Expression, Purification and evaluation of the Immunogenicity of RecombinantC-terminus of the Receptor-Binding Domain of Neurotoxin Botulinum Protein Type B (BoNT/B-HcC) [PDF]
مجله علمی دانشگاه علوم پزشکی کردستان, 2023 Background and Aim: Botulism, a syndrome caused by food poisoning, results from use of food contaminated with the botulinum toxin, which is very dangerous and deadly.
Hossein Samiei Abianeh +5 more
doaj
Structural-Functional Analysis Reveals a Specific Domain Organization in Family GH20 Hexosaminidases. [PDF]
PLoS ONE, 2015 Hexosaminidases are involved in important biological processes catalyzing the hydrolysis of N-acetyl-hexosaminyl residues in glycosaminoglycans and glycoconjugates.
Cristina Val-Cid +3 more
doaj +1 more source
Structural Insight of a Trimodular Halophilic Cellulase with a Family 46 Carbohydrate-Binding Module. [PDF]
PLoS ONE, 2015 Cellulases are the key enzymes used in the biofuel industry. A typical cellulase contains a catalytic domain connected to a carbohydrate-binding module (CBM) through a flexible linker.
Huaidong Zhang +6 more
doaj +1 more source
RBR E3 ubiquitin ligases: new structures, new insights, new questions [PDF]
, 2014 The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
Shaw, Gary S. +2 more
core +1 more source
Structure and inhibition mechanism of the catalytic domain of human squalene epoxidase
Nature Communications, 2019 Squalene epoxidase (SQLE), also known as squalene monooxygenase, catalyzes the stereospecific conversion of squalene to 2,3(S)-oxidosqualene, a key step in cholesterol biosynthesis.
A. Padyana +16 more
semanticscholar +1 more source
Structural and functional characterization of mature forms of metalloprotease E495 from Arctic sea-ice bacterium Pseudoalteromonas sp. SM495. [PDF]
PLoS ONE, 2012 E495 is the most abundant protease secreted by the Arctic sea-ice bacterium Pseudoalteromonas sp. SM495. As a thermolysin family metalloprotease, E495 was found to have multiple active forms in the culture of strain SM495.
Hai-Lun He +8 more
doaj +1 more source
RpfC (Rv1884) atomic structure shows high structural conservation within the resuscitation promoting factor catalytic domain [PDF]
, 2014 We report the first structure of the catalytic domain of RpfC (Rv1884), one of theresuscitation-promoting factors (RPFs) from Mycobacterium tuberculosis.
Bagneris, Claire +8 more
core +1 more source
Catalytic polymeric nanoreactors : more than a solid supported catalyst [PDF]
, 2012 Polymeric nanostructures can be synthesized where the catalytic motif is covalently attached within the core domain and protected from the environment by a polymeric shell.
Bosman, Liu, Wang, Yan
core +2 more sources
Zinc Binding Catalytic Domain of Human Tankyrase 1 [PDF]
Journal of Molecular Biology, 2008 Tankyrases are recently discovered proteins implicated in many important functions in the cell including telomere homeostasis and mitosis. Tankyrase modulates the activity of target proteins through poly(ADP-ribosyl)ation, and here we report the structure of the catalytic poly(ADP-ribose) polymerase (PARP) domain of human tankyrase 1. This is the first
Lari, Lehtiö +9 more
openaire +2 more sources
FEBS Letters, 2019 X‐linked intellectual disabilities (XLID) are common developmental disorders. The enzyme O‐GlcNAc transferase encoded by OGT, a recently discovered XLID gene, attaches O‐GlcNAc to nuclear and cytoplasmic proteins.
V. Pravata +9 more
semanticscholar +1 more source