C. Lemke

发表

Multimodal small-molecule screening for human prion protein binders

Jayme L. Dahlin, David R. Liu, S. Schreiber, 2020, The Journal of Biological Chemistry.

Multimodal small-molecule screening for human prion protein binders

Jayme L. Dahlin, David R. Liu, S. Schreiber, 2020, The Journal of Biological Chemistry.

Novel inhibitor binding site discovery on HIV-1 capsid N-terminal domain by NMR and X-ray crystallography.

J. Mercier, J. Rancourt, S. Titolo, 2013, ACS chemical biology.

Inhibition of HIV-1 capsid assembly: optimization of the antiviral potency by site selective modifications at N1, C2 and C16 of a 5-(5-furan-2-yl-pyrazol-1-yl)-1H-benzimidazole scaffold.

J. Duan, O. Hucke, M. Garneau, 2012, Bioorganic & medicinal chemistry letters.

Potent triazolyl-proline-based inhibitors of HCV NS3 protease.

P. White, N. Goudreau, M. Llinàs-Brunet, 2008, Bioorganic & medicinal chemistry letters.

Peptide backbone replacement of hepatitis C virus NS3 serine protease C-terminal cleavage product analogs: discovery of potent succinamide inhibitors.

M. Garneau, P. White, Jeff O'meara, 2013, Bioorganic & medicinal chemistry letters.

Synthesis and optimization of a novel series of HCV NS3 protease inhibitors: 4-arylproline analogs.

M. Garneau, P. White, Jeff O'meara, 2013, Bioorganic & medicinal chemistry letters.

Discovery of novel P2 substituted 4-biaryl proline inhibitors of hepatitis C virus NS3 serine protease.

M. Bailey, C. Lemke, T. Halmos, 2013, Bioorganic & medicinal chemistry letters.

Molecular Mechanism by Which a Potent Hepatitis C Virus NS3-NS4A Protease Inhibitor Overcomes Emergence of Resistance

G. Kukolj, P. White, Jeff O'meara, 2012, The Journal of Biological Chemistry.

Point mutations at the catalytic site of PCSK9 inhibit folding, autoprocessing, and interaction with the LDL receptor

Nadine H. Elowe, C. Garvie, V. Kaushik, 2016, Protein science : a publication of the Protein Society.

Structure–function analysis of the SHOC2–MRAS–PP1C holophosphatase complex

D. Root, A. Stamford, F. McCormick, 2022, Nature.

Crystallization and preliminary crystallographic analysis of an aminoglycoside kinase from Legionella pneumophila.

A. Berghuis, N. Cianciotto, B. Xiong, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

Optimization of a 1,5-dihydrobenzo[b][1,4]diazepine-2,4-dione series of HIV capsid assembly inhibitors 1: addressing configurational instability through scaffold modification.

O. Hucke, P. Bonneau, S. Morin, 2013, Bioorganic & medicinal chemistry letters.

Discovery and Structure-Based Design of Potent Covalent PPARγ Inverse-Agonists BAY-4931 and BAY-0069

Lindsay C. Westlake, M. Meyerson, A. Cherniack, 2022, Journal of medicinal chemistry.

Discovery of a 1,5-dihydrobenzo[b][1,4]diazepine-2,4-dione series of inhibitors of HIV-1 capsid assembly.

O. Hucke, P. Bonneau, C. Yoakim, 2011, Bioorganic & medicinal chemistry letters.

Structure of PDE3A-SLFN12 complex reveals requirements for activation of SLFN12 RNase

Lindsay C. Westlake, M. Meyerson, S. Carr, 2021, Nature Communications.

Discovery of Novel Small-Molecule HIV-1 Replication Inhibitors That Stabilize Capsid Complexes

Jean-François Mercier, Wesley I. Sundquist, Stephen W. Mason, 2013, Antimicrobial Agents and Chemotherapy.

Optimization of a 1,5-dihydrobenzo[b][1,4]diazepine-2,4-dione series of HIV capsid assembly inhibitors 2: structure-activity relationships (SAR) of the C3-phenyl moiety.

J. Duan, O. Hucke, M. Garneau, 2013, Bioorganic & medicinal chemistry letters.

Monitoring Binding of HIV‐1 Capsid Assembly Inhibitors Using 19F Ligand‐and 15N Protein‐Based NMR and X‐ray Crystallography: Early Hit Validation of a Benzodiazepine Series

Jean-François Mercier, Yves Bousquet, J. Mercier, 2013, ChemMedChem.

Distinct Effects of Two HIV-1 Capsid Assembly Inhibitor Families That Bind the Same Site within the N-Terminal Domain of the Viral CA Protein

Wesley I. Sundquist, Stephen W. Mason, W. Sundquist, 2012, Journal of Virology.

Bound Structure and Biochemical Mechanism of Action of BI 201335, a Potent, Non-covalent Inhibitor of HCV NS3-NS4A Protease

O. Hucke, P. White, D. Thibeault, 2010 .

Paralog knockout profiling identifies DUSP4 and DUSP6 as a digenic dependence in MAPK pathway-driven cancers

John G Doench, G. Getz, W. Sellers, 2021, Nature Genetics.

Structure of the Antibiotic Resistance Factor Spectinomycin Phosphotransferase from Legionella pneumophila*

D. Fong, A. Berghuis, B. Xiong, 2010, The Journal of Biological Chemistry.

Substrate Induced Conformational Changes in Argininosuccinate Synthetase*

P. Howell, C. Lemke, 2002, The Journal of Biological Chemistry.

Expression, purification, crystallization and preliminary X-ray analysis of Escherichia coli argininosuccinate synthetase.

P. Howell, C. Lemke, M. Yeung, 1999, Acta crystallographica. Section D, Biological crystallography.

Combined X-ray, NMR, and Kinetic Analyses Reveal Uncommon Binding Characteristics of the Hepatitis C Virus NS3-NS4A Protease Inhibitor BI 201335*

O. Hucke, P. White, N. Goudreau, 2011, The Journal of Biological Chemistry.

Ligand bioactive conformation plays a critical role in the design of drugs that target the hepatitis C virus NS3 protease.

H. Nar, S. LaPlante, A. Jakalian, 2014, Journal of medicinal chemistry.

The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis.

P. Howell, C. Lemke, 2001, Structure.

Enantiomeric atropisomers inhibit HCV polymerase and/or HIV matrix: characterizing hindered bond rotations and target selectivity.

O. Hucke, S. LaPlante, R. Coulombe, 2014, Journal of medicinal chemistry.

A novel inhibitor-binding site on the HIV-1 capsid N-terminal domain leads to improved crystallization via compound-mediated dimerization.

P. Bonneau, S. Titolo, A. Faucher, 2013, Acta crystallographica. Section D, Biological crystallography.

Substructure determination in multiwavelength anomalous diffraction, single anomalous diffraction, and single isomorphous replacement with anomalous scattering data using Shake-and-Bake.

P. Howell, G. D. Smith, C. Lemke, 2007, Methods in molecular biology.

Structure of the Antibiotic Resistance Factor Spectinomycin Phosphotransferase from Legionella pneumophila*

D. Fong, A. Berghuis, B. Xiong, 2010, The Journal of Biological Chemistry.

Correction to “Discovery and Structure-Based Design of Potent Covalent PPARγ Inverse-Agonists BAY-4931 and BAY-0069”

Lindsay C. Westlake, M. Meyerson, A. Cherniack, 2022, Journal of medicinal chemistry.

Discovery and characterization of orally bioavailable 4-chloro-6-fluoroisophthalamides as covalent PPARG inverse-agonists.

P. Lienau, E. Pook, Jonathan T. Goldstein, 2022, Bioorganic & medicinal chemistry.