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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Phosphoglucomutase 5

aciculin, PGM5, PGM-RP, phosphoglucomutase 5
Phosphoglucomutases (EC, such as PGM5, are phosphotransferases involved in interconversion of glucose-1-phosphate and glucose-6-phosphate. PGM activity is essential in formation of carbohydrates from glucose-6-phosphate and in formation of glucose-6-phosphate from galactose and glycogen (Edwards et al., 1995 [PubMed 8586438]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Phosphoglucomutase, Utrophin, vinculin, Actin, CAN
Papers on aciculin
Aciculin interacts with filamin C and Xin and is essential for myofibril assembly, remodeling and maintenance.
F├╝rst et al., Bonn, Germany. In J Cell Sci, 2014
We identified the dystrophin-binding protein aciculin (also known as phosphoglucomutase-like protein 5, PGM5) as a new interaction partner of FLNc and Xin.
Secretome analysis of atherosclerotic and non-atherosclerotic arteries reveals dynamic extracellular remodeling during pathogenesis.
Alvarez-Llamas et al., Madrid, Spain. In J Proteomics, 2012
Four proteins were significantly released in higher amounts by mammary tissue: gelsolin, vinculin, lamin A/C and phosphoglucomutase 5. CONCLUSION: The study of tissue secretome reveals key proteins involved in atherosclerosis which have not been previously reported in plasma.
A new method to identify flanking sequence tags in chlamydomonas using 3'-RACE.
Vallon et al., Saint-Pierre-des-Corps, France. In Plant Methods, 2011
Among these are insertions in genes coding for PSBS3 (possibly involved in non-photochemical quenching), the NimA-related protein kinase CNK2, the mono-dehydroascorbate reductase MDAR1, the phosphoglycerate mutase PGM5 etc.. CONCLUSION: We propose that our 3'-RACE FST method can be used to build large scale FST libraries in Chlamydomonas and other transformable organisms.
[Screening genes related to 'black' character in wu-ding chicken by delta differential display].
Shi et al., Changsha, China. In Yi Chuan Xue Bao, 2005
Five ESTs have high similarity rate with human TTN gene, human phosphoglucomutase 5 gene, human or mouse signal recongnition particle 54 kD gene, human or mouse ribonuclease/angiogenin inhibitor gene, respectively, with similarity rate 82%, 82%, 87%, 99% and 99%.
Diverse fates of paralogs following segmental duplication of telomeric genes.
Ledbetter et al., Atlanta, United States. In Genomics, 2004
These paralogous regions span approximately 200 kb and contain seven transcriptional units, including the previously identified CBWD, FOXD4, PGM5, F379, CXYorf1, and two human Unigene clusters, Hs.115173 and Hs.189160.
Gene content and function of the ancestral chromosome fusion site in human chromosome 2q13-2q14.1 and paralogous regions.
Trask et al., Seattle, United States. In Genome Res, 2002
The draft sequence of the human genome also provides new information on the location and intron-exon structure of functional copies of other 2q-fusion genes (PGM5, retina-specific F379, helicase CHLR1, and acrosin).
Aciculin and its relation to dystrophin: immunocytochemical studies in human normal and Duchenne dystrophy quadriceps muscles.
Oniki et al., Yokohama, Japan. In Acta Neuropathol, 2000
Aciculin is a novel adherens junction antigen extracted from human uterine smooth muscle that is reported to associate biochemically with dystrophin.
Functional diversity of the phosphoglucomutase superfamily: structural implications.
Satir et al., United States. In Protein Eng, 1999
Although the general domain structure and the active site of rabbit muscle phosphoglucomutase are preserved in the model of phosphoglucomutase-related protein, a major structural difference is likely to occur in domain 1 due to the absence of 55 amino acid residues in PGM-RP.
Characterisation of the promoter which regulates expression of a phosphoglucomutase-related protein, a component of the dystrophin/utrophin cytoskeleton predominantly expressed in smooth muscle.
Critchley et al., Leicester, United Kingdom. In Eur J Biochem, 1997
We have recently characterised a 60-kDa muscle-specific phosphoglucomutase-related protein (PGM-RP) which is expressed predominantly in adult visceral and vascular smooth muscle.
Localization of cranin (dystroglycan) at sites of cell-matrix and cell-cell contact: recruitment to focal adhesions is dependent upon extracellular ligands.
Smalheiser et al., Chapel Hill, United States. In Cell Adhes Commun, 1996
Within mature focal adhesions, cranin was present within the plaque region defined by beta 1 integrin, vinculin and phosphotyrosine staining, but occupied a larger domain corresponding to the terminal segments of stress fibers that was more precisely co-extensive with the cytoskeletal proteins alpha-actinin, utrophin and aciculin.
A novel dystrophin/utrophin-associated protein is an enzymatically inactive member of the phosphoglucomutase superfamily.
Critchley et al., Leicester, United Kingdom. In Eur J Biochem, 1996
A 60-kDa protein localised in adherens-type cellular junctions, and previously called aciculin, has been found to interact with the cytoskeletal proteins dystrophin and utrophin [Belkin, A. M. & Burridge, K. (1995) J. Biol.
Dystrophin, vinculin, and aciculin in skeletal muscle subject to chronic use and disuse.
Hood et al., North York, Canada. In Med Sci Sports Exerc, 1996
We hypothesized 1) that chronic muscle use and disuse would alter the expression of dystrophin as a compensatory mechanism designed to prevent muscle damage, and 2) that other subsarcolemmal cytoskeletal proteins (vinculin, M-vinculin, aciculin 60/63 kDa) that colocalize with dystrophin in muscle adherens junctions would be changed in parallel.
A novel human phosphoglucomutase (PGM5) maps to the centromeric region of chromosome 9.
Ives et al., London, United Kingdom. In Genomics, 1995
We propose that this gene be designated PGM5 and that it represents a novel member of the PGM family.
Association of aciculin with dystrophin and utrophin.
Burridge et al., Chapel Hill, United States. In J Biol Chem, 1995
Aciculin is a recently identified 60-kDa cytoskeletal protein, highly homologous to the glycolytic enzyme phosphoglucomutase type 1, (Belkin, A. M., Klimanskaya, I. V., Lukashev, M. E., Lilley, K., Critchley, D., and Koteliansky, V. E. (1994) J. Cell Sci.
Expression and localization of the phosphoglucomutase-related cytoskeletal protein, aciculin, in skeletal muscle.
Burridge et al., Chapel Hill, United States. In J Cell Sci, 1994
C2C12 mouse myoblasts did not express any aciculin before cell fusion in culture.
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