Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Razia Tajwar"'
Autor:
Dimitrios Moianos, Maria Makri, Georgia-Myrto Prifti, Aristeidis Chiotellis, Alexandros Pappas, Molly E. Woodson, Razia Tajwar, John E. Tavis, Grigoris Zoidis
Publikováno v:
Molecules, Vol 29, Iss 12, p 2942 (2024)
Hepatitis B virus (HBV) remains a global health threat. Ribonuclease H (RNase H), part of the virus polymerase protein, cleaves the pgRNA template during viral genome replication. Inhibition of RNase H activity prevents (+) DNA strand synthesis and r
Externí odkaz:
https://doaj.org/article/92d2fc12da214c62bb8eb197a88cae60
Publikováno v:
ASPET 2023 Annual Meeting Abstract - Drug Discovery and Development.
Publikováno v:
Protein Science. 31
Hepatitis B virus (HBV) replicates by protein-primed reverse transcription. It chronically infects >250 million people, and the dominant anti-HBV drugs are nucleos(t)ide analogs targeting the viral polymerase (P). P has four domains, the terminal pro
Publikováno v:
The FASEB Journal. 36
Publikováno v:
Journal of Biotechnology. 306:118-124
Using multi-step error prone PCR (ep-PCR) of the gene encoding endoglucanase Cel12A (27 kDa) from Thermotoga neapolitana, mutants were obtained with many fold increase in the enzyme activity. The best mutant (C6, N47S/E57 K/ V88A/S157 P/K165 H) obtai
Publikováno v:
The Enzymes. 50
Hepatitis B virus (HBV) is a hepatotropic, partially double-stranded DNA virus that replicates by reverse transcription and is a major cause of chronic liver disease and hepatocellular carcinoma. Reverse transcription is catalyzed by the four-domain
Publikováno v:
Journal of Biological Chemistry. 298:101790
The ribonucleases H (RNases H) of HIV and hepatitis B virus are type 1 RNases H that are promising drug targets because inhibiting their activity blocks viral replication. Eukaryotic ribonuclease H1 (RNase H1) is an essential protein and a probable o
Publikováno v:
Extremophiles. 22:109-119
A novel, family GH10 enzyme, Xyn10B from Acidothermus cellulolyticus 11B was cloned and expressed in Escherichia coli. This enzyme was purified to homogeneity by binding to regenerated amorphous cellulose. It had higher binding on Avicel as compared
Publikováno v:
Enzyme and Microbial Technology. 106:75-82
Xylanase XynB of the hyperthermophile Thermotoga maritima, which belongs to glycoside hydrolase family 10 (GH10), does not have an associated carbohydrate binding module (CBM) in the native state. CBM6 and CBM22 from a thermophile Clostridium thermoc