Хайлтын үр дүнгүүд - Timothy Palzkill

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  1. 1
    Metallo‐β‐lactamase structure and function

    Metallo‐β‐lactamase structure and function -н Timothy Palzkill

    Хэвлэсэн 2012
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  2. 2
    Structural and Mechanistic Basis for Extended-Spectrum Drug-Resistance Mutations in Altering the Specificity of TEM, CTX-M, and KPC β-lactamases

    Structural and Mechanistic Basis for Extended-Spectrum Drug-Resistance Mutations in Altering the Specificity of TEM, CTX-M, and KPC β-lactamases -н Timothy Palzkill

    Хэвлэсэн 2018
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  3. 3
    A natural polymorphism in β-lactamase is a global suppressor

    A natural polymorphism in β-lactamase is a global suppressor -н Wanzhi Huang, Timothy Palzkill

    Хэвлэсэн 1997
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  4. 4
    Systematic mutagenesis of the active site omega loop of TEM-1 beta-lactamase

    Systematic mutagenesis of the active site omega loop of TEM-1 beta-lactamase -н Joseph F. Petrosino, Timothy Palzkill

    Хэвлэсэн 1996
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  5. 5
    The mechanism of ceftazidime and cefiderocol hydrolysis by D179Y variants of KPC carbapenemases is similar and involves the formation of a long-lived covalent intermediate

    The mechanism of ceftazidime and cefiderocol hydrolysis by D179Y variants of KPC carbapenemases is similar and involves the formation of a long-lived covalent intermediate -н André Birgy, Christina Nnabuife, Timothy Palzkill

    Хэвлэсэн 2024
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  6. 6
    Natural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme Stability

    Natural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme Stability -н Shrenik Mehta, Kacie Rice, Timothy Palzkill

    Хэвлэсэн 2015
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  7. 7
    DNA sequence analysis of<i>ARS</i>elements from chromosome III of<i>Saccharomyces cerevisiae</i>: identification of a new conserved sequence

    DNA sequence analysis of<i>ARS</i>elements from chromosome III of<i>Saccharomyces cerevisiae</i>: identification of a new conserved sequence -н Timothy Palzkill, Stephen G. Oliver, Carol S. Newlon

    Хэвлэсэн 1986
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  8. 8
    How Structural and Physicochemical Determinants Shape Sequence Constraints in a Functional Enzyme

    How Structural and Physicochemical Determinants Shape Sequence Constraints in a Functional Enzyme -н Luciano A. Abriata, Timothy Palzkill, Matteo Dal Peraro

    Хэвлэсэн 2015
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  9. 9
    A secondary drug resistance mutation of TEM-1 β-lactamase that suppresses misfolding and aggregation

    A secondary drug resistance mutation of TEM-1 β-lactamase that suppresses misfolding and aggregation -н Vera Sideraki, Wanzhi Huang, Timothy Palzkill, Hiram Gilbert

    Хэвлэсэн 2000
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  10. 10
    Amino Acid Sequence Determinants of β-Lactamase Structure and Activity

    Amino Acid Sequence Determinants of β-Lactamase Structure and Activity -н Wanzhi Huang, Joseph F. Petrosino, Marc Hirsch, Peter S. Shenkin, Timothy Palzkill

    Хэвлэсэн 1996
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  11. 11
    Probing regulon of ArcA in Shewanella oneidensis MR-1 by integrated genomic analyses

    Probing regulon of ArcA in Shewanella oneidensis MR-1 by integrated genomic analyses -н Haichun Gao, Xiaohu Wang, Zamin K. Yang, Timothy Palzkill, Jizhong Zhou

    Хэвлэсэн 2008
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  12. 12
    Multiple Global Suppressors of Protein Stability Defects Facilitate the Evolution of Extended-Spectrum TEM β-Lactamases

    Multiple Global Suppressors of Protein Stability Defects Facilitate the Evolution of Extended-Spectrum TEM β-Lactamases -н Nicholas G. Brown, Jeanine M. Pennington, Wanzhi Huang, Tulin Ayvaz, Timothy Palzkill

    Хэвлэсэн 2010
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  13. 13
    Differential active site requirements for NDM-1 β-lactamase hydrolysis of carbapenem versus penicillin and cephalosporin antibiotics

    Differential active site requirements for NDM-1 β-lactamase hydrolysis of carbapenem versus penicillin and cephalosporin antibiotics -н Zhizeng Sun, Liya Hu, Banumathi Sankaran, B. V. Venkataram Prasad, Timothy Palzkill

    Хэвлэсэн 2018
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  14. 14
    Slow Protein Dynamics Elicits New Enzymatic Functions by Means of Epistatic Interactions

    Slow Protein Dynamics Elicits New Enzymatic Functions by Means of Epistatic Interactions -н María-Agustina Rossi, Timothy Palzkill, Fábio C. L. Almeida, Alejandro J. Vila

    Хэвлэсэн 2022
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  15. 15
    Structure of the catalytic domain of the colistin resistance enzyme MCR-1

    Structure of the catalytic domain of the colistin resistance enzyme MCR-1 -н V. Stojanoski, Banumathi Sankaran, B. V. Venkataram Prasad, Laurent Poirel, Patrice Nordmann, Timothy Palzkill

    Хэвлэсэн 2016
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  16. 16
    Small Molecule Inhibition of the Steroid Receptor Coactivators, SRC-3 and SRC-1

    Small Molecule Inhibition of the Steroid Receptor Coactivators, SRC-3 and SRC-1 -н Ying Wang, David M. Lonard, Yang Yu, Dar‐Chone Chow, Timothy Palzkill, Bert W. O’Malley

    Хэвлэсэн 2011
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  17. 17
    Network of epistatic interactions in an enzyme active site revealed by large-scale deep mutational scanning

    Network of epistatic interactions in an enzyme active site revealed by large-scale deep mutational scanning -н Allison Judge, Banumathi Sankaran, Liya Hu, Murugesan Palaniappan, André Birgy, B. V. Venkataram Prasad, Timothy Palzkill

    Хэвлэсэн 2024
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  18. 18
    A Triple Mutant in the Ω-loop of TEM-1 β-Lactamase Changes the Substrate Profile via a Large Conformational Change and an Altered General Base for Catalysis

    A Triple Mutant in the Ω-loop of TEM-1 β-Lactamase Changes the Substrate Profile via a Large Conformational Change and an Altered General Base for Catalysis -н V. Stojanoski, Dar‐Chone Chow, Liya Hu, Banumathi Sankaran, Hiram Gilbert, B. V. Venkataram Prasad, Timothy Palzkill

    Хэвлэсэн 2015
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  19. 19
    The Binary Protein Interactome of Treponema pallidum – The Syphilis Spirochete

    The Binary Protein Interactome of Treponema pallidum – The Syphilis Spirochete -н Bjoern Titz, Seesandra V. Rajagopala, Johannes B. Goll, Roman Häuser, Matthew McKevitt, Timothy Palzkill, Peter Uetz

    Хэвлэсэн 2008
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  20. 20
    Structural Basis of Substrate Specificity and Protease Inhibition in Norwalk Virus

    Structural Basis of Substrate Specificity and Protease Inhibition in Norwalk Virus -н Zana Muhaxhiri, Lisheng Deng, Sreejesh Shanker, Banumathi Sankaran, Mary K. Estes, Timothy Palzkill, Yongcheng Song, B. V. Venkataram Prasad

    Хэвлэсэн 2013
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