Results 21 to 30 of about 1,013 (157)
The ApaH-like phosphatase TbALPH1 is the major mRNA decapping enzyme of trypanosomes. [PDF]
PLoS Pathogens, 2017 5'-3' decay is the major mRNA decay pathway in many eukaryotes, including trypanosomes. After deadenylation, mRNAs are decapped by the nudix hydrolase DCP2 of the decapping complex and finally degraded by the 5'-3' exoribonuclease. Uniquely, trypanosomes
Susanne Kramer
doaj +1 more source
Polyphosphatase Activity of CthTTM, a Bacterial Triphosphate Tunnel Metalloenzyme [PDF]
Journal of Biological Chemistry, 2008 Triphosphate tunnel metalloenzymes (TTMs) are a superfamily of phosphotransferases with a distinctive active site located within an eight-stranded beta barrel. The best understood family members are the eukaryal RNA triphosphatases, which catalyze the initial step in mRNA capping.
Ruchi, Jain, Stewart, Shuman
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, 2022 Inclusion bodies are typically ignored as they are considered unwanted protein waste generated by prokaryotic host cells during recombinant protein production or harmful protein inclusions in human cell biology.
Jozef Nahalka (5711945) +3 more
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Angewandte Chemie, Volume 137, Issue 11, March 10, 2025.The more the merrier: Oligophosphorimidazolide reagents enable the concomitant conjugation of multiple phosphate units to phosphopeptides, yielding derivatives with monodisperse phosphate chain lengths (up to hexaphosphate). This simple transformation occurs chemoselectively under mild conditions.
Kevin Qian +3 more
wiley +2 more sources
Substrate Binding in Protein-tyrosine Phosphatase-like Inositol Polyphosphatases [PDF]
Journal of Biological Chemistry, 2012 Protein-tyrosine phosphatase-like inositol polyphosphatases are microbial enzymes that catalyze the stepwise removal of one or more phosphates from highly phosphorylated myo-inositols via a relatively ordered pathway. To understand the substrate specificity and kinetic mechanism of these enzymes we have determined high resolution, single crystal, x-ray
Robert J, Gruninger +6 more
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Bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in E. coli [PDF]
, 2017 Processes for the biological removal of phosphate from wastewater rely on temporary manipula-tion of bacterial polyphosphate levels by phased environmental stimuli. In E.
Frank, S +4 more
core +4 more sources
Derepression of polyphosphatase in Escherichia coli by starvation for inorganic phosphate [PDF]
FEBS Letters, 1975 Several micro-organisms are known to accumulate polyphosphate (polyP) when subjected to unbalanced growth conditions such as low pH, sulphur starvation or following a period of phosphate-starvation. The accumulated polyP, which can be degraded, is thought to regulate the level of inorganic phosphorous (Pi) of the cells or, alternatively, to serve as a ...
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, 2013 The rh-TRAP was separated from Sf9 cell culture supernatant by co-precipitation with anti-TRAP antibodies (15A4 and 13B9). Polyphosphatase activity was also measured using [32P]poly(P)40 (0.346 mM) as substrate.
Kazuya Doi (299343) +7 more
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ApaH Diadenosine Polyphosphatase from Legionella pneumophila
The FASEB Journal, 2011 Legionella pneumophila (LP), the causative agent of Legionnaires' disease, is a Gram‐negative bacterium and facultative intracellular parasite. The Nudix diadenosine polyphosphatase, NudA, is a virulence factor in LP, and a related nonNudix diadenosine polyphosphatase, ApaH, is a virulence factor in E. coli and acts additively with the E. coli NudA for
Alejandra Rizo Patron +6 more
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, 2013 A) Confocal fluorescence microscopy of fixed HeLa cells transfected with a vector with: the NoLS-scPPX construct (pIRES-NoLS-scPPX), a scPPX construct (pIRES-scPPX), or an empty vector (pIRES).
Concepción Iglesias (388834) +6 more
core +1 more source