Results 101 to 110 of about 365,538 (313)
The enzymatic processing of α-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site. [PDF]
PLoS ONE, 2018 Dystroglycan (DG) is a membrane receptor, belonging to the dystrophin-glycoprotein complex (DGC) and formed by two subunits, α-dystroglycan (α-DG) and β-dystroglycan (β -DG).
Magda Gioia +12 more
doaj +1 more source
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
FEBS Letters, EarlyView.Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley +1 more source
Elucidating the Function of Non catalytic Domains of Collagenases and Aggrecanases
Connective Tissue Research, 2008 Metalloproteinases that degrade extracellular matrix molecules play important roles in development and progression of various diseases. Among them, collagenases are unique as they have an ability to degrade triple helical interstitial collagens into 3/4 and 1/4 fragments, a crucial step for collagenolysis in the tissue.
Nagase, H, Fushimi, K
openaire +3 more sources
Nucleotide-Binding Sites of the Heterodimeric LmrCD ABC-Multidrug Transporter of Lactococcus lactis Are Asymmetric [PDF]
, 2006 LmrCD is a lactococcal, heterodimeric multidrug transporter, which belongs to the ABC superfamily. It consists of two half-transporters, LmrC and LmrD, that are necessary and sufficient for drug extrusion and ATP hydrolysis.
Konings, Wil N. +7 more
core +1 more source
Phosphoinositides and inositol phosphates as molecular glues
FEBS Letters, EarlyView.Inositol phosphates (IPs) and phosphoinositides (PIPs) regulate diverse eukaryotic processes. Beyond recruiting signaling proteins or acting as structural cofactors, recent studies suggest they mediate protein–protein interactions as natural molecular glues.
Aleshia Seaton‐Terry +9 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
, 2010 CFTR, the ABC protein defective in cystic fibrosis, functions as an anion channel. Once phosphorylated by protein kinase A, a CFTR channel is opened and closed by events at its two cytosolic nucleotide binding domains (NBDs).
Gadsby, David C. +5 more
core +1 more source
Dimeric structure of the bacterial extracellular foldase PrsA [PDF]
, 2015 Secretion of proteins into the membrane-cell wall space is essential for cell wall biosynthesis and pathogenicity in Gram-positive bacteria. Folding and maturation of many secreted proteins depend on a single extracellular foldase, the PrsA protein. PrsA
Schmidpeter, Philipp A. M. +7 more
core +1 more source
Structural insights and therapeutic targets in Acinetobacter baumannii capsule biosynthesis
FEBS Letters, EarlyView.Hypervirulent KL49 A. baumannii's capsular polysaccharide contains the nonulosonic acid 8‐epi‐Leg5,7Ac2, synthesized by epimerization via ElaA, ElaB, and ElaC. Crystal structures of ElaA, ElaB, and ElaC reveal their role in CMP‐Leg5,7Ac2 synthesis and regioselective C8 epimerization.
Woo Cheol Lee +7 more
wiley +1 more source