scholarly journals A Conservative Amino Acid Mutation in the Chromosome‐Encoded Dihydrofolate Reductase Confers Trimethoprim Resistance inStreptococcus pneumoniae

1998 ◽  
Vol 178 (3) ◽  
pp. 700-706 ◽  
Author(s):  
Andreas Pikis ◽  
Jacob A. Donkersloot ◽  
William J. Rodriguez ◽  
Jerry M. Keith
Keyword(s):  
Amino Acid ◽  
Dihydrofolate Reductase ◽  
Amino Acid Mutation

scholarly journals Amino acid mutation in Plasmodium vivax dihydrofolate reductase (dhfr) and dihydropteroate synthetase (dhps) genes in Hormozgan Province, southern Iran

2019 ◽  
Vol 56 (2) ◽  
pp. 170 ◽  
Author(s):  
Gholamreza Hatam ◽  
Somayeh Maghsoodloorad ◽  
Nahid Hosseinzadeh ◽  
Ali Haghighi ◽  
Rahmat Solgi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Plasmodium Vivax ◽  
Dihydrofolate Reductase ◽  
Amino Acid Mutation ◽  
Southern Iran

scholarly journals Characterization and amino acid sequence of Neisseria gonorrhoeae dihydrofolate reductase.

1984 ◽  
Vol 259 (19) ◽  
pp. 12291-12298 ◽  
Author(s):  
D P Baccanari ◽  
R L Tansik ◽  
S J Paterson ◽  
D Stone
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neisseria Gonorrhoeae ◽  
Dihydrofolate Reductase

scholarly journals Prospective mapping of viral mutations that escape antibodies used to treat COVID-19

Science ◽  
2021 ◽  
Vol 371 (6531) ◽  
pp. 850-854 ◽  
Author(s):  
Tyler N. Starr ◽  
Allison J. Greaney ◽  
Amin Addetia ◽  
William W. Hannon ◽  
Manish C. Choudhary ◽  
...  
Keyword(s):  
Amino Acid ◽  
Infected Patient ◽  
Viral Escape ◽  
Single Amino Acid ◽  
Receptor Binding Domain ◽  
Amino Acid Mutation ◽  
The Individual ◽  
Viral Surveillance ◽  
Single Amino Acid Mutation

Antibodies are a potential therapy for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), but the risk of the virus evolving to escape them remains unclear. Here we map how all mutations to the receptor binding domain (RBD) of SARS-CoV-2 affect binding by the antibodies in the REGN-COV2 cocktail and the antibody LY-CoV016. These complete maps uncover a single amino acid mutation that fully escapes the REGN-COV2 cocktail, which consists of two antibodies, REGN10933 and REGN10987, targeting distinct structural epitopes. The maps also identify viral mutations that are selected in a persistently infected patient treated with REGN-COV2 and during in vitro viral escape selections. Finally, the maps reveal that mutations escaping the individual antibodies are already present in circulating SARS-CoV-2 strains. These complete escape maps enable interpretation of the consequences of mutations observed during viral surveillance.

Single amino acid mutation in alpha-helical peptide affect second harmonic generation hyperpolarizability

2013 ◽  
Vol 556 ◽  
pp. 260-265 ◽  
Author(s):  
Jing Wei ◽  
Jin-Yun Wang ◽  
Min-Yi Zhang ◽  
Guo-Liang Chai ◽  
Chen-Sheng Lin ◽  
...  
Keyword(s):  
Amino Acid ◽  
Second Harmonic Generation ◽  
Harmonic Generation ◽  
Second Harmonic ◽  
Single Amino Acid ◽  
Amino Acid Mutation ◽  
Helical Peptide ◽  
Single Amino Acid Mutation ◽  
Alpha Helical Peptide

A single amino acid substitution in Staphylococcus aureus dihydrofolate reductase determines trimethoprim resistance 1 1 Edited by T.Richmond

1997 ◽  
Vol 266 (1) ◽  
pp. 23-30 ◽  
Author(s):  
Glenn E. Dale ◽  
Clemens Broger ◽  
Allan D' Arcy ◽  
Peter G. Hartman ◽  
Ronald DeHoogt ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Dihydrofolate Reductase ◽  
Amino Acid Substitution ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid

Spontaneous splicing mutations at the dihydrofolate reductase locus in Chinese hamster ovary cells

1986 ◽  
Vol 6 (6) ◽  
pp. 1926-1935
Author(s):  
P J Mitchell ◽  
G Urlaub ◽  
L Chasin
Keyword(s):  
Amino Acid ◽  
Dihydrofolate Reductase ◽  
Splice Site ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Splice Sites ◽  
Ovary Cells ◽  
Splicing Mutations ◽  
Intron 4

We isolated and characterized three spontaneous mutants of Chinese hamster ovary cells that were deficient in dihydrofolate reductase activity. All three mutants contained no detectable enzyme activity and produced dihydrofolate reductase mRNA species that were shorter than those of the wild type by about 120 bases. Six exons are normally represented in this mRNA; exon 5 was missing in all three mutant mRNAs. Nuclease S1 analysis of the three mutants indicated that during the processing of the mutant RNA, exon 4 was spliced to exon 6. The three mutant genes were cloned, and the regions around exons 4 and 5 were sequenced. In one mutant, the GT dinucleotide at the 5' end of intron 5 had changed to CT. In a second mutant, the first base in exon 5 had changed from G to T. In a revertant of this mutant, this base was further mutated to A, a return to a purine. Approximately 25% of the mRNA molecules in the revertant were spliced correctly to produce an enzyme with one presumed amino acid change. In the third mutant, the AG at the 3' end of intron 4 had changed to AA. A mutation that partially reversed the mutant phenotype had changed the dinucleotide at the 5' end of intron 4 from GT to AT. The splicing pattern in this revertant was consistent with the use of cryptic donor and acceptor splice sites close to the original sites to produce an mRNA with three base changes and a protein with two amino acid changes. These mutations argue against a scanning model for the selection of splice site pairs and suggest that only a single splice site need be inactivated to bring about efficient exon skipping (a regulatory mechanism for some genes). The fact that all three mutants analyzed exhibited exon 5 splicing mutations indicates that these splice sites are hot spots for spontaneous mutation.

Zika virus increased virulence due to single amino acid mutation

2018 ◽  
Vol 54 (8) ◽  
pp. 926-927
Author(s):  
David Isaacs
Keyword(s):  
Amino Acid ◽  
Zika Virus ◽  
Single Amino Acid ◽  
Amino Acid Mutation ◽  
Single Amino Acid Mutation
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