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Fanconi anemia, complementation group A

FAA, FAH, FANCA, fumarylacetoacetate hydrolase, fumarylacetoacetase
The Fanconi anemia complementation group (FANC) currently includes FANCA, FANCB, FANCC, FANCD1 (also called BRCA2), FANCD2, FANCE, FANCF, FANCG, FANCI, FANCJ (also called BRIP1), FANCL, FANCM and FANCN (also called PALB2). The previously defined group FANCH is the same as FANCA. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA crosslinking agents, increased chromosomal breakage, and defective DNA repair. The members of the Fanconi anemia complementation group do not share sequence similarity; they are related by their assembly into a common nuclear protein complex. This gene encodes the protein for complementation group A. Alternative splicing results in multiple transcript variants encoding different isoforms. Mutations in this gene are the most common cause of Fanconi anemia. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, FANCC, FANCG
Papers using FAA antibodies
Cleavage and cytoplasmic relocalization of histone deacetylase 3 are important for apoptosis progression.
Akhtar Asifa, In PLoS Genetics, 2006
... Darmstadt, Germany), the anti-phospho ATM from Cell Signalling technology, Inc (Boston, MA), the anti-H2A.Z and anti-FANCA from Abcam Inc (Cambridge, MA), the ...
Current concepts: Prosthetic-joint infections.
Bergh Kåre et al., In Acta Orthopaedica, 2003
... , FAA agar (Merck) was incubated in an ...
Papers on FAA
Sex-related difference in food anticipatory activity of mice.
Wang et al., China. In Horm Behav, 28 Mar 2015
UNASSIGNED: The expression of food-anticipatory activity (FAA) is induced by restricted feeding (RF), and its entrainment requires food-entrainable oscillators, the neuroanatomical basis of which is currently unclear.
Founder Haplotype Analysis of Fanconi Anemia in the Korean Population Finds Common Ancestral Haplotypes for a FANCG Variant.
Park et al., Seoul, South Korea. In Ann Hum Genet, 20 Mar 2015
UNASSIGNED: A common ancestral haplotype is strongly suggested in the Korean and Japanese patients with Fanconi anemia (FA), because common mutations have been frequently found: c.2546delC and c.3720_3724delAAACA of FANCA; c.307+1G>C, c.1066C>T, and c.1589_1591delATA of FANCG.
Metabolomics method to comprehensively analyze amino acids in different domains.
Raftery et al., Seattle, United States. In Analyst, 20 Mar 2015
Many studies have profiled free amino acids (FAAs) or proteins; however, few have connected the measurement of FAA with individual amino acids in the proteome.
Geographical and Ethnic Distribution of Mutations of the Fumarylacetoacetate Hydrolase Gene in Hereditary Tyrosinemia Type 1.
Tanguay et al., Québec, Canada. In Jimd Rep, 15 Mar 2015
HT1 results from a deficiency of the last enzyme of tyrosine catabolism, fumarylacetoacetate hydrolase (FAH).
Sub-nephrotoxic cisplatin sensitizes rats to acute renal failure and increases urinary excretion of fumarylacetoacetase.
Morales et al., Salamanca, Spain. In Toxicol Lett, 09 Mar 2015
In addition, the urinary excretion of fumarylacetoacetase was increased in cisplatin-treated animals at subtoxic doses, which might be exploited as a cisplatin-induced predisposition marker.
Genome editing with Cas9 in adult mice corrects a disease mutation and phenotype.
Anderson et al., Cambridge, United States. In Nat Biotechnol, Jun 2014
We demonstrate CRISPR-Cas9-mediated correction of a Fah mutation in hepatocytes in a mouse model of the human disease hereditary tyrosinemia.
Direct reprogramming of human fibroblasts to functional and expandable hepatocytes.
Hui et al., Shanghai, China. In Cell Stem Cell, Apr 2014
Upon transplantation into mice with concanavalin-A-induced acute liver failure and fatal metabolic liver disease due to fumarylacetoacetate dehydrolase (Fah) deficiency, hiHeps restore the liver function and prolong survival.
Recurrent inactivation of STAG2 in bladder cancer is not associated with aneuploidy.
Real et al., Madrid, Spain. In Nat Genet, 2013
A discovery exome sequencing screen (n = 17), followed by a prevalence screen (n = 60), identified new genes mutated in this tumor coding for proteins involved in chromatin modification (MLL2, ASXL2 and BPTF), cell division (STAG2, SMC1A and SMC1B) and DNA repair (ATM, ERCC2 and FANCA).
Amino acid profiles in term and preterm human milk through lactation: a systematic review.
Lőnnerdal et al., Urbana, United States. In Nutrients, 2013
We report a systematic review of total amino acid (TAA) and free amino acid (FAA) profiles, in term and preterm HM derived from 13 and 19 countries, respectively.
The Fanconi anemia DNA repair pathway: structural and functional insights into a complex disorder.
Deans et al., Dundee, United Kingdom. In Annu Rev Biophys, 2013
Mutations in any of at least sixteen FANC genes (FANCA-Q) cause Fanconi anemia, a disorder characterized by sensitivity to DNA interstrand crosslinking agents.
Reprogramming fibroblasts into bipotential hepatic stem cells by defined factors.
Hu et al., Shanghai, China. In Cell Stem Cell, 2013
In the injured liver of fumarylacetoacetate hydrolase (Fah)-deficient mice, repopulating iHepSCs become hepatocyte-like cells.
Hereditary breast and ovarian cancer susceptibility genes (review).
Matsuura et al., Kashihara, Japan. In Oncol Rep, 2013
Mutations in BRCA genes cannot account for all cases of HBOC, indicating that the remaining cases can be attributed to the involvement of constitutive epimutations or other cancer susceptibility genes, which include Fanconi anemia (FA) cluster (FANCD2, FANCA and FANCC), mismatch repair (MMR) cluster (MLH1, MSH2, PMS1, PMS2 and MSH6), DNA repair cluster (ATM, ATR and CHK1/2), and tumor suppressor cluster (TP53, SKT11 and PTEN).
In vitro expansion of single Lgr5+ liver stem cells induced by Wnt-driven regeneration.
Clevers et al., Utrecht, Netherlands. In Nature, 2013
Such clonal organoids can be induced to differentiate in vitro and to generate functional hepatocytes upon transplantation into Fah(-/-) mice.
Recommendations for the management of tyrosinaemia type 1.
Spiekerkötter et al., Brussels, Belgium. In Orphanet J Rare Dis, 2012
The management of tyrosinaemia type 1 (HT1, fumarylacetoacetase deficiency) has been revolutionised by the introduction of nitisinone but dietary treatment remains essential and the management is not easy.
Fanconi anemia complementation group A (FANCA) protein has intrinsic affinity for nucleic acids with preference for single-stranded forms.
Zhang et al., Miami, United States. In J Biol Chem, 2012
the nucleic acid-binding domain of FANCA is located primarily at its C terminus, where most disease-causing mutations are found.
Evidence for complete epistasis of null mutations in murine Fanconi anemia genes Fanca and Fancg.
Arwert et al., Amsterdam, Netherlands. In Dna Repair (amst), 2012
null mutations in Fanca or Fancg are fully epistatic
Identification of mutations causing hereditary tyrosinemia type I in patients of Middle Eastern origin.
Al-Sayed et al., Riyadh, Saudi Arabia. In Mol Genet Metab, 2011
We detected 11 novel and 6 previously described pathogenic mutations in the fumarylacetoacetase gene in a cohort of 43 patients originating from the Middle East with the acute form hereditary tyrosinemia type I
Hepatorenal tyrosinemia.
Kitagawa, Tokyo, Japan. In Proc Jpn Acad Ser B Phys Biol Sci, 2011
They suggested that the primary enzyme deficiency in patients with HRT was fumarylacetoacetate hydrolase, and this was soon confirmed.
Evaluation of Fanconi anaemia genes FANCA, FANCC and FANCL in cervical cancer susceptibility.
Gyllensten et al., Uppsala, Sweden. In Gynecol Oncol, 2011
genetic diversity in FANCA, FANCC and FANCL does not support an association of these genes with cervical cancer susceptibility in the Swedish population.
Origin, functional role, and clinical impact of Fanconi anemia FANCA mutations.
Surrallés et al., Barcelona, Spain. In Blood, 2011
All missense mutations studied lead to an altered FANCA protein that is unable to relocate to the nucleus and activate the FA/BRCA pathway.
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