A binding free energy decomposition approach for accurate calculations of the fidelity of DNA polymerases

Por Rucker, Robert, Oelschlaeger, Peter, Warshel, Arieh
Publicado em 2010

Systematic Analysis of Metallo-β-Lactamases Using an Automated Database

Por Widmann, Michael, Pleiss, Jürgen, Oelschlaeger, Peter
Publicado em 2012

Impact of remote mutations on metallo-β-lactamase substrate specificity: Implications for the evolution of antibiotic resistance

Por Oelschlaeger, Peter, Mayo, Stephen L., Pleiss, Juergen
Publicado em 2005

The Sequence-Activity Relationship between Metallo-β-Lactamases IMP-1, IMP-6, and IMP-25 Suggests an Evolutionary Adaptation to Meropenem Exposure

Por Liu, Eleanor M., Pegg, Kevin M., Oelschlaeger, Peter
Publicado em 2012

Azolylthioacetamide: A Highly Promising Scaffold for the Development of Metallo-β-lactamase Inhibitors

Por Yang, Shao-Kang, Kang, Joon S., Oelschlaeger, Peter, Yang, Ke-Wu
Publicado no ACS Med Chem Lett (2015)

Magnesium-Cationic Dummy Atom Molecules Enhance Representation of DNA Polymerase β in Molecular Dynamics Simulations: Improved Accuracy in Studies of Structural Features and Mutati...

Por Oelschlaeger, Peter, Klahn, Marco, Beard, William A., Wilson, Samuel H., Warshel, Arieh
Publicado em 2006

Biochemical Characterization of IMP-30, a Metallo-β-Lactamase with Enhanced Activity toward Ceftazidime

Por Pegg, Kevin M., Liu, Eleanor M., LaCuran, Alecander E., Oelschlaeger, Peter
Publicado em 2013

Amino Acid Thioester Derivatives: A Highly Promising Scaffold for the Development of Metallo-β-lactamase L1 Inhibitors

Por Liu, Xiao-Long, Shi, Ying, Kang, Joon S., Oelschlaeger, Peter, Yang, Ke-Wu
Publicado no ACS Med Chem Lett (2015)

Uncovering Molecular Bases Underlying Bone Morphogenetic Protein Receptor Inhibitor Selectivity

Por Alsamarah, Abdelaziz, LaCuran, Alecander E., Oelschlaeger, Peter, Hao, Jijun, Luo, Yun
Publicado no PLoS One (2015)

Evolving Carbapenemases: Can Medicinal Chemists Advance One Step Ahead Of The Coming Storm? (Perspective)

Por Oelschlaeger, Peter, Ai, Ni, DuPrez, Kevin T., Welsh, William J., Toney, Jeffrey H.
Publicado em 2010

Structural insights into quinolone antibiotic resistance mediated by pentapeptide repeat proteins: conserved surface loops direct the activity of a Qnr protein from a Gram-negative...

Por Xiong, Xiaoli, Bromley, Elizabeth H. C., Oelschlaeger, Peter, Woolfson, Derek N., Spencer, James
Publicado em 2011

Intramolecular Interactions between the Protease and Structural Domains Are Important for the Functions of Serine Protease Autotransporters

Por Tsang, Casey, Malik, Huma, Nassman, Deana, Huang, Antony, Tariq, Fayha, Oelschlaeger, Peter, Stathopoulos, Christos
Publicado em 2010

Triazolylthioacetamide: A Valid Scaffold for the Development of New Delhi Metallo-β-Lactmase-1 (NDM-1) Inhibitors

Por Zhai, Le, Zhang, Yi-Lin, Kang, Joon S., Oelschlaeger, Peter, Xiao, Lin, Nie, Sha-Sha, Yang, Ke-Wu
Publicado no ACS Med Chem Lett (2016)

Carbamylmethyl Mercaptoacetate Thioether: A Novel Scaffold for the Development of L1 Metallo-β-lactamase Inhibitors

Por Chang, Ya-Nan, Xiang, Yang, Zhang, Yue-Juan, Wang, Wen-Ming, Chen, Cheng, Oelschlaeger, Peter, Yang, Ke-Wu
Publicado no ACS Med Chem Lett (2017)

New β-phospholactam as a carbapenem transition state analog: synthesis of a broad-spectrum inhibitor of metallo-β-lactamases

Por Yang, Ke-Wu, Feng, Lei, Yang, Shao-Kang, Aitha, Mahesh, LaCuran, Alecander E., Oelschlaeger, Peter, Crowder, Michael W.
Publicado em 2013

Meropenem and Chromacef Intermediates Observed in IMP-25 Metallo-β-Lactamase-Catalyzed Hydrolysis

Por Oelschlaeger, Peter, Aitha, Mahesh, Yang, Hao, Kang, Joon S., Zhang, Antonia L., Liu, Eleanor M., Buynak, John D., Crowder, Michael W.
Publicado no Antimicrob Agents Chemother (2015)

Understanding the determinants of substrate specificity in IMP family metallo-β-lactamases: The importance of residue 262

Por Pegg, Kevin M, Liu, Eleanor M, George, Alex C, LaCuran, Alecander E, Bethel, Christopher R, Bonomo, Robert A, Oelschlaeger, Peter
Publicado no Protein Sci (2014)

Elucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution

Por LaCuran, Alecander E., Pegg, Kevin M., Liu, Eleanor M., Bethel, Christopher R., Ai, Ni, Welsh, William J., Bonomo, Robert A., Oelschlaeger, Peter
Publicado no Antimicrob Agents Chemother (2015)

Triethysilyl Enol Ethers in the Synthesis of Carbapenem Precursors

Por Nguyen, Thu Q., Chai, Weirui, Gu, Jane, Cook, Katie, Kim, Eugene, Goetz, Sam, Farni, Zach, Chepuru, Monica, Cox, Melina, Nguyen, Pauline, Raja, Hashim, Magistrado, Patrick, Michael, Faith, Oelschlaeger, Peter, Buynak, John D.
Publicado no Tetrahedron Lett (2015)

Functionalizing the γ-Position of α-Diazo-β-ketoesters

Por Nguyen, Thu Q., Alqurafi, Maha, Edwards, Cash, Nguyen, Pauline, Kim, Jean, Casco, Samuel, Bennet, Maricka, Chiang, Christopher, Lohry, Maureen, Cox, Melina, Meshram, Byron, Le, Duyen, Kim, Eugene, Smriti, Snigdha, Oelschlaeger, Peter, Buynak, John D.
Publicado no Tetrahedron Lett (2016)