIyidogan P, Sullivan T, Chordia M, Frey K, Anderson K. Design, Synthesis, and Antiviral Evaluation of Chimeric Inhibitors of HIV Reverse Transcriptase. ACS Medicinal Chemistry Letters 2013, 4: 1183-1188. PMID: 24900627, PMCID: PMC4027223, DOI: 10.1021/ml4002979.
- Pre-steady state kinetic analysis of cyclobutyl derivatives of 2′-deoxyadenosine 5′-triphosphate as inhibitors of HIV-1 reverse transcriptaseKim J, Wang L, Li Y, Becnel K, Frey K, Garforth S, Prasad V, Schinazi R, Liotta D, Anderson K. Pre-steady state kinetic analysis of cyclobutyl derivatives of 2′-deoxyadenosine 5′-triphosphate as inhibitors of HIV-1 reverse transcriptase. Bioorganic & Medicinal Chemistry Letters 2012, 22: 4064-4067. PMID: 22595174, PMCID: PMC3362660, DOI: 10.1016/j.bmcl.2012.04.078.
- Active site residues critical for flavin binding and 5,6‐dimethylbenzimidazole biosynthesis in the flavin destructase enzyme BluBYu T, Mok K, Kennedy K, Valton J, Anderson K, Walker G, Taga M. Active site residues critical for flavin binding and 5,6‐dimethylbenzimidazole biosynthesis in the flavin destructase enzyme BluB. Protein Science 2012, 21: 839-849. PMID: 22528544, PMCID: PMC3403419, DOI: 10.1002/pro.2068.
- Balancing Antiviral Potency and Host Toxicity: Identifying a Nucleotide Inhibitor with an Optimal Kinetic Phenotype for HIV-1 Reverse TranscriptaseSohl C, Kasiviswanathan R, Kim J, Pradere U, Schinazi R, Copeland W, Mitsuya H, Baba M, Anderson K. Balancing Antiviral Potency and Host Toxicity: Identifying a Nucleotide Inhibitor with an Optimal Kinetic Phenotype for HIV-1 Reverse Transcriptase. Molecular Pharmacology 2012, 82: 125-133. PMID: 22513406, PMCID: PMC3382833, DOI: 10.1124/mol.112.078758.
- Lethal Mutagenesis as an Unconventional Approach to Combat HIVIyidogan P, Anderson K. Lethal Mutagenesis as an Unconventional Approach to Combat HIV. 2011, 50: 283-306. DOI: 10.1002/9783527635955.ch11.
- [d4U]-Spacer-[HI-236] double-drug inhibitors of HIV-1 reverse-transcriptaseYounis Y, Hunter R, Muhanji C, Hale I, Singh R, Bailey C, Sullivan T, Anderson K. [d4U]-Spacer-[HI-236] double-drug inhibitors of HIV-1 reverse-transcriptase. Bioorganic & Medicinal Chemistry 2010, 18: 4661-4673. PMID: 20605472, PMCID: PMC2964380, DOI: 10.1016/j.bmc.2010.05.025.
- 102 Yeast homologues of disease mutations in DNA polymerase gamma cause mtDNA depletion and mutagenesisStumpf J, Spell D, Stillwagon M, Anderson K, Copeland W. 102 Yeast homologues of disease mutations in DNA polymerase gamma cause mtDNA depletion and mutagenesis. Mitochondrion 2010, 10: 228. DOI: 10.1016/j.mito.2009.12.094.
- mip1 containing mutations associated with mitochondrial disease causes mutagenesis and depletion of mtDNA in Saccharomyces cerevisiaeStumpf J, Bailey C, Spell D, Stillwagon M, Anderson K, Copeland W. mip1 containing mutations associated with mitochondrial disease causes mutagenesis and depletion of mtDNA in Saccharomyces cerevisiae. Human Molecular Genetics 2010, 19: 2123-2133. PMID: 20185557, PMCID: PMC2865372, DOI: 10.1093/hmg/ddq089.
- 8.18 Detection of Novel Enzyme IntermediatesFurdui C, Anderson K. 8.18 Detection of Novel Enzyme Intermediates. 2010, 663-688. DOI: 10.1016/b978-008045382-8.00158-1.
- C-2-Aryl O-substituted HI-236 derivatives as non-nucleoside HIV-1 reverse-transcriptase inhibitorsHunter R, Younis Y, Muhanji C, Curtin T, Naidoo K, Petersen M, Bailey C, Basavapathruni A, Anderson K. C-2-Aryl O-substituted HI-236 derivatives as non-nucleoside HIV-1 reverse-transcriptase inhibitors. Bioorganic & Medicinal Chemistry 2008, 16: 10270-10280. PMID: 18996020, PMCID: PMC2639753, DOI: 10.1016/j.bmc.2008.10.048.
- Epidermal Growth Factor Receptor Mutants from Human Lung Cancers Exhibit Enhanced Catalytic Activity and Increased Sensitivity to GefitinibMulloy R, Ferrand A, Kim Y, Sordella R, Bell D, Haber D, Anderson K, Settleman J. Epidermal Growth Factor Receptor Mutants from Human Lung Cancers Exhibit Enhanced Catalytic Activity and Increased Sensitivity to Gefitinib. Cancer Research 2007, 67: 2325-2330. PMID: 17332364, DOI: 10.1158/0008-5472.can-06-4293.
- FEP-Guided Selection of Bicyclic Heterocycles in Lead Optimization for Non-Nucleoside Inhibitors of HIV-1 Reverse Transcriptase [J. Am. Chem. Soc. 2006, 128, 15372−15373].Kim J, Hamilton A, Bailey C, Domaoal R, Wang L, Anderson K, Jorgensen W. FEP-Guided Selection of Bicyclic Heterocycles in Lead Optimization for Non-Nucleoside Inhibitors of HIV-1 Reverse Transcriptase [J. Am. Chem. Soc. 2006, 128, 15372−15373]. Journal Of The American Chemical Society 2007, 129: 3027-3027. DOI: 10.1021/ja076881s.
- Alternative Synthetic Routes to 2′,3′‐Didehydro‐2′,3′‐dideoxy‐5‐hydroxymethyluridine.Chung R, Anderson K. Alternative Synthetic Routes to 2′,3′‐Didehydro‐2′,3′‐dideoxy‐5‐hydroxymethyluridine. ChemInform 2007, 38: no-no. DOI: 10.1002/chin.200710216.
- [d4U]-butyne-[HI-236] as a non-cleavable, bifunctional NRTI/NNRTI HIV-1 reverse-transcriptase inhibitorHunter R, Muhanji C, Hale I, Bailey C, Basavapathruni A, Anderson K. [d4U]-butyne-[HI-236] as a non-cleavable, bifunctional NRTI/NNRTI HIV-1 reverse-transcriptase inhibitor. Bioorganic & Medicinal Chemistry Letters 2007, 17: 2614-2617. PMID: 17317163, DOI: 10.1016/j.bmcl.2007.01.107.
- Alternative synthetic routes to 2′,3′-didehydro-2′,3′-dideoxy-5-hydroxymethyluridineChung R, Anderson K. Alternative synthetic routes to 2′,3′-didehydro-2′,3′-dideoxy-5-hydroxymethyluridine. Tetrahedron Letters 2006, 47: 8361-8363. DOI: 10.1016/j.tetlet.2006.09.083.
- Optimization of Diarylamines as Non‐Nucleoside Inhibitors of HIV‐1 Reverse Transcriptase.Ruiz‐Caro J, Basavapathruni A, Kim J, Bailey C, Wang L, Anderson K, Hamilton A, Jorgensen W. Optimization of Diarylamines as Non‐Nucleoside Inhibitors of HIV‐1 Reverse Transcriptase. ChemInform 2006, 37: no-no. DOI: 10.1002/chin.200618152.
- Developing novel nonnucleoside HIV-1 reverse transcriptase inhibitors: beyond the butterfly.Basavapathruni A, Anderson K. Developing novel nonnucleoside HIV-1 reverse transcriptase inhibitors: beyond the butterfly. Current Pharmaceutical Design 2006, 12: 1857-65. PMID: 16724952, DOI: 10.2174/138161206776873617.
- The role of the proteome in catalysis and regulationAnderson K, Mattevi A. The role of the proteome in catalysis and regulation. Current Opinion In Structural Biology 2004, 14: 639-641. DOI: 10.1016/j.sbi.2004.10.014.
- 2′,3′‐Didehydro‐2′,3′‐dideoxynucleosides Are Degraded to Furfuryl Alcohol under Acidic Conditions.Shi J, Ray A, Mathew J, Anderson K, Chu C, Schinazi R. 2′,3′‐Didehydro‐2′,3′‐dideoxynucleosides Are Degraded to Furfuryl Alcohol under Acidic Conditions. ChemInform 2004, 35: no-no. DOI: 10.1002/chin.200435215.
- Relationship between Antiviral Activity and Host Toxicity: Comparison of the Incorporation Efficiencies of 2′,3′-Dideoxy-5-Fluoro-3′-Thiacytidine-Triphosphate Analogs by Human Immunodeficiency Virus Type 1 Reverse Transcriptase and Human Mitochondrial DNA PolymeraseFeng J, Murakami E, Zorca S, Johnson A, Johnson K, Schinazi R, Furman P, Anderson K. Relationship between Antiviral Activity and Host Toxicity: Comparison of the Incorporation Efficiencies of 2′,3′-Dideoxy-5-Fluoro-3′-Thiacytidine-Triphosphate Analogs by Human Immunodeficiency Virus Type 1 Reverse Transcriptase and Human Mitochondrial DNA Polymerase. Antimicrobial Agents And Chemotherapy 2004, 48: 1300-1306. PMID: 15047533, PMCID: PMC375312, DOI: 10.1128/aac.48.4.1300-1306.2004.
- Detection and characterization of enzyme intermediates: utility of rapid chemical quench methodology and single enzyme turnover experimentsAnderson K. Detection and characterization of enzyme intermediates: utility of rapid chemical quench methodology and single enzyme turnover experiments. 2003, 19-48. DOI: 10.1093/oso/9780198524946.003.0002.
- Characterization of Novel Reverse Transcriptase and Other RNA-associated Catalytic Activities by Human DNA Polymerase γ IMPORTANCE IN MITOCHONDRIAL DNA REPLICATION*Murakami E, Feng J, Lee H, Hanes J, Johnson K, Anderson K. Characterization of Novel Reverse Transcriptase and Other RNA-associated Catalytic Activities by Human DNA Polymerase γ IMPORTANCE IN MITOCHONDRIAL DNA REPLICATION*. Journal Of Biological Chemistry 2003, 278: 36403-36409. PMID: 12857740, DOI: 10.1074/jbc.m306236200.
- Virally Encoded Polymerases as Targets for Chemotherapy: Application to HIV and HBVPainter G, Anderson K, Bouygues M, Joubert M, Liotta D. Virally Encoded Polymerases as Targets for Chemotherapy: Application to HIV and HBV. ChemInform 2002, 33: 256-256. DOI: 10.1002/chin.200248256.
- Catalysis and regulation: Bringing proteins to lifeAnderson K, Mattevi A. Catalysis and regulation: Bringing proteins to life. Current Opinion In Structural Biology 2002, 12: 695-697. DOI: 10.1016/s0959-440x(02)00403-7.
- Mechanistic Characterization of Toxoplasma gondiiThymidylate Synthase (TS-DHFR)-Dihydrofolate Reductase EVIDENCE FOR A TS INTERMEDIATE AND TS HALF-SITES REACTIVITY*Johnson E, Hinz W, Atreya C, Maley F, Anderson K. Mechanistic Characterization of Toxoplasma gondiiThymidylate Synthase (TS-DHFR)-Dihydrofolate Reductase EVIDENCE FOR A TS INTERMEDIATE AND TS HALF-SITES REACTIVITY*. Journal Of Biological Chemistry 2002, 277: 43126-43136. PMID: 12192007, DOI: 10.1074/jbc.m206523200.
- The Kinetic Mechanism of the Human Bifunctional Enzyme ATIC (5-Amino-4-imidazolecarboxamide Ribonucleotide Transformylase/Inosine 5′-Monophosphate Cyclohydrolase) A SURPRISING LACK OF SUBSTRATE CHANNELING*Bulock K, Beardsley G, Anderson K. The Kinetic Mechanism of the Human Bifunctional Enzyme ATIC (5-Amino-4-imidazolecarboxamide Ribonucleotide Transformylase/Inosine 5′-Monophosphate Cyclohydrolase) A SURPRISING LACK OF SUBSTRATE CHANNELING*. Journal Of Biological Chemistry 2002, 277: 22168-22174. PMID: 11948179, DOI: 10.1074/jbc.m111964200.
- Virally Encoded Polymerases as Targets for Chemotherapy: Application to HIV and HBVPainter G, Anderson K, Bouygues M, Joubert M, Liotta D. Virally Encoded Polymerases as Targets for Chemotherapy: Application to HIV and HBV. Anti-Infective Agents 2002, 1: 99-117. DOI: 10.2174/1568012023354974.
- Reverse TranscriptasesAnderson K. Reverse Transcriptases. 2002 DOI: 10.1002/0471203076.emm1230.
- Deoxythioguanosine triphosphate impairs HIV replication: a new mechanism for an old drugKRYNETSKAIA N, FENG J, KRYNETSKI E, GARCIA J, PANETTA J, ANDERSON K, EVANS W. Deoxythioguanosine triphosphate impairs HIV replication: a new mechanism for an old drug. The FASEB Journal 2001, 15: 1902-1908. PMID: 11532970, DOI: 10.1096/fj.01-0124com.
- Toxicity of Antiviral Nucleoside Analogs and the Human Mitochondrial DNA Polymerase*Johnson A, Ray A, Hanes J, Suo Z, Colacino J, Anderson K, Johnson K. Toxicity of Antiviral Nucleoside Analogs and the Human Mitochondrial DNA Polymerase*. Journal Of Biological Chemistry 2001, 276: 40847-40857. PMID: 11526116, DOI: 10.1074/jbc.m106743200.
- Insights into the Molecular Mechanism of Mitochondrial Toxicity by AIDS Drugs*Feng J, Johnson A, Johnson K, Anderson K. Insights into the Molecular Mechanism of Mitochondrial Toxicity by AIDS Drugs*. Journal Of Biological Chemistry 2001, 276: 23832-23837. PMID: 11328813, DOI: 10.1074/jbc.m101156200.
- MECHANISTIC STUDIES TO UNDERSTAND THE INHIBITION OF WILD TYPE AND MUTANT HIV-1 REVERSE TRANSCRIPTASE BY CARBOVIR-TRIPHOSPHATERay A, Anderson K. MECHANISTIC STUDIES TO UNDERSTAND THE INHIBITION OF WILD TYPE AND MUTANT HIV-1 REVERSE TRANSCRIPTASE BY CARBOVIR-TRIPHOSPHATE. Nucleosides Nucleotides & Nucleic Acids 2001, 20: 1247-1250. PMID: 11562995, DOI: 10.1081/ncn-100002528.
- Y265H Mutator Mutant of DNA Polymerase β PROPER GEOMETRIC ALIGNMENT IS CRITICAL FOR FIDELITY*Shah A, Li S, Anderson K, Sweasy J. Y265H Mutator Mutant of DNA Polymerase β PROPER GEOMETRIC ALIGNMENT IS CRITICAL FOR FIDELITY*. Journal Of Biological Chemistry 2001, 276: 10824-10831. PMID: 11154692, DOI: 10.1074/jbc.m008680200.
- Mechanism of Action of 1-β-d-2,6-Diaminopurine Dioxolane, a Prodrug of the Human Immunodeficiency Virus Type 1 Inhibitor 1-β-d-Dioxolane GuanosineFurman P, Jeffrey J, Kiefer L, Feng J, Anderson K, Borroto-Esoda K, Hill E, Copeland W, Chu C, Sommadossi J, Liberman I, Schinazi R, Painter G. Mechanism of Action of 1-β-d-2,6-Diaminopurine Dioxolane, a Prodrug of the Human Immunodeficiency Virus Type 1 Inhibitor 1-β-d-Dioxolane Guanosine. Antimicrobial Agents And Chemotherapy 2001, 45: 158-165. PMID: 11120959, PMCID: PMC90254, DOI: 10.1128/aac.45.1.158-165.2001.
- Insights into the HER-2 Receptor Tyrosine Kinase Mechanism and Substrate Specificity Using a Transient Kinetic Analysis †Jan A, Johnson E, Diamonti A, Carraway K, Anderson K. Insights into the HER-2 Receptor Tyrosine Kinase Mechanism and Substrate Specificity Using a Transient Kinetic Analysis †. Biochemistry 2000, 39: 9786-9803. PMID: 10933796, DOI: 10.1021/bi9924922.
- Energetics of S-Adenosylmethionine Synthetase Catalysis †McQueney M, Anderson K, Markham G. Energetics of S-Adenosylmethionine Synthetase Catalysis †. Biochemistry 2000, 39: 4443-4454. PMID: 10757994, DOI: 10.1021/bi992876s.
- An analysis of the catalytic cycle of HIV-1 reverse transcriptase: opportunities for chemotherapeutic intervention based on enzyme inhibition.Furman P, Painter G, Anderson K. An analysis of the catalytic cycle of HIV-1 reverse transcriptase: opportunities for chemotherapeutic intervention based on enzyme inhibition. Current Pharmaceutical Design 2000, 6: 547-67. PMID: 10788596, DOI: 10.2174/1381612003400777.
- Mechanism of Inhibition of the Human Immunodeficiency Virus Type 1 Reverse Transcriptase by d4TTP: an Equivalent Incorporation Efficiency Relative to the Natural Substrate dTTP †Vaccaro J, Parnell K, Terezakis S, Anderson K. Mechanism of Inhibition of the Human Immunodeficiency Virus Type 1 Reverse Transcriptase by d4TTP: an Equivalent Incorporation Efficiency Relative to the Natural Substrate dTTP †. Antimicrobial Agents And Chemotherapy 2000, 44: 217-221. PMID: 10602755, PMCID: PMC89660, DOI: 10.1128/aac.44.1.217-221.2000.
- Initiation of Minus-Strand DNA Synthesis by Human Immunodeficiency Virus Type 1 Reverse Transcriptase †Vaccaro J, Singh H, Anderson K. Initiation of Minus-Strand DNA Synthesis by Human Immunodeficiency Virus Type 1 Reverse Transcriptase †. Biochemistry 1999, 38: 15978-15985. PMID: 10625465, DOI: 10.1021/bi990945x.
- Crystallographic Studies of Phosphonate-Based α-Reaction Transition-State Analogues Complexed to Tryptophan Synthase † , ‡Sachpatzidis A, Dealwis C, Lubetsky J, Liang P, Anderson K, Lolis E. Crystallographic Studies of Phosphonate-Based α-Reaction Transition-State Analogues Complexed to Tryptophan Synthase † , ‡. Biochemistry 1999, 38: 12665-12674. PMID: 10504236, DOI: 10.1021/bi9907734.
- Mechanistic studies show that (−)‐FTC‐TP is a better inhibitor of HIV‐1 reverse transcriptase than 3TC‐TPFeng J, Shi J, Schinazi R, Anderson K. Mechanistic studies show that (−)‐FTC‐TP is a better inhibitor of HIV‐1 reverse transcriptase than 3TC‐TP. The FASEB Journal 1999, 13: 1511-1517. PMID: 10463941, DOI: 10.1096/fasebj.13.12.1511.
- Mechanistic Studies Examining the Efficiency and Fidelity of DNA Synthesis by the 3TC-Resistant Mutant (184V) of HIV-1 Reverse Transcriptase †Feng J, Anderson K. Mechanistic Studies Examining the Efficiency and Fidelity of DNA Synthesis by the 3TC-Resistant Mutant (184V) of HIV-1 Reverse Transcriptase †. Biochemistry 1999, 38: 9440-9448. PMID: 10413520, DOI: 10.1021/bi990709m.
- The Catalytic Mechanism of EPSP Synthase Revisited †Lewis J, Johnson K, Anderson K. The Catalytic Mechanism of EPSP Synthase Revisited †. Biochemistry 1999, 38: 7372-7379. PMID: 10353849, DOI: 10.1021/bi9830258.
- Using loop length variants to dissect the folding pathway of a four-helix-bundle protein 11Edited by P. E. WrightNagi A, Anderson K, Regan L. Using loop length variants to dissect the folding pathway of a four-helix-bundle protein 11Edited by P. E. Wright. Journal Of Molecular Biology 1999, 286: 257-265. PMID: 9931264, DOI: 10.1006/jmbi.1998.2474.
- [6] Fundamental mechanisms of substrate channelingAnderson K. [6] Fundamental mechanisms of substrate channeling. 1999, 308: 111-145. PMID: 10507003, DOI: 10.1016/s0076-6879(99)08008-8.
- Mechanistic Studies Comparing the Incorporation of (+) and (−) Isomers of 3TCTP by HIV-1 Reverse Transcriptase †Feng J, Anderson K. Mechanistic Studies Comparing the Incorporation of (+) and (−) Isomers of 3TCTP by HIV-1 Reverse Transcriptase †. Biochemistry 1998, 38: 55-63. PMID: 9890882, DOI: 10.1021/bi982340r.
- Catalytic Mechanism of Kdo8P Synthase: Transient Kinetic Studies and Evaluation of a Putative Reaction Intermediate †Liang P, Lewis J, Anderson K, Kohen A, D'Souza F, Benenson Y, Baasov T. Catalytic Mechanism of Kdo8P Synthase: Transient Kinetic Studies and Evaluation of a Putative Reaction Intermediate †. Biochemistry 1998, 37: 16390-16399. PMID: 9819231, DOI: 10.1021/bi981374w.
- Implication of the tRNA Initiation Step for Human Immunodeficiency Virus Type 1 Reverse Transcriptase in the Mechanism of 3‘-Azido-3‘-deoxythymidine (AZT) Resistance †Vaccaro J, Anderson K. Implication of the tRNA Initiation Step for Human Immunodeficiency Virus Type 1 Reverse Transcriptase in the Mechanism of 3‘-Azido-3‘-deoxythymidine (AZT) Resistance †. Biochemistry 1998, 37: 14189-14194. PMID: 9760256, DOI: 10.1021/bi9810353.
- Substrate Channeling and Domain−Domain Interactions in Bifunctional Thymidylate Synthase−Dihydrofolate Reductase †Liang P, Anderson K. Substrate Channeling and Domain−Domain Interactions in Bifunctional Thymidylate Synthase−Dihydrofolate Reductase †. Biochemistry 1998, 37: 12195-12205. PMID: 9724533, DOI: 10.1021/bi9803168.
- Kinetic Reaction Scheme for the Dihydrofolate Reductase Domain of the Bifunctional Thymidylate Synthase−Dihydrofolate Reductase from Leishmania major †Liang P, Anderson K. Kinetic Reaction Scheme for the Dihydrofolate Reductase Domain of the Bifunctional Thymidylate Synthase−Dihydrofolate Reductase from Leishmania major †. Biochemistry 1998, 37: 12206-12212. PMID: 9724534, DOI: 10.1021/bi9803170.
- Loop Closure and Intersubunit Communication in Tryptophan Synthase † , ‡Schneider T, Gerhardt E, Lee M, Liang P, Anderson K, Schlichting I. Loop Closure and Intersubunit Communication in Tryptophan Synthase † , ‡. Biochemistry 1998, 37: 5394-5406. PMID: 9548921, DOI: 10.1021/bi9728957.
- Leishmania major Pteridine Reductase 1 Belongs to the Short Chain Dehydrogenase Family: Stereochemical and Kinetic Evidence †Luba J, Nare B, Liang P, Anderson K, Beverley S, Hardy L. Leishmania major Pteridine Reductase 1 Belongs to the Short Chain Dehydrogenase Family: Stereochemical and Kinetic Evidence †. Biochemistry 1998, 37: 4093-4104. PMID: 9521731, DOI: 10.1021/bi972693a.
- Structure and Functional Relationships in Human pur HBeardsley G, Rayl E, Gunn K, Moroson B, Seow H, Anderson K, Vergis J, Fleming K, Worland S, Condon B, Davies J. Structure and Functional Relationships in Human pur H. 1998, 431: 221-226. PMID: 9598063, DOI: 10.1007/978-1-4615-5381-6_43.
- Detection and Identification of Transient Enzyme Intermediates Using Rapid Mixing, Pulsed-Flow Electrospray Mass Spectrometry †Paiva A, Tilton R, Crooks G, Huang L, Anderson K. Detection and Identification of Transient Enzyme Intermediates Using Rapid Mixing, Pulsed-Flow Electrospray Mass Spectrometry †. Biochemistry 1997, 36: 15472-15476. PMID: 9398276, DOI: 10.1021/bi971883i.
- RNA Dependent DNA Replication Fidelity of HIV-1 Reverse Transcriptase: Evidence of Discrimination between DNA and RNA Substrates †Kerr S, Anderson K. RNA Dependent DNA Replication Fidelity of HIV-1 Reverse Transcriptase: Evidence of Discrimination between DNA and RNA Substrates †. Biochemistry 1997, 36: 14056-14063. PMID: 9369477, DOI: 10.1021/bi971385+.
- Pre-Steady-State Kinetic Characterization of Wild Type and 3‘-Azido-3‘-deoxythymidine (AZT) Resistant Human Immunodeficiency Virus Type 1 Reverse Transcriptase: Implication of RNA Directed DNA Polymerization in the Mechanism of AZT Resistance †Kerr S, Anderson K. Pre-Steady-State Kinetic Characterization of Wild Type and 3‘-Azido-3‘-deoxythymidine (AZT) Resistant Human Immunodeficiency Virus Type 1 Reverse Transcriptase: Implication of RNA Directed DNA Polymerization in the Mechanism of AZT Resistance †. Biochemistry 1997, 36: 14064-14070. PMID: 9369478, DOI: 10.1021/bi9713862.
- Catalytic mechanism of KDO8P synthase. Pre-steady-state kinetic analysis using rapid chemical quench flow methodsLiang P, Kohen A, Baasov T, Anderson K. Catalytic mechanism of KDO8P synthase. Pre-steady-state kinetic analysis using rapid chemical quench flow methods. Bioorganic & Medicinal Chemistry Letters 1997, 7: 2463-2468. DOI: 10.1016/s0960-894x(97)10021-x.
- Pre-Steady-State Kinetic Analysis of the Trichodiene Synthase Reaction Pathway †Cane D, Chiu H, Liang P, Anderson K. Pre-Steady-State Kinetic Analysis of the Trichodiene Synthase Reaction Pathway †. Biochemistry 1997, 36: 8332-8339. PMID: 9204880, DOI: 10.1021/bi963018o.
- Pre-steady state kinetic analysis of the bifunctional human amino-imidazole carboxamide ribonucleotide formyltransferase/AMP cyclohydrolase (AICARFT/IMPCHase), a 10-formyltetrahydro-folate-requiring enzyme essential for de novo purine biosynthesisRayl E, Moroson B, Beardsley G, Anderson K. Pre-steady state kinetic analysis of the bifunctional human amino-imidazole carboxamide ribonucleotide formyltransferase/AMP cyclohydrolase (AICARFT/IMPCHase), a 10-formyltetrahydro-folate-requiring enzyme essential for de novo purine biosynthesis. Clinical Biochemistry 1997, 30: 275-276. DOI: 10.1016/s0009-9120(97)87769-7.
- Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitudeMunson M, Anderson K, Regan L. Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude. Structure 1997, 2: 77-87. PMID: 9080201, DOI: 10.1016/s1359-0278(97)00008-4.
- Surface point mutations that significantly alter the structure and stability of a protein's denatured stateSmith C, Bu Z, Engelman D, Regan L, Anderson K, Sturtevant J. Surface point mutations that significantly alter the structure and stability of a protein's denatured state. Protein Science 1996, 5: 2009-2019. PMID: 8897601, PMCID: PMC2143264, DOI: 10.1002/pro.5560051007.
- HIV-1 Reverse Transcriptase Resistance to Nonnucleoside Inhibitors †Spence R, Anderson K, Johnson K. HIV-1 Reverse Transcriptase Resistance to Nonnucleoside Inhibitors †. Biochemistry 1996, 35: 1054-1063. PMID: 8547241, DOI: 10.1021/bi952058+.
- Intersubunit Communication in Tryptophan Synthase by Carbon-13 and Fluorine-19 REDOR NMR †McDowell L, Lee M, McKay R, Anderson K, Schaefer J. Intersubunit Communication in Tryptophan Synthase by Carbon-13 and Fluorine-19 REDOR NMR †. Biochemistry 1996, 35: 3328-3334. PMID: 8605170, DOI: 10.1021/bi9518297.
- Observation of an aminoacrylate enzyme intermediate in the tryptophan synthase reaction by solid-state NMRMcDowell L, Lee M, Schaefer J, Anderson K. Observation of an aminoacrylate enzyme intermediate in the tryptophan synthase reaction by solid-state NMR. Journal Of The American Chemical Society 1995, 117: 12352-12353. DOI: 10.1021/ja00154a045.
- Kinetic Characterization of Channel Impaired Mutants of Tryptophan Synthase (∗)Anderson K, Kim A, Quillen J, Sayers E, Yang X, Miles E. Kinetic Characterization of Channel Impaired Mutants of Tryptophan Synthase (∗). Journal Of Biological Chemistry 1995, 270: 29936-29944. PMID: 8530393, DOI: 10.1074/jbc.270.50.29936.
- Reevaluating glyphosate as a transition-state inhibitor of EPSP synthase: identification of an EPSP synthase.EPSP.glyphosate ternary complex.Sammons R, Gruys K, Anderson K, Johnson K, Sikorski J. Reevaluating glyphosate as a transition-state inhibitor of EPSP synthase: identification of an EPSP synthase.EPSP.glyphosate ternary complex. Biochemistry 1995, 34: 6433-40. PMID: 7756274, DOI: 10.1021/bi00019a024.
- Crystallization and preliminary X‐ray investigation of the recombinant Trypanosoma brucei rhodesiense calmodulinEl‐Sayed N, Patton C, Harkins P, Fox R, Anderson K. Crystallization and preliminary X‐ray investigation of the recombinant Trypanosoma brucei rhodesiense calmodulin. Proteins Structure Function And Bioinformatics 1995, 21: 354-357. PMID: 7567957, DOI: 10.1002/prot.340210409.
- Expression of Human Cyclophilin‐40 and the Effect of the His141→Trp Mutation on Catalysis and Cyclosporin A BindingHoffmann K, Kakalis L, Anderson K, Armitage I, Handschumacher R. Expression of Human Cyclophilin‐40 and the Effect of the His141→Trp Mutation on Catalysis and Cyclosporin A Binding. The FEBS Journal 1995, 229: 188-193. PMID: 7744028, DOI: 10.1111/j.1432-1033.1995.0188l.x.
- Mechanism of Inhibition of HIV-1 Reverse Transcriptase by Nonnucleoside InhibitorsSpence R, Kati W, Anderson K, Johnson K. Mechanism of Inhibition of HIV-1 Reverse Transcriptase by Nonnucleoside Inhibitors. Science 1995, 267: 988-993. PMID: 7532321, PMCID: PMC7526747, DOI: 10.1126/science.7532321.
- Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ.Brown E, Marquardt J, Lee J, Walsh C, Anderson K. Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ. Biochemistry 1994, 33: 10638-45. PMID: 8075064, DOI: 10.1021/bi00201a010.
- Synthesis & characterization of N-amino-glyphosate as a potent analog inhibitor of E. coli EPSP synthase.Knowles W, Anderson K, Andrew S, Phillion D, Ream J, Johnson K, Sikorski J. Synthesis & characterization of N-amino-glyphosate as a potent analog inhibitor of E. coli EPSP synthase. Bioorganic & Medicinal Chemistry Letters 1993, 3: 2863-2868. DOI: 10.1016/s0960-894x(01)80780-0.
- Isolation and structural elucidation of a tetrahedral intermediate in the UDP-N-acetylglucosamine enolpyruvoyl transferase enzymic pathwayMarquardt J, Brown E, Walsh C, Anderson K. Isolation and structural elucidation of a tetrahedral intermediate in the UDP-N-acetylglucosamine enolpyruvoyl transferase enzymic pathway. Journal Of The American Chemical Society 1993, 115: 10398-10399. DOI: 10.1021/ja00075a081.
- EPSP synthase inhibitor design II. The importance of the 3-phosphate group for ligand binding at the shikimate-3-phosphate site & the identification of 3-malonate ethers as novel 3-phosphate mimics.Miller M, Anderson K, Braccolino D, Cleary D, Gruys K, Han C, Lin K, Pansegrau P, Ream J, Sammons R, Sikorski J. EPSP synthase inhibitor design II. The importance of the 3-phosphate group for ligand binding at the shikimate-3-phosphate site & the identification of 3-malonate ethers as novel 3-phosphate mimics. Bioorganic & Medicinal Chemistry Letters 1993, 3: 1435-1440. DOI: 10.1016/s0960-894x(01)80425-x.
- Mechanism and fidelity of HIV reverse transcriptase.Kati W, Johnson K, Jerva L, Anderson K. Mechanism and fidelity of HIV reverse transcriptase. Journal Of Biological Chemistry 1992, 267: 25988-25997. PMID: 1281479, DOI: 10.1016/s0021-9258(18)35706-5.
- Isolation and structural elucidation of a novel phosphocysteine intermediate in the LAR protein tyrosine phosphatase enzymic pathwayCho H, Krishnaraj R, Kitas E, Bannwarth W, Walsh C, Anderson K. Isolation and structural elucidation of a novel phosphocysteine intermediate in the LAR protein tyrosine phosphatase enzymic pathway. Journal Of The American Chemical Society 1992, 114: 7296-7298. DOI: 10.1021/ja00044a052.
- ChemInform Abstract: Synthesis and Evaluation of Two New Inhibitors (I), (II) of EPSP (5‐ Enol‐pyruvoylshikimate 3‐Phosphate) Synthase.PANSEGRAU P, ANDERSON K, WIDLANSKI T, REAM J, SAMMONS R, SIKORSKI J, KNOWLES J. ChemInform Abstract: Synthesis and Evaluation of Two New Inhibitors (I), (II) of EPSP (5‐ Enol‐pyruvoylshikimate 3‐Phosphate) Synthase. ChemInform 1992, 23: no-no. DOI: 10.1002/chin.199211265.
- Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold.Stallings W, Abdel-Meguid S, Lim L, Shieh H, Dayringer H, Leimgruber N, Stegeman R, Anderson K, Sikorski J, Padgette S, Kishore G. Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 5046-5050. PMID: 11607190, PMCID: PMC51804, DOI: 10.1073/pnas.88.11.5046.
- Synthesis and evaluation of two new inhibitors of EPSP synthasePansegrau P, Anderson K, Widlanski T, Ream J, Sammons R, Sikorski J, Knowles J. Synthesis and evaluation of two new inhibitors of EPSP synthase. Tetrahedron Letters 1991, 32: 2589-2592. DOI: 10.1016/s0040-4039(00)78792-2.
- Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanismAnderson K, Miles E, Johnson K. Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism. Journal Of Biological Chemistry 1991, 266: 8020-8033. PMID: 1902468, DOI: 10.1016/s0021-9258(18)92934-0.
- Isolation and structure elucidation of the 4-amino-4-deoxychorismate intermediate in the PABA enzymic pathwayAnderson K, Kati W, Ye Q, Liu J, Walsh C, Benesi A, Johnson K. Isolation and structure elucidation of the 4-amino-4-deoxychorismate intermediate in the PABA enzymic pathway. Journal Of The American Chemical Society 1991, 113: 3198-3200. DOI: 10.1021/ja00008a073.
- Kinetic and structural analysis of enzyme intermediates: lessons from EPSP synthaseAnderson K, Johnson K. Kinetic and structural analysis of enzyme intermediates: lessons from EPSP synthase. Chemical Reviews 1990, 90: 1131-1149. DOI: 10.1021/cr00105a004.
- "Kinetic competence" of the 5-enolpyruvoylshikimate-3-phosphate synthase tetrahedral intermediate.Anderson K, Johnson K. "Kinetic competence" of the 5-enolpyruvoylshikimate-3-phosphate synthase tetrahedral intermediate. Journal Of Biological Chemistry 1990, 265: 5567-5572. PMID: 2180929, DOI: 10.1016/s0021-9258(19)39398-6.
- Observation by 13C NMR of the EPSP synthase tetrahedral intermediate bound to the enzyme active site.Anderson K, Sammons R, Leo G, Sikorski J, Benesi A, Johnson K. Observation by 13C NMR of the EPSP synthase tetrahedral intermediate bound to the enzyme active site. Biochemistry 1990, 29: 1460-5. PMID: 2334707, DOI: 10.1021/bi00458a017.
- An Enzyme-Targeted Herbicide Design Program Based on EPSP Synthase: Chemical Mechanism and Glyphosate Inhibition StudiesSikorski J, Anderson K, Cleary D, Miller M, Pansegrau P, Ream J, Sammons R, Johnson K. An Enzyme-Targeted Herbicide Design Program Based on EPSP Synthase: Chemical Mechanism and Glyphosate Inhibition Studies. 1990, 23-39. DOI: 10.1007/978-1-4757-9637-7_3.
- Isolation and structural elucidation of the tetrahedral intermediate in the EPSP synthase enzymic pathwayAnderson K, Sikorski J, Benesi A, Johnson K. Isolation and structural elucidation of the tetrahedral intermediate in the EPSP synthase enzymic pathway. Journal Of The American Chemical Society 1988, 110: 6577-6579. DOI: 10.1021/ja00227a056.
- A tetrahedral intermediate in the EPSP synthase reaction observed by rapid quench kinetics.Anderson K, Sikorski J, Johnson K. A tetrahedral intermediate in the EPSP synthase reaction observed by rapid quench kinetics. Biochemistry 1988, 27: 7395-406. PMID: 3061457, DOI: 10.1021/bi00419a034.
- Evaluation of 5-enolpyruvoylshikimate-3-phosphate synthase substrate and inhibitor binding by stopped-flow and equilibrium fluorescence measurements.Anderson K, Sikorski J, Johnson K. Evaluation of 5-enolpyruvoylshikimate-3-phosphate synthase substrate and inhibitor binding by stopped-flow and equilibrium fluorescence measurements. Biochemistry 1988, 27: 1604-10. PMID: 3284585, DOI: 10.1021/bi00405a032.