Results 31 to 40 of about 224,774 (318)
The human urine mannose 6-phosphate glycoproteome [PDF]
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2007 Glycoproteins containing the mannose 6-phosphate (Man-6-P) modification represent a class of proteins of considerable biomedical importance. They include over sixty different soluble lysosomal hydrolases and accessory proteins, deficiencies of which result in over forty different known human genetic diseases.
David E. Sleat +2 more
openaire +3 more sources
Expression of mannose 6-phosphate receptors in chicken [PDF]
Developmental Dynamics, 1996 In mammals, the sorting of newly synthesized lysosomal enzymes is accomplished by two mannose 6-phosphate receptors (MPR) designated MPR46 and MPR300. MPR300 has an additional function in clearing the nonglycosylated insulin-like growth factor II (IGFII).
U. Matzner +3 more
openaire +3 more sources
The cation‐independent mannose‐6‐phosphate receptor binds to soluble GPI‐linked proteins via mannose‐6‐phosphate [PDF]
FEBS Letters, 1995 The cation‐independent mannose‐6‐phosphate/insulin‐like growth factor II receptor has been observed to bind to soluble forms of glycosyl‐phosphatidylinositol‐linked molecules, one of mammalian origin (rat Thy‐1) and two of protozoan origins. Of the two phosphate groups found on the soluble forms of the protozoan glycosyl‐phosphatidylinositol‐linked ...
Green, Paula J. +3 more
openaire +5 more sources
npj Biofilms and Microbiomes, 2022 In addition to catalyzing coupled transport and phosphorylation of carbohydrates, the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) regulates various physiological processes in most bacteria.
Hye-Young Lee +6 more
doaj +1 more source
Phosphomannosyl receptors may participate in the adhesive interaction between lymphocytes and high endothelial venules. [PDF]
, 1984 Normal and malignant lymphocytes can migrate from the bloodstream into lymph nodes and Peyer's patches. This process helps distribute normal lymphocytes throughout the lymphoid system and may provide a portal of entry for circulating malignant cells.
Rosen, SD, Stoolman, LM, Tenforde, TS
core +1 more source
Crystal Structure of the Mannose-6-Phosphate Uncovering Enzyme [PDF]
Structure, 2020 Most lysosomal hydrolytic enzymes reach their destination via the mannose-6-phosphate (M6P) pathway. The enzyme N-acetylglucosamine-1-phosphodiester α-N-acetylglucosaminidase (NAGPA, or "uncovering enzyme") catalyzes the second step in the M6P tag formation, namely the removal of the masking N-acetylglucosamine (GlcNAc) portion. Defects in this protein
Alexei Gorelik +2 more
openaire +3 more sources
Interaction of mannose-6-phosphate with the hysteretic transition in glucose-6-phosphate hydrolysis in intact liver microsomes [PDF]
, 1992 We showed previously that glucose-6-phosphatase activity was characterised in intact liver microsomes by a hysteretic transition between a rapid and a slower catalytic form of the enzyme.
Berteloot, Alfred +4 more
core +1 more source
Disruption of the GDP-mannose synthesis pathway in Streptomyces coelicolor results in antibiotic hyper-susceptible phenotypes [PDF]
, 2018 Actinomycete bacteria use polyprenol phosphate mannose as a lipid linked sugar donor for extra-cytoplasmic glycosyl transferases that transfer mannose to cell envelope polymers, including glycoproteins and glycolipids.
Green +5 more
core +1 more source
The Cation-dependent Mannose 6-Phosphate Receptor
Journal of Biological Chemistry, 1989 The structural requirements for oligomerization and the generation of a functional mannose 6-phosphate (Man-6-P) binding site of the cation-dependent mannose 6-phosphate receptor (CD-MPR) were analyzed. Chemical cross-linking studies on affinity-purified CD-MPR and on solubilized membranes containing the receptor indicate that the CD-MPR exists as a ...
Nancy M. Dahms, Stuart Kornfeld
openaire +3 more sources
eLife, 2017 Chlamydia trachomatis is an obligate intracellular pathogen that resides in a membrane-bound compartment, the inclusion. The bacteria secrete a unique class of proteins, Incs, which insert into the inclusion membrane and modulate the host-bacterium ...
C. Elwell +8 more
semanticscholar +1 more source