Results 71 to 80 of about 349,791 (266)
Evidence for disulfide bonds in SR Protein Kinase 1 (SRPK1) that are required for activity and nuclear localization. [PDF]
PLoS ONE, 2017 Serine/arginine protein kinases (SRPKs) phosphorylate Arg/Ser dipeptide-containing proteins that play crucial roles in a broad spectrum of basic cellular processes.
Maria Koutroumani +4 more
doaj +1 more source
β‐Helical catalytic domains in glycoside hydrolase families 49, 55 and 87: domain architecture, modelling and assignment of catalytic residues [PDF]
FEBS Letters, 2002 X‐ray crystallography and bioinformatics studies reveal a tendency for the right‐handed β‐helix domain architecture to be associated with carbohydrate binding proteins. Here we demonstrate the presence of catalytic β‐helix domains in glycoside hydrolase (GH) families 49, 55 and 87 and provide evidence for their sharing a common evolutionary ancestor ...
Rigden, Daniel J, Franco, Octávio L
openaire +2 more sources
Reconstructing enzyme evolution by protein engineering
FEBS Letters, EarlyView.Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler +2 more
wiley +1 more source
Mutational analysis of two residues in the DYRK homology box of the protein kinase DYRK1A
BMC Research Notes, 2018 Objective Dual specificity tyrosine phosphorylation-regulated kinases (DYRK) contain a characteristic sequence motif (DYRK homology box, DH box) that is located N-terminal of the catalytic domain and supports the autophosphorylation of a conserved ...
Esti Wahyu Widowati +2 more
doaj +1 more source
Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery. [PDF]
PLoS ONE, 2016 The Gram-positive bacterium Paenibacillus sp. str. FPU-7 effectively hydrolyzes chitin by using a number of chitinases. A unique chitinase with two catalytic domains, ChiW, is expressed on the cell surface of this bacterium and has high activity towards ...
Takafumi Itoh +10 more
doaj +1 more source
Phosphorylation in the Catalytic Cleft Stabilizes and Attracts Domains of a Phosphohexomutase [PDF]
Biophysical Journal, 2015 Phosphorylation can modulate the activities of enzymes. The phosphoryl donor in the catalytic cleft of α-D-phosphohexomutases is transiently dephosphorylated while the reaction intermediate completes a 180° reorientation within the cleft. The phosphorylated form of 52 kDa bacterial phosphomannomutase/phosphoglucomutase is less accessible to dye or ...
Xu, Jia +3 more
openaire +2 more sources
FEBS Letters, EarlyView.The process of internalization of the Shiga toxin A subunit via formation of a complex with the Shiga toxin B subunit, which specifically binds to the Gb3 receptor. The peptide is designed to act as a carrier of drugs into cancer cells. Here, we explored the potential of peptides derived from the catalytic A subunit of Shiga toxin (STxA) to be drug ...
Giulia Opassi +6 more
wiley +1 more source
Epigenetic reprogramming of lineage switching in cancer
FEBS Letters, EarlyView.Cancer cells rarely commit to a single identity. Epigenetic mechanisms and tumor microenvironment cues push epithelial cells toward flexible, hybrid states that can shift into mesenchymal, neuroendocrine, or stem‐like fates, driving metastasis, drug resistance, and tumor heterogeneity. Targeting the epigenetic regulators behind these transitions, using
Ezgi Boyvatlı +4 more
wiley +1 more source
Catalytic domains in porous catalysts
, 2018 Understanding of the catalytic domains within porous catalysts is essential for control of these systems in order to obtain desired reaction yields and selectivities. This body of work consists of studies on two types of porous catalysts, mesoporous silica and zeolites, that can have interesting cooperative catalytic interactions between the inorganic ...
openaire +3 more sources
Endostatin binds to the catalytic domain of matrix metalloproteinase‐2
FEBS Letters, 2002 We previously reported that endostatin inhibits endothelial and tumor cellular invasion by blocking activation and catalytic activity of matrix metalloproteinase (MMP)‐2. Here we have examined the domain of proMMP‐2 responsible for the binding of endostatin using surface plasmon resonance.
Lee, Seo-Jin +6 more
openaire +2 more sources