Results 41 to 50 of about 112,119 (302)

The Synthesis of Mannose-6-Phosphate Using Polyphosphate-Dependent Mannose Kinase [PDF]

open access: yesCatalysts, 2019
Mannose-6-phosphate (M6P) is involved in many metabolic pathways in life, and it has important applications in the treatment of diseases. This study explored a cost-effective enzyme catalytic synthesis method of M6P, using polyphosphate-dependent mannose kinase from Arthrobacter species.
Zhu, Gao, Chen, Tan, Cao, Liu
openaire   +2 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

Inactivation of the three GGA genes in HeLa cells partially compromises lysosomal enzyme sorting

open access: yesFEBS Open Bio, 2021
The Golgi‐localized, gamma‐ear containing, ADP‐ribosylation factor‐binding proteins (GGAs 1, 2, and 3) are multidomain proteins that bind mannose 6‐phosphate receptors (MPRs) at the Golgi and play a role, along with adaptor protein complex 1 (AP‐1), in ...
Balraj Doray   +4 more
doaj   +1 more source

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

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

Data for analysis of mannose-6-phosphate glycans labeled with fluorescent tags

open access: yesData in Brief, 2016
Mannose-6-phosphate (M-6-P) glycan plays an important role in lysosomal targeting of most therapeutic enzymes for treatment of lysosomal storage diseases.
Ji-Yeon Kang   +3 more
doaj   +1 more source

Pathogenic Variants in Fucokinase Cause a Congenital Disorder of Glycosylation [PDF]

open access: yes, 2018
FUK encodes fucokinase, the only enzyme capable of converting L-fucose to fucose-1-phosphate, which will ultimately be used for synthesizing GDP-fucose, the donor substrate for all fucosyltransferases.
Bearden, David R.   +9 more
core   +1 more source

Systems Biology and Pangenome of Salmonella O-Antigens. [PDF]

open access: yes, 2019
O-antigens are glycopolymers in lipopolysaccharides expressed on the cell surface of Gram-negative bacteria. Variability in the O-antigen structure constitutes the basis for the establishment of the serotyping schema. We pursued a two-pronged approach to
Kavvas, Erol   +4 more
core   +2 more sources

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

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

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