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Alexander Mankin
Alexander Mankin
University of Illinois at Chicagp
Bestätigte E-Mail-Adresse bei uic.edu
Titel
Zitiert von
Zitiert von
Jahr
Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action
JA Dunkle, L Xiong, AS Mankin, JHD Cate
Proceedings of the national academy of sciences 107 (40), 17152-17157, 2010
4982010
Acquisition of a natural resistance gene renders a clinical strain of methicillin‐resistant Staphylococcus aureus resistant to the synthetic antibiotic linezolid
SM Toh, L Xiong, CA Arias, MV Villegas, K Lolans, J Quinn, AS Mankin
Molecular microbiology 64 (6), 1506-1514, 2007
4362007
How macrolide antibiotics work
N Vázquez-Laslop, AS Mankin
Trends in biochemical sciences 43 (9), 668-684, 2018
3842018
Macrolide antibiotics: binding site, mechanism of action, resistance
M Gaynor, AS Mankin
Current topics in medicinal chemistry 3 (9), 949-960, 2003
3462003
The site of action of oxazolidinone antibiotics in living bacteria and in human mitochondria
KL Leach, SM Swaney, JR Colca, WG McDonald, JR Blinn, LM Thomasco, ...
Molecular cell 26 (3), 393-402, 2007
3442007
Molecular mechanism of drug-dependent ribosome stalling
N Vazquez-Laslop, C Thum, AS Mankin
Molecular cell 30 (2), 190-202, 2008
2982008
Nucleotide biosynthesis is critical for growth of bacteria in human blood
S Samant, H Lee, M Ghassemi, J Chen, JL Cook, AS Mankin, AA Neyfakh
PLoS pathogens 4 (2), e37, 2008
2892008
Resistance mutations in 23 S rRNA identify the site of action of the protein synthesis inhibitor linezolid in the ribosomal peptidyl transferase center
P Kloss, L Xiong, DL Shinabarger, AS Mankin
Journal of molecular biology 294 (1), 93-101, 1999
2881999
The ribosomal peptidyl transferase center: structure, function, evolution, inhibition
N Polacek, AS Mankin
Critical reviews in biochemistry and molecular biology 40 (5), 285-311, 2005
2722005
Protein synthesis by ribosomes with tethered subunits
C Orelle, ED Carlson, T Szal, T Florin, MC Jewett, AS Mankin
Nature 524 (7563), 119-124, 2015
2582015
Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide
N Polacek, M Gaynor, A Yassin, AS Mankin
Nature 411 (6836), 498-501, 2001
2342001
Oxazolidinone Resistance Mutations in 23S rRNA ofEscherichia coli Reveal the Central Region of Domain V as the Primary Site of Drug Action
L Xiong, P Kloss, S Douthwaite, NM Andersen, S Swaney, ...
Journal of bacteriology 182 (19), 5325-5331, 2000
2312000
Antibiotics and the ribosome
T Tenson, A Mankin
Molecular microbiology 59 (6), 1664-1677, 2006
2112006
The general mode of translation inhibition by macrolide antibiotics
K Kannan, P Kanabar, D Schryer, T Florin, E Oh, N Bahroos, T Tenson, ...
Proceedings of the National Academy of Sciences 111 (45), 15958-15963, 2014
2072014
A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase centre
L Xiong, S Shah, P Mauvais, AS Mankin
Molecular microbiology 31 (2), 633-639, 1999
1961999
Cross-linking in the living cell locates the site of action of oxazolidinone antibiotics
JR Colca, WG McDonald, DJ Waldon, LM Thomasco, RC Gadwood, ...
Journal of Biological Chemistry 278 (24), 21972-21979, 2003
1942003
Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition
MG Gagnon, RN Roy, IB Lomakin, T Florin, AS Mankin, TA Steitz
Nucleic acids research 44 (5), 2439-2450, 2016
1832016
Programmed drug‐dependent ribosome stalling
H Ramu, A Mankin, N Vazquez‐Laslop
Molecular microbiology 71 (4), 811-824, 2009
1832009
Binding site of macrolide antibiotics on the ribosome: new resistance mutation identifies a specific interaction of ketolides with rRNA
G Garza-Ramos, L Xiong, P Zhong, A Mankin
Journal of bacteriology 183 (23), 6898-6907, 2001
1822001
RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA
F Yan, JM LaMarre, R Röhrich, J Wiesner, H Jomaa, AS Mankin, ...
Journal of the American Chemical Society 132 (11), 3953-3964, 2010
1782010
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