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APEX nuclease

APE2, APEX2, AP endonuclease II
Apurinic/apyrimidinic (AP) sites occur frequently in DNA molecules by spontaneous hydrolysis, by DNA damaging agents or by DNA glycosylases that remove specific abnormal bases. AP sites are pre-mutagenic lesions that can prevent normal DNA replication so the cell contains systems to identify and repair such sites. Class II AP endonucleases cleave the phosphodiester backbone 5' to the AP site. This gene encodes a protein shown to have a weak class II AP endonuclease activity. Most of the encoded protein is located in the nucleus but some is also present in mitochondria. This protein may play an important role in both nuclear and mitochondrial base excision repair (BER). [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: POLYMERASE, CAN, ACID, uracil-DNA glycosylase, PCNA
Papers on APE2
An enhanced ascorbate peroxidase 2/antibody-binding domain fusion protein (APEX2-ABD) as a recombinant target-specific signal amplifier.
New
Kang et al., Ulsan, South Korea. In Chem Commun (camb), Aug 2015
A recombinant target-specific signal amplifier was constructed by genetically fusing the enhanced ascorbate peroxidase 2 (APEX2) and an antibody-binding domain (ABD).
Quantification of the APE2 gene expression level in Candida albicans clinical isolates from patients with diagnosed fungal infections.
New
Chudy et al., Warsaw, Poland. In Eur J Clin Microbiol Infect Dis, Jul 2015
Aminopeptidase 2 (Ape2) facilitates the penetration of C. albicans into the host tissue, by providing free amino acids to support fungal growth and proliferation.
New synthetic sulfone derivatives inhibit growth, adhesion and the leucine arylamidase APE2 gene expression of Candida albicans in vitro.
New
Ochal et al., Warsaw, Poland. In Bioorg Med Chem, Feb 2015
Bromodichloromethyl-4-chloro-3-nitrophenyl sulfone (named compound 6); dichloromethyl-4-chloro-3-nitrophenyl sulfone (named 7); and chlorodibromomethyl-4-hydrazino-3-nitrophenyl sulfone (named 11) on inhibition of planktonic cells' growth, leucine arylamidase APE2 gene expression, and adhesion to epithelial cells were investigated.
Directed evolution of APEX2 for electron microscopy and proximity labeling.
Impact
Ting et al., Cambridge, United States. In Nat Methods, 2015
APEX2 is far more active in cells, enabling the use of electron microscopy to resolve the submitochondrial localization of calcium uptake regulatory protein MICU1.
Recognition and repair of chemically heterogeneous structures at DNA ends.
Review
Williams et al., United States. In Environ Mol Mutagen, 2015
Nucleolytic processing enzymes such as the MRE11/RAD50/NBS1/CtIP complex, Flap endonuclease (FEN1) and the apurinic endonucleases (APE1 and APE2) also act in the chemical "cleansing" of DNA breaks to prevent genomic instability and disease, and promote progression of DNA- and RNA-DNA damage response (DDR and RDDR) pathways.
Multi-Trait GWAS and New Candidate Genes Annotation for Growth Curve Parameters in Brahman Cattle.
Moore et al., Viçosa, Brazil. In Plos One, 2014
The annotated genes closest to the most significant SNPs for A had direct biological functions related to muscle development (RAB28), myogenic induction (BTG1), fetal growth (IL2), and body weights (APEX2); K genes were functionally associated with body weight, body height, average daily gain (TMEM18), and skeletal muscle development (SMN1).
AP endonucleases process 5-methylcytosine excision intermediates during active DNA demethylation in Arabidopsis.
Huh et al., Seoul, South Korea. In Nucleic Acids Res, 2014
We demonstrate that Arabidopsis AP endonucleases APE1L, APE2 and ARP have distinct functions to process such harmful lesions to allow nucleotide extension.
Apurinic/apyrimidinic endonuclease 2 regulates the expansion of germinal centers by protecting against activation-induced cytidine deaminase-independent DNA damage in B cells.
Schrader et al., Amsterdam, Netherlands. In J Immunol, 2014
APE2-deficient mice have smaller GCs and reduced Ab responses compared with wild-type mice.
Differential expression of APE1 and APE2 in germinal centers promotes error-prone repair and A:T mutations during somatic hypermutation.
Schrader et al., Fukuoka, Japan. In Proc Natl Acad Sci U S A, 2014
In contrast, the less efficient homolog, APE2, is highly expressed and contributes not only to the frequency of mutations, but also to the generation of mutations at A:T base pair (bp), insertions, and deletions.
Expression, functionality, and localization of apurinic/apyrimidinic endonucleases in replicative and non-replicative forms of Trypanosoma cruzi.
Cabrera et al., Santiago, Chile. In J Cell Biochem, 2014
In this work the localization, expression and functionality of two T. cruzi APEs (TcAP1, Homo sapiens APE1 orthologous and TcAP2, orthologous to Homo sapiens APE2 and to Schizosaccaromyces pombe Apn2p) were determined.
APE2 is required for ATR-Chk1 checkpoint activation in response to oxidative stress.
Yan et al., Charlotte, United States. In Proc Natl Acad Sci U S A, 2013
A base excision repair protein, Apurinic/apyrimidinic (AP) endonuclease 2 (APE2, APN2, or APEX2), is required for the generation of replication protein A (RPA)-bound single-stranded DNA, the recruitment of a checkpoint protein complex [ATR, ATR-interacting protein (ATRIP), and Rad9] to damage sites, and H2O2-induced Chk1 phosphorylation.
Apurinic/apyrimidinic endonuclease 1 is the essential nuclease during immunoglobulin class switch recombination.
Yu et al., East Lansing, United States. In Mol Cell Biol, 2013
Finally, deletion of AP endonuclease 2 (APE2) has no effect on CSR in either APE1-proficient or -deficient cells.
Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase δ catalytic subunit gene, POLD1.
Sif et al., Columbus, United States. In J Biol Chem, 2012
Our findings show that PRMT7 negatively regulates expression of genes involved in DNA repair, including ALKBH5, APEX2, POLD1, and POLD2.
Small-molecule inhibitors of APE1 DNA repair function: an overview.
Review
Neamati et al., Los Angeles, United States. In Curr Mol Pharmacol, 2012
In addition, we give an overview of APE2, as well as other APE1 homologues in some disease-causing pathogens.
Apurinic/apyrimidinic endonuclease 2 is necessary for normal B cell development and recovery of lymphoid progenitors after chemotherapeutic challenge.
GeneRIF
Schrader et al., Worcester, United States. In J Immunol, 2011
Extensive analysis of bone marrow hematopoiesis in APE2-deficient mice finds inhibition of the pro-B to pre-B lymphocyte transition, due to a p53-dependent DNA damage response, independent from its ubiquitous and essential homolog APE1.
Apex2 is required for efficient somatic hypermutation but not for class switch recombination of immunoglobulin genes.
GeneRIF
Honjo et al., Kyoto, Japan. In Int Immunol, 2009
Apex2 is required for efficient somatic hypermutation of immunoglobulin genes.
Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'-5' exonuclease activities of human Ape2 in repair of oxidative DNA damage.
GeneRIF
Haracska et al., Szeged, Hungary. In Nucleic Acids Res, 2009
Ape2 may be involved in repair of oxidative DNA damage and PCNA-dependent repair synthesis.
Prefrontal cortex shotgun proteome analysis reveals altered calcium homeostasis and immune system imbalance in schizophrenia.
GeneRIF
Turck et al., São Paulo, Brazil. In Eur Arch Psychiatry Clin Neurosci, 2009
Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
The roles of APE1, APE2, DNA polymerase beta and mismatch repair in creating S region DNA breaks during antibody class switch.
Review
Stavnezer et al., Worcester, United States. In Philos Trans R Soc Lond B Biol Sci, 2009
We show that abasic sites are converted into single-strand breaks (SSBs) by apurinic/apyrimidinic endonucleases (APE1 and APE2).
Requirement for abasic endonuclease gene homologues in Arabidopsis seed development.
GeneRIF
Hatteroth et al., Davis, United States. In Plos One, 2008
plants with knock-out mutations in any one of Ape1L, Ape2, or Arp show no apparent differences from wild type in growth rate, growth habit, and fertility
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