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anti-Human Phosphoglucomutase 1 Antikörper:
anti-Rat (Rattus) Phosphoglucomutase 1 Antikörper:
anti-Mouse (Murine) Phosphoglucomutase 1 Antikörper:
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Human Polyclonal Phosphoglucomutase 1 Primary Antibody für ELISA, WB - ABIN562197
Eberl, Littman: The role of the nuclear hormone receptor RORgammat in the development of lymph nodes and Peyer's patches. in Immunological reviews 2003
Show all 6 Pubmed References
Human Monoclonal Phosphoglucomutase 1 Primary Antibody für IF, IP - ABIN562198
Guillemin, Bonnet, Jurie, Picard: Functional analysis of beef tenderness. in Journal of proteomics 2011
Cow (Bovine) Polyclonal Phosphoglucomutase 1 Primary Antibody für WB - ABIN2786674
Yokoyama, Tanase, Takahara: [Present state of female urology]. in Hinyokika kiyo. Acta urologica Japonica 2007
Human Polyclonal Phosphoglucomutase 1 Primary Antibody für ICC, IF - ABIN4890928
Zhu, Sun, Zou, Ge: Inducible metabolic adaptation promotes mesenchymal stem cell therapy for ischemia: a hypoxia-induced and glycogen-based energy prestorage strategy. in Arteriosclerosis, thrombosis, and vascular biology 2014
Integrated analyses of PGM1 and FOXJ2 expression provide a better prediction for the malignance and prognosis of hepatocellular carcinoma. This study establishes a tumor-suppressive role of PGM1 by regulating glucose trafficking and uncovers a novel regulatory mechanism of PGM1 expression.
PGM1 deficiency has been recognized as a cause of the congenital disorders of glycosylation.
The structural perturbation resulting from mutation of this single amino acid reveals the molecular mechanism underlying PGM1 deficiency in these missense variants.
Homozygous mutation in the PGM1 gene is associated with PGM1 deficiency.
analysis of the structural basis of PGM1 enzyme dysfunction in PGM1 deficiency
both PGM1 protein misfolding and catalytic impairment may play a role in PGM1 deficiency
PGM1 is required for sustained cell growth during nutritional changes
Phosphoglucomutase 1 deficiency, previously identified as a glycogenosis, is also a congenital disorder of glycosylation.
The analysis involved the data on nine polymorphic codominant loci: HP, GC, TF, PI, PGM1, GLO1, C3, ACP1, and ESD. The loci were selected by significance of differences in genotype frequencies between tuberculosis patients and healthy controls
cell signaling kinase Pak1 is a novel regulator of glucose metabolism through its phosphorylation and regulation of PGM activity.
Results report a novel human protein, calphoglin, which activates inorganic pyrophosphatase (IPP) and enhances phosphoglucomutase activity through the activated IPP.
During extrauterine life, females carrying the PGM1*2 allele are relatively protected from extreme body mass increase, and during intrauterine life, PGM1*2/*2 homozygotes show a tendency to low body mass increase.
There is a correlation between glomerular expression of MCP-1 and PGM1 and worsening renal prognosis in paediatric lupus nephritis.
ZASP/Cypher anchors PGM1 to Z-disc under conditions of stress. The impaired binding of PGM1 to ZASP/Cypher might be involved in the pathogenesis of dilated cardiomyopathy.
Growth reduction in the pgm mutant is largely caused by exaggerated root respiration, but not by leaf respiration.
Gravitropic mutants phosphoglucomutase (pgm) and sgr9 show abnormal amyloplast distribution and reduced gravitropism at 1 g.
The focus of this report is the analysis of gravitropic responses in lateral roots of wild-type background and pgm-1 mutants.
pgm-1 roots respond to gravity at one-third the rate of wild-type (WT) roots.
Sucrose-inducible genes are upregulated in pgm leaves at the end of a light treatment, when soluble sugars levels are higher than in the wild type.
Data indicate that the phosphoglucomutase 1 (PGM1) pattern of expression changes during skeletal muscle development.
The protein encoded by this gene is an isozyme of phosphoglucomutase (PGM) and belongs to the phosphohexose mutase family. There are several PGM isozymes, which are encoded by different genes and catalyze the transfer of phosphate between the 1 and 6 positions of glucose. In most cell types, this PGM isozyme is predominant, representing about 90% of total PGM activity. In red cells, PGM2 is a major isozyme. This gene is highly polymorphic. Mutations in this gene cause glycogen storage disease type 14. Alternativley spliced transcript variants encoding different isoforms have been identified in this gene.
, glucose phosphomutase 1
, hypothetical protein
, glucose phosphomutase 2
, phosphoglucomutase 2
, phosphoglucomutase 1
, chondroitin sulfate proteoglycan 2
, chondroitin sulfate proteoglycan core protein 2
, large fibroblast proteoglycan
, versican core protein
, phosphoglucomutase isoform1
, Glucose phosphomutase 1