Ngā hua rapu kaituhi

1

Metallo‐β‐lactamase structure and function mā Timothy Palzkill

I whakaputaina 2012

Whiwhi kuputuhi katoa
Revisão

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2

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

I whakaputaina 2018

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
Revisão

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3

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

I whakaputaina 1997

Whiwhi kuputuhi katoa
Artigo

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4

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

I whakaputaina 1996

Whiwhi kuputuhi katoa
Artigo

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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 mā André Birgy, Christina Nnabuife, Timothy Palzkill

I whakaputaina 2024

Whiwhi kuputuhi katoa
Artigo

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6

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

I whakaputaina 2015

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
Artigo

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7

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

I whakaputaina 1986

Whiwhi kuputuhi katoa
Artigo

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8

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

I whakaputaina 2015

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
Artigo

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9

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

I whakaputaina 2000

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
Artigo

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10

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

I whakaputaina 1996

Whiwhi kuputuhi katoa
Artigo

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11

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

I whakaputaina 2008

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
Artigo

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12

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

I whakaputaina 2010

Whiwhi kuputuhi katoa
Artigo

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13

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

I whakaputaina 2018

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
Artigo

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14

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

I whakaputaina 2022

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
Artigo

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15

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

I whakaputaina 2016

Whiwhi kuputuhi katoa
Artigo

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16

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

I whakaputaina 2011

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
Artigo

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17

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

I whakaputaina 2024

Whiwhi kuputuhi katoa
Artigo

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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 mā V. Stojanoski, Dar‐Chone Chow, Liya Hu, Banumathi Sankaran, Hiram Gilbert, B. V. Venkataram Prasad, Timothy Palzkill

I whakaputaina 2015

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
Artigo

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19

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

I whakaputaina 2008

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
Artigo

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20

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

I whakaputaina 2013

Whiwhi kuputuhi katoa Whiwhi kuputuhi katoa
Artigo

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Ngā hua rapu - Timothy Palzkill

Metallo‐β‐lactamase structure and function mā Timothy Palzkill

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

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

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

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 mā André Birgy, Christina Nnabuife, Timothy Palzkill

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

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

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

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

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

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

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

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

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

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

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

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

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 mā V. Stojanoski, Dar‐Chone Chow, Liya Hu, Banumathi Sankaran, Hiram Gilbert, B. V. Venkataram Prasad, Timothy Palzkill

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

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

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