Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells

Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells

Item
http://www.wikidata.org/entity/Q28593471
The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1aKinetic properties and tissular distribution of mammalian phosphomannomutase isozymesLack of homozygotes for the most frequent disease allele in carbohydrate-deficient glycoprotein syndrome type 1ABeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphataseFrom structure to function: YrbI from Haemophilus influenzae (HI1679) is a phosphataseMechanistic studies of phosphoserine phosphatase, an enzyme related to P-type ATPasesA new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motifBovine cytosolic 5'-nucleotidase acts through the formation of an aspartate 52-phosphoenzyme intermediate.The normal phenotype of Pmm1-deficient mice suggests that Pmm1 is not essential for normal mouse development.Heterodimerization of Two Pathological Mutants Enhances the Activity of Human Phosphomannomutase2Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-1,6-bisphosphataseBiochemical phenotype of a common disease-causing mutation and a possible therapeutic approach for the phosphomannomutase 2-associated disorder of glycosylationPhosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase.A mutant of phosphomannomutase1 retains full enzymatic activity, but is not activated by IMP: Possible implications for the disease PMM2-CDG.The α-Phosphoglucomutase ofLactococcus lactisIs Unrelated to the α-d-Phosphohexomutase Superfamily and Is Encoded by the Essential GenepgmHThe Analysis of Variants in the General Population Reveals That Is Extremely Tolerant to Missense Mutations and That Diagnosis of PMM2-CDG Can Benefit from the Identification of Modifiers
P2860

Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells

Item
http://www.wikidata.org/entity/Q28593471
description
1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1997
@ast
im Juli 1997 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1997/07/14)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/07/14)
@nl
наукова стаття, опублікована в липні 1997
@uk
مقالة علمية (نشرت في 14-7-1997)
@ar
name
Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
@ast
Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
@en
Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
@nl
type
label
Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
@ast
Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
@en
Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
@nl
prefLabel
Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
@ast
Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
@en
Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P356
P1433
P1476
Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells
@en
P2093
P2860
P304
P31
P356
10.1016/S0014-5793(97)00704-7
P407
P433
P478
P50
P577
P698
P921