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. |
Page: 1