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PedAM

Pediatric Disease Annotations & Medicines




Disease myopathy
Phenotype C0029401|paget disease of bone
Sentences 24
PubMedID- 25388089 Dominant mutations in the valosin-containing protein (vcp) gene cause inclusion body myopathy associated with paget disease of bone and frontotemporal dementia, which is characterized by progressive muscle weakness, dysfunction in bone remodeling, and frontotemporal dementia.
PubMedID- 24838343 Its dominant mutations cause hereditary inclusion body myopathy associated with paget disease of bone and frontotemporal dementia (ibmpfd) or amyotrophic lateral sclerosis.
PubMedID- 20301649 Inclusion body myopathy associated with paget disease of bone (pdb) and/or frontotemporal dementia (ibmpfd) is characterized by adult-onset proximal and distal muscle weakness (clinically resembling a limb-girdle muscular dystrophy syndrome), early-onset pdb, and premature frontotemporal dementia (ftd).
PubMedID- 21320982 Background: missense mutations in the valosin-containing protein (vcp) gene on chromosome 9p13.3-p12 cause inclusion body myopathy with paget disease of bone and frontotemporal dementia (hereafter referred to as ibmpfd; omim 167320).
PubMedID- 22728077 To date, 19 different single amino acid-substitutions in vcp have been reported to cause ibmpfd (inclusion body myopathy associated with paget disease of bone and frontotemporal dementia), an autosomal dominant inherited human disease.
PubMedID- 23169451 Introduction: mutations in the valosin-containing protein (vcp) gene cause hereditary inclusion body myopathy (ibm) associated with paget disease of bone (pdb), and frontotemporal dementia (ftd).
PubMedID- 25698929 However, p97 dysfunction was recently linked to some forms of amyotrophic lateral sclerosis and hereditary inclusion body myopathy associated with paget disease of bone and frontotemporal dementia (ibmpfd) and a connection to failed mitochondrial quality control was suspected (yamanaka et al., 2012).
PubMedID- 24598262 Mutations in human p97 (known as vcp) are linked to neurodegenerative disorders, such as amyotrophic lateral sclerosis [4] and inclusion body myopathy associated with paget disease of bone and frontotemporal dementia (ibmpfd) [5].
PubMedID- 26388768 Other uncommon mutations have been identified in the valosin-containing protein (vcp) gene, which cause inclusion body myopathy with paget disease of bone and ftd (watts et al., 2004), and in the charged multivesicular body protein 2b (chmp2b) gene, involved in the endosomal–lysosomal pathway (skibinski et al., 2005).
PubMedID- 23747512 Mutations in valosin-containing protein (vcp) cause a rare, autosomal dominant disease called inclusion body myopathy associated with paget disease of bone and frontotemporal dementia (ibmpfd).
PubMedID- 22270372 Here we have tested ten major inclusion body myopathy associated with paget disease of bone and frontotemporal dementia-linked mutants for atpase activity and found that all have increased activity over the wild type, with one mutant, p97(a232e), having three times higher activity.
PubMedID- 22105171 Inclusion body myopathy with paget disease of bone and frontotemporal dementia (ibmpfd) is an autosomal dominant disorder characterized by progressive myopathy that is often accompanied by bone weakening and/or frontotemporal dementia.
PubMedID- 25884947 Mutations in the valosin containing protein (vcp) gene cause hereditary inclusion body myopathy (hibm) associated with paget disease of bone (pdb), frontotemporal dementia (ftd), more recently termed multisystem proteinopathy (msp).
PubMedID- 20833645 Mutations of the human valosin-containing protein gene cause autosomal-dominant inclusion body myopathy associated with paget disease of bone and frontotemporal dementia.
PubMedID- 22909335 Genotype-phenotype studies of vcp-associated inclusion body myopathy with paget disease of bone and/or frontotemporal dementia.
PubMedID- 20604808 Several mis-sense mutations in the human vcp gene have been identified in patients suffering inclusion body myopathy associated with paget disease of bone and frontotemporal dementia (ibmpfd).
PubMedID- 23630012 Conversely, the accumulation of autophagosomes is a pathognomonic feature in other classes of myopathies including autophagic vacuolar myopathies (avms), lysosomal storage diseases, inclusion body myopathy with rimmed vacuoles paget disease of bone-frontotemporal dementia (ibmpfd) (nishino, 2003).
PubMedID- 21781992 P97 was identified as a causative factor for inclusion body myopathy associated with paget disease of bone and frontotemporal dementia (ibmpfd) and more recently as a causative factor for amyotrophic lateral sclerosis (als).
PubMedID- 25031631 Vcp mutations also cause the syndrome of inclusion body myopathy with paget disease of bone and ftd [108].
PubMedID- 23715207 Inclusion body myopathy with paget disease of bone and frontotemporal dementia is a progressive autosomal dominant disorder associated with a mutation in valosin-containing protein (vcp) with typical onset of symptoms in the 30s.
PubMedID- 23827524 Mutations in the prion-like domain (prld) of hnrnpa1 and a2/b1 genes were recently identified in 2 families with inclusion body myopathy associated with paget disease of bone, frontotemporal dementia (ftd), and amyotrophic lateral sclerosis, and in als patients.
PubMedID- 23316025 Regardless of the precise explanation for the differential activity of these compounds, the more selective behavior of ml241 suggests that developing pathway-specific p97 inhibitors may prove to be a valuable approach to study the role of p97 in regulating a variety of cellular pathways.31 pathway-selective p97 inhibitors with differential effects on apoptosis induction may enable the development of therapies that target p97 activity in diverse clinical settings, including ibmpfd (inclusion body myopathy associated with paget disease of bone and frontotemporal dementia),22, 11 retinitis pigmentosa,32 and cancer.33 understanding the basis of the divergent activities of ml240 and ml241 as well as potentially exploiting such effects toward the development of novel therapeutics are the aim of ongoing studies.
PubMedID- 22852081 Mutations in vcp have previously been identified in patients with inclusion body myopathy associated with paget disease of bone and frontotemporal dementia (ibmpfd) [91].
PubMedID- 25002991 Soon after it was revealed that several mutations in the tardbp gene, which encodes tdp-43, can cause some rare forms of fals and sals.6,7 tdp-43 inclusions are also prevalent in two other rare, progressive neurodegenerative diseases: inclusion body myopathy with paget disease of bone and frontotemporal dementia (ibmpfd) and perry syndrome, as well as in secondary pathology in huntington, parkinson and alzheimer diseases.8 the conjunction of genetics and pathology place tdp-43 as a major player in als and related neurodegenerative diseases.

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