Results 51 to 60 of about 224,774 (318)

Cell-free enzymatic synthesis of GDP-l-fucose from mannose

open access: yesAMB Express, 2019
GDP-l-fucose, the key substrate for fucosyloligosaccharide biosynthesis, has been synthesized via a de novo pathway in bacteria. In the present study, genes for GDP-l-fucose biosynthesis were cloned into the expression vector pET-28a (+) to construct ...
Weiyang Wang   +6 more
doaj   +1 more source

D-mannose transport and metabolism in isolated enterocytes [PDF]

open access: yes, 2004
D-mannose transport and metabolism has been studied in enterocytes isolated from chicken small intestine. In the presence of Na+, the mannose taken up by the cells either remains free, is phosphorylated, is catabolized to H2O, or becomes part of membrane
Cano Rodríguez, María Mercedes   +3 more
core   +1 more source

A zebrafish model of congenital disorders of glycosylation with phosphomannose isomerase deficiency reveals an early opportunity for corrective mannose supplementation

open access: yesDisease Models & Mechanisms, 2013
SUMMARY Individuals with congenital disorders of glycosylation (CDG) have recessive mutations in genes required for protein N-glycosylation, resulting in multi-systemic disease. Despite the well-characterized biochemical consequences in these individuals,
Jaime Chu   +9 more
doaj   +1 more source

Convergent and divergent mechanisms of sugar recognition across kingdoms [PDF]

open access: yes, 2014
Protein modules that bind specific oligosaccharides are found across all kingdoms of life from single-celled organisms to man. Different, overlapping and evolving designations for sugar-binding domains in proteins can sometimes obscure common features ...
Drickamer, K, Taylor, ME
core   +1 more source

Decreased bone formation and increased osteoclastogenesis cause bone loss in mucolipidosis II

open access: yesEMBO Molecular Medicine, 2013
Mucolipidosis type II (MLII) is a severe multi‐systemic genetic disorder caused by missorting of lysosomal proteins and the subsequent lysosomal storage of undegraded macromolecules.
Katrin Kollmann   +14 more
doaj   +1 more source

Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor

open access: yesJournal of Cell Biology, 2004
The cation-independent mannose 6-phosphate receptor (CI-MPR) mediates sorting of lysosomal hydrolase precursors from the TGN to endosomes. After releasing the hydrolase precursors into the endosomal lumen, the unoccupied receptor returns to the TGN for ...
C. Arighi   +4 more
semanticscholar   +1 more source

A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells [PDF]

open access: yes, 2008
Mannose 6-phosphate receptors (MPRs) are transported from endosomes to the Golgi after delivering lysosomal enzymes to the endocytic pathway. This process requires Rab9 guanosine triphosphatase (GTPase) and the putative tether GCC185.
Espinosa, Eric   +2 more
core   +3 more sources

Strategies for carbohydrate recognition by the mannose 6-phosphate receptors [PDF]

open access: yesGlycobiology, 2008
The two members of the P-type lectin family, the 46 kDa cation-dependent mannose 6-phosphate receptor (CD-MPR) and the 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR), are ubiquitously expressed throughout the animal kingdom and are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues.
Nancy M. Dahms   +2 more
openaire   +3 more sources

Expression of the insulin-like growth factor-II/mannose-6-phosphate receptor in multiple human tissues during fetal life and early infancy [PDF]

open access: yes, 1992
The insulin like growth factor-II/mannose-6-phosphate (IGF-II/M6P) receptor has been detected in many cells and tissues. In the rat, there is a dramatic developmental regulation of IGF-II/M6P receptor expression, the receptor being high in fetal and ...
Eisenmenger, Wolfgang   +5 more
core   +1 more source

Ligand interactions of the cation-dependent mannose 6-phosphate receptor [PDF]

open access: yesJournal of Biological Chemistry, 1989
The interactions of the bovine cation-dependent mannose 6-phosphate receptor with monovalent and divalent ligands have been studied by equilibrium dialysis. This receptor appears to be a homodimer or a tetramer. Each mole of receptor monomer bound 1.2 mol of the monovalent ligands, mannose 6-phosphate and pentamannose phosphate with Kd values of 8 X 10(
Stuart Kornfeld, P Y Tong
openaire   +2 more sources

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