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ALG1 Alg1p

ALG1, beta-1,4-mannosyltransferase
Top mentioned proteins: MT1, ACID, ALG-2, DPM1, CDG-Ia
Papers on ALG1
A Novel N-Tetrasaccharide in Patients with Congenital Disorders of Glycosylation, Including Asparagine-Linked Glycosylation Protein 1, Phosphomannomutase 2, and Mannose Phosphate Isomerase Deficiencies.
He et al., Boston, United States. In Clin Chem, Jan 2016
METHOD: We used LC-MS/MS and MALDI-TOF-MS analysis to identify and quantify a novel N-linked tetrasaccharide linked to the protein core, an N-tetrasaccharide (Neu5Acα2,6Galβ1,4-GlcNAcβ1,4GlcNAc) in plasma, serum glycoproteins, and a fibroblast lysate from patients with CDG caused by ALG1 [ALG1 (asparagine-linked glycosylation protein 1), chitobiosyldiphosphodolichol β-mannosyltransferase], PMM2 (phosphomannomutase 2), and MPI (mannose phosphate isomerase).
Serum transferrin carrying the xeno-tetrasaccharide NeuAc-Gal-GlcNAc2 is a biomarker of ALG1-CDG.
Eklund et al., Lund, Sweden. In J Inherit Metab Dis, Jan 2016
ALG1-CDG (formerly CDG-Ik) is a subtype of congenital disorders of glycosylation (CDG) where the genetic defect disrupts the synthesis of the lipid-linked oligosaccharide precursor required for N-glycosylation.
Electroclinical Features of Early-Onset Epileptic Encephalopathies in Congenital Disorders of Glycosylation (CDGs).
Jaeken et al., Catania, Italy. In Jimd Rep, Nov 2015
We describe a series of patients with EOEE and genetically confirmed CDG (ALG3-CDG, ALG6-CDG, DPM2-CDG, ALG1-CDG).
Congenital disorders of glycosylation with emphasis on cerebellar involvement.
Jaeken et al., Catania, Italy. In Semin Neurol, 2014
It has also been reported in some patients with ALG1-CDG, ALG3-CDG, ALG9-CDG, ALG6-CDG, ALG8-CDG, PIGA-CDG, DPM1-CDG, DPM2-CDG, B4GALT1-CDG, SLC35A2-CDG, COG1-CDG, COG5-CDG, COG7-CDG, and COG8-CDG.
ALG1-CDG: a new case with early fatal outcome.
Marquardt et al., Münster, Germany. In Gene, 2014
The deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase, encoded by the human ortholog of ALG1 from yeast, is known as ALG1-CDG (CDG-Ik).
Draft Genome Sequence of Falsirhodobacter sp. Strain alg1, an Alginate-Degrading Bacterium Isolated from Fermented Brown Algae.
Takeyama et al., Tokyo, Japan. In Genome Announc, 2013
alg1 is an alginate-degrading bacterium, the second species from the nonphototrophic bacterial genus Falsirhodobacter.
Defining the phenotype in congenital disorder of glycosylation due to ALG1 mutations.
Wevers et al., Nijmegen, Netherlands. In Pediatrics, 2012
Deficiency of β-1,4 mannosyltransferase (MT-1) congenital disorder of glycosylation (CDG), due to ALG1 gene mutations.
O-GlcNAc-specific antibody CTD110.6 cross-reacts with N-GlcNAc2-modified proteins induced under glucose deprivation.
Isono, Ōtsu, Japan. In Plos One, 2010
Furthermore, CTD110.6 antibodies reacted with N-GlcNAc(2)-modified glycoproteins produced by a yeast strain with a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2).
Guanosine diphosphate-mannose:GlcNAc2-PP-dolichol mannosyltransferase deficiency (congenital disorders of glycosylation type Ik): five new patients and seven novel mutations.
Moore et al., Paris, France. In J Med Genet, 2010
Methods LLO biosynthesis was examined in skin biopsy fibroblasts, mannosyltransferases were assayed in microsomes prepared from these cells, and ALG1-encoding MT-1 was sequenced at the DNA and complementary DNA levels.
Reproducibility of joint swelling assessment by sonography in patients with long-lasting rheumatoid arthritis (SEA-Repro study part II).
Saraux et al., Brest, France. In J Rheumatol, 2010
The sonographic reference standard was at least grade 1 (ALG1) or 2 (ALG2) synovitis according to at least 4/7 sonographers.
Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides.
Hennet et al., Zürich, Switzerland. In Hum Mutat, 2009
This review sets the state of the art by listing all mutations identified in the 15 genes (PMM2, MPI, DPAGT1, ALG1, ALG2, ALG3, ALG9, ALG12, ALG6, ALG8, DOLK, DPM1, DPM3, MPDU1, and RFT1) that yield a deficiency of dolichol-linked oligosaccharide biosynthesis.
[Primary study on glycan structure in pathopoiesis mechanism of recurrent respiratory papillomatosis].
Xiao et al., Beijing, China. In Zhonghua Er Bi Yan Hou Tou Jing Wai Ke Za Zhi, 2008
The expression of dolichyl-phosphate mannosyltransferase polypeptide 1 (DPM1), asparagine-linked glycosylation 1 homolog (ALG1), fucosyltransferase 8 (FUT8) and alpha-mannosidase 1A (MAN1A) were regulated and beta-hexosaminidase (HEXB), beta1-galactosidase (GLB1), exostoses 1 (EXT1), fucosyltransferase (FUT) reduced expression and heparan sulfate 3-O-sulfotransferase 1 (HS3ST3A1) increased expression.
In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis.
Imperiali et al., Cambridge, United States. In Biochemistry, 2006
The roles of Alg2 and Alg1 in the dolichol pathway were studied.
Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik.
Hennet et al., Zürich, Switzerland. In Hum Mol Genet, 2004
The accumulation pattern suggested a deficiency of the ALG1 beta1,4 mannosyltransferase, which adds the first mannose residue to lipid-linked oligosaccharides.
Deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik.
Körner et al., Regensburg, Germany. In Am J Hum Genet, 2004
The molecular nature of a severe multisystemic disorder with a recurrent nonimmune hydrops fetalis was identified as deficiency of GDP-Man:GlcNAc(2)-PP-dolichol mannosyltransferase, the human orthologue of the yeast ALG1 gene (MIM 605907).
ALG/alg: a single gene controlling the utilization of lactate in the presence of antimycin in the yeast Saccharomyces cerevisiae.
Puglisi et al., Parma, Italy. In Curr Genet, 1984
A strain dependent growth on lactate in the presence of antimycin A (AA) has been observed - the strain D261 can grow on lactate and AA, whereas in the strain K8/6C antimycin A prevents the utilization of lactate and the induction of LDH.Genetic analysis demonstrates that growth on lactate in the presence of AA segregates from D261 as a single nuclear factor which we indicate by ALG1 and alg1 in its dominant and recessive states.
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