Results 21 to 30 of about 112,119 (302)

Characterization of the GDP-D-mannose biosynthesis pathway in Coxiella burnetii: the initial steps for GDP-β-D-virenose biosynthesis. [PDF]

open access: yesPLoS ONE, 2011
Coxiella burnetii, the etiologic agent of human Q fever, is a gram-negative and naturally obligate intracellular bacterium. The O-specific polysaccharide chain (O-PS) of the lipopolysaccharide (LPS) of C. burnetii is considered a heteropolymer of the two
Craig T Narasaki   +2 more
doaj   +1 more source

A mutant of phosphomannomutase1 retains full enzymatic activity, but is not activated by IMP: Possible implications for the disease PMM2-CDG. [PDF]

open access: yesPLoS ONE, 2017
The most frequent disorder of glycosylation, PMM2-CDG, is caused by a deficiency of phosphomannomutase activity. In humans two paralogous enzymes exist, both of them require mannose 1,6-bis-phosphate or glucose 1,6-bis-phosphate as activators, but only ...
Valentina Citro   +5 more
doaj   +1 more source

Characterization of a Mannose-6-Phosphate Isomerase from Bacillus amyloliquefaciens and Its Application in Fructose-6-Phosphate Production. [PDF]

open access: yesPLoS ONE, 2015
The BaM6PI gene encoding a mannose-6-phosphate isomerase (M6PI, EC 5.3.1.8) was cloned from Bacillus amyloliquefaciens DSM7 and overexpressed in Escherichia coli.
Sujan Sigdel   +9 more
doaj   +1 more source

The human urine mannose 6-phosphate glycoproteome [PDF]

open access: yesBiochimica 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]

open access: yesDevelopmental 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]

open access: yesFEBS 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

A mannose-sensing AraC-type transcriptional activator regulates cell–cell aggregation of Vibrio cholerae

open access: yesnpj 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

Evidence that cholic acid CoA ligase is located asymmetrically on the cytoplasmic surface of hepatic microsomal vesicles.

open access: yesJournal of Lipid Research, 1979
The cholic acid CoA ligase activity of rat liver was quantitatively inactivated by proteolysis with pronase, chymotrypsin, subtilisin, or proteinase K in intact microsomal vesicles.
M A Polokoff, R A Coleman, R M Bell
doaj   +1 more source

Human immunodeficiency virus-1 uses the mannose-6-phosphate receptor to cross the blood-brain barrier. [PDF]

open access: yesPLoS ONE, 2012
HIV-1 circulates both as free virus and within immune cells, with the level of free virus being predictive of clinical course. Both forms of HIV-1 cross the blood-brain barrier (BBB) and much progress has been made in understanding the mechanisms by ...
Shinya Dohgu   +3 more
doaj   +1 more source

Phosphomannosyl receptors may participate in the adhesive interaction between lymphocytes and high endothelial venules. [PDF]

open access: yes, 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

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