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Human Monoclonal POLI Primary Antibody for ELISA, WB - ABIN564869
Wang, Woodgate, McManus, Mead, McCormick, Maher: Evidence that in xeroderma pigmentosum variant cells, which lack DNA polymerase eta, DNA polymerase iota causes the very high frequency and unique spectrum of UV-induced mutations. in Cancer research 2007
Show all 3 references for ABIN564869
Human Polyclonal POLI Primary Antibody for ELISA, WB - ABIN1534839
McDonald, Rapić-Otrin, Epstein, Broughton, Wang, Lehmann, Wolgemuth, Woodgate: Novel human and mouse homologs of Saccharomyces cerevisiae DNA polymerase eta. in Genomics 1999
Germline genetic variations in human POLI gene may either hinder or promote the translesion synthesis (TLS (show FUS Antibodies)) capability of pol iota (show POLM Antibodies) with various DNA lesions in vitro, emphasizing the potential translational importance of these pol iota (show POLM Antibodies) genetic variations, e.g., individual differences in TLS (show FUS Antibodies), mutation, and cancer susceptibility to genotoxic carcinogens.
a single residue in pol iota (show POLM Antibodies) is able to discriminate between NTPs and dNTPs during DNA synthesis.
Dysregulation of pol iota (show POLM Antibodies) by JNK/c-Jun is involved in carcinogenesis and offer a novel understanding of the role of pol iota (show POLM Antibodies) or c-Jun (show JUN Antibodies) in mutagenesis.
Human Pol iota and yeast Pol zeta complex could function efficiently in the insertion and extension steps, respectively, of ranslesion synthesis and human Pol kappa and Pol eta could also extend past these lesions, albeit much less efficiently.
POLI and MC4R (show MC4R Antibodies) nearby single nucleotide polymorphisms in human chromosome 18 are associated with a moderate risk of type 2 diabetes.
Results show that the physical and functional interaction between pols eta and iota occurs between ubiquitinated forms of either polymerase via their respective ubiquitin-binding domains.
this review briefly discusses the main structural features and possible functional mechanisms of the active center of Pol iota (show POLM Antibodies). [review]
structural mechanism of high-fidelity 8-oxo-G replication by a human DNA polymerase (show POLB Antibodies)
Structural basis for proficient incorporation of dTTP opposite O6-methylguanine by human DNA polymerase iota.
In the presence of Mn2 (show MUC7 Antibodies)+, the Pol iota activity in carcinoma was 2.5-fold higher than the control cells.
PolH (show POLH Antibodies) contributes to accurate translesion synthesis (TLS (show FUS Antibodies)) past both T- & C-containing dimers. PolI is involved in error-prone TLS (show FUS Antibodies) past cytosine-containing dimers when Poleta is inactivated.
Poliota causes the Par2 (show F2RL1 Antibodies) effect and inhibits tumorigenesis and mutagenesis
Upon DNA damage, the UBDs (UBM domains) of polymerase iota (Pol iota) interact with ubiquitinated proliferating cell nuclear antigen (show PCNA Antibodies) to regulate the interchange between processive DNA polymerases and translesional synthesis
In the presence of Mg2 (show MCOLN1 Antibodies)+, the enzyme was active only in testicles and brain, whereas in the presence of Mn2+ the activity was found in all organs.
Data suggest that either DNA polymerase iota does not participate in hypermutation, or its role is nonessential and can be readily assumed by another low-fidelity polymerase.
Nucleotide polymorphisms in DNA polymerase iota is associated with lung tumorigenesis in mouse and humans
Pol kappa (show POLL Antibodies) and Pol iota double-deficient mice had the normal somatic hypermutation frequency
Pol iota gene may participate in error-free repair of damaged DNA and prevention of lung tumor development
identification of two previously unknown ubiquitin-binding domains in the Y-family translesion synthesis polymerases that enable them to interact with monoubiquitinated targets and undergo monoubiquitination in vivo
suggest the involvement of the Pol eta and Pol iota proteins in UV-induced skin carcinogenesis
Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity (By similarity).
DNA polymerase iota
, polymerase (DNA directed) iota
, DNA polymerase iota-like
, RAD30 homolog B
, polymerase (DNA-directed), iota