Results 31 to 40 of about 467,506 (265)

Substrate specificity of Ty1 integrase [PDF]

open access: yesJournal of Virology, 1995
Integration of the Saccharomyces cerevisiae retrotransposon Ty1 requires the element-encoded integrase (IN) protein, which is a component of cytoplasmic virus-like particles (VLPs). Using purified recombinant Ty1 IN and an oligonucleotide integration assay based on Ty1 long terminal repeat sequences, we have compared IN activity on substrates having ...
S P, Moore, M, Powers, D J, Garfinkel
openaire   +2 more sources

Probabilistic approach to predicting substrate specificity of methyltransferases.

open access: yesPLoS Computational Biology, 2014
We present a general probabilistic framework for predicting the substrate specificity of enzymes. We designed this approach to be easily applicable to different organisms and enzymes.
Teresa Szczepińska   +7 more
doaj   +1 more source

The impact of tunnel mutations on enzymatic catalysis depends on the tunnel-substrate complementarity and the rate-limiting step

open access: yesComputational and Structural Biotechnology Journal, 2020
Transport of ligands between bulk solvent and the buried active sites is a critical event in the catalytic cycle of many enzymes. The rational design of transport pathways is far from trivial due to the lack of knowledge about the effect of mutations on ...
Piia Kokkonen   +8 more
doaj   +1 more source

Structural basis for substrate specificity of mammalian neuraminidases.

open access: yesPLoS ONE, 2014
The removal of sialic acid (Sia) residues from glycoconjugates in vertebrates is mediated by a family of neuraminidases (sialidases) consisting of Neu1, Neu2, Neu3 and Neu4 enzymes.
Victoria Smutova   +7 more
doaj   +1 more source

Reciprocal control of viral infection and phosphoinositide dynamics

open access: yesFEBS Letters, EarlyView.
Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley   +1 more source

Crystal structure and substrate specificity of Drosophila 3,4-dihydroxyphenylalanine decarboxylase. [PDF]

open access: yesPLoS ONE, 2010
3,4-Dihydroxyphenylalanine decarboxylase (DDC), also known as aromatic L-amino acid decarboxylase, catalyzes the decarboxylation of a number of aromatic L-amino acids.
Qian Han   +4 more
doaj   +1 more source

Substrate Specificity of Soybean Lipoxidase

open access: yesJournal of Biological Chemistry, 1969
Abstract Purified soybean lipoxidase was used to test the substrate specificity of all cis,cis-methylene-interrupted isomers of linoleic acid. The natural 9,12-isomer was found to be the best substrate, and the 13,16-isomer 50% as effective. The presence of calcium ions broadened the pattern of specificity.
R T, Holman, P O, Egwim, W W, Christie
openaire   +2 more sources

Spatiotemporal and quantitative analyses of phosphoinositides – fluorescent probe—and mass spectrometry‐based approaches

open access: yesFEBS Letters, EarlyView.
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho   +3 more
wiley   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

open access: yesFEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe   +3 more
wiley   +1 more source

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