Browse our Phosphorylase, Glycogen, Muscle Proteins (PYGM)

Horse (Equine) Phosphorylase, Glycogen, Muscle (PYGM) interaction partners

1. The horse PYGM gene was broadly expressed in all tissues tested with the highest expression observed in skeletal muscle. It contains fewer mobile elements than its human ortholog, resulting in an increase in the structural stability of the gene sequence.

Mouse (Murine) Phosphorylase, Glycogen, Muscle (PYGM) interaction partners

1. Results show that PYGM and RAC1 are altered in the dorsolateral prefrontal cortex in chronic schizophrenia and are controlled by NMDA signaling in the rodent cortex and cortical astrocytes suggesting an altered NMDA-dependent glycogenolysis in astrocytes in schizophrenia.

2. Data suggest that the irreversible inhibition of glycogen (show GYS1 Proteins) phosphorylase (GP) could represent one of the mechanisms that contribute to mercury-dependent muscle toxicity.

3. Data show that glycogen (show GYS1 Proteins) phosphorylase is irreversibly impaired by exposure to peroxynitrite, and suggest that the peroxynitrite-dependent inactivation of the enzyme could be due to the nitration of Tyr613 at the allosteric inhibitor site of the enzyme.

Rabbit Phosphorylase, Glycogen, Muscle (PYGM) interaction partners

1. The formation of a complex between the denatured monomeric form of Phb (show PHB Proteins) and the dissociated forms of GroEL (show GroEL Proteins) is detected during heating at 46 degrees C.

2. alpha-crystallin interacts with the intermediates of unfolding of the Phb (show PHB Proteins) molecule

Human Phosphorylase, Glycogen, Muscle (PYGM) interaction partners

1. Results show that PYGM and RAC1 are altered in the dorsolateral prefrontal cortex in chronic schizophrenia and are controlled by NMDA signaling in the rodent cortex and cortical astrocytes suggesting an altered NMDA-dependent glycogenolysis in astrocytes in schizophrenia.

2. This report expands the phenotype and genotype of McArdle disease and suggests that PYGM mutations should be looked for in patients with very late-onset myopathy with no previous history of exercise intolerance

3. Because the NMD mechanism does not seem to operate in nonspecific cells, PBMCs were more suitable than muscle biopsies for detecting the pathogenicity of some PYGM mutations, notably the silent mutation whose effect in the splicing of intron 6 was unnoticed in previous muscle transcriptomic studies

4. Variations in AMPD1 (show AMPD1 Proteins), CPT2 (show CPT2 Proteins), and PGYM genes are not associated with the onset, susceptibility, or severity of chronic fatigue syndrome.

5. update of the reported mutations and polymorphisms in the PYGM gene [review]

6. study found that T lymphocytes expressed myophosphorylase in healthy donors, but expression was significantly lower in McArdle patients (p<0.001); PYGM mRNA levels were also lower in white blood cells from McArdle patients

7. biological significance of this PKCtheta (show PRKCQ Proteins);/alphaPIX (show ARHGEF6 Proteins)/Rac 1 GTPase (show RACGAP1 Proteins)/PYGM signaling pathway seems to be the control of different cellular responses such as migration and proliferation

8. 5 different PYGM mutations were found in 8 Brazilian families: 4 previously described (p.R50X, p.T692kfs30, p.K609K, and p.G455R), and one, pI513V, a novel heterozygous mutation.

9. a novel mutation, in the PYGM gene c.632delG, in three unrelated families of Jewish descent originating from the Caucasus region

10. a new role for Rac1 in cell signaling, showing that this GTPase (show RACGAP1 Proteins) triggers T-cell proliferation upon IL-2 (show IL2 Proteins) stimulation by associating with PYGM and modulating its enzymatic activity.

Pig (Porcine) Phosphorylase, Glycogen, Muscle (PYGM) interaction partners

1. Data indicate that a G/T mutation in exon 8 in muscle glycogen phosphorylase (PYGM) was identified and association analysis with meat quality traits showed that it was significantly associated with lean meat percentage(p<0.05).