The APOBEC Protein Family: United by Structure, Divergent in Function.
about
Opossum APOBEC1 is a DNA mutator with retrovirus and retroelement restriction activity.Structural determinants of APOBEC3B non-catalytic domain for molecular assembly and catalytic regulationHepatitis B virus X protein is capable of down-regulating protein level of host antiviral protein APOBEC3G.Reactivation of dormant anti-tumor immunity - a clinical perspective of therapeutic immune checkpoint modulation.DNA mutagenic activity and capacity for HIV-1 restriction of the cytidine deaminase APOBEC3G depend on whether DNA or RNA binds to tyrosine 315.RNA binding to APOBEC deaminases; Not simply a substrate for C to U editing.Nanoscale Characterization of Interaction of APOBEC3G with RNA.Roles of APOBEC3A and APOBEC3B in Human Papillomavirus Infection and Disease Progression.APOBEC3G acts as a therapeutic target in mesenchymal gliomas by sensitizing cells to radiation-induced cell death.APOBEC Enzymes as Targets for Virus and Cancer Therapy.Deazaguanine derivatives, examples of crosstalk between RNA and DNA modification pathways.Molecular Interactions of a DNA Modifying Enzyme APOBEC3F Catalytic Domain with a Single-Stranded DNA.Hydrogen bonds are a primary driving force for de novo protein folding.Computational Model and Dynamics of Monomeric Full-Length APOBEC3G.Enzyme cycling contributes to efficient induction of genome mutagenesis by the cytidine deaminase APOBEC3B.Utility of high-throughput DNA sequencing in the study of the human papillomaviruses.Deep sequencing of HIV-1 reverse transcripts reveals the multifaceted antiviral functions of APOBEC3G.Viral subversion of APOBEC3s: Lessons for anti-tumor immunity and tumor immunotherapy.Mechanisms for targeted, purposeful mutation revealed in an APOBEC-DNA complex.Mitochondrial complex II regulates a distinct oxygen sensing mechanism in monocytes.APOBEC3 induces mutations during repair of CRISPR-Cas9-generated DNA breaks.Commentary: Programmable base editing of A·T to G·C in genomic DNA without DNA cleavage.Expansions, diversification, and interindividual copy number variations of AID/APOBEC family cytidine deaminase genes in lampreys.Can modulators of apolipoproteinB biogenesis serve as an alternate target for cholesterol-lowering drugs?Emergency Services of Viral RNAs: Repair and Remodeling.Correlation of gene expression and associated mutation profiles of APOBEC3A, APOBEC3B, REV1, UNG, and FHIT with chemosensitivity of cancer cell lines to drug treatment.Characterization of BK Polyomaviruses from Kidney Transplant Recipients Suggests a Role for APOBEC3 in Driving In-Host Virus Evolution.Diversification of AID/APOBEC-like deaminases in metazoa: multiplicity of clades and widespread roles in immunity.AID/APOBEC-like cytidine deaminases are ancient innate immune mediators in invertebrates.Modeling the Embrace of a Mutator: APOBEC Selection of Nucleic Acid LigandsGenetic and mechanistic basis for APOBEC3H alternative splicing, retrovirus restriction, and counteraction by HIV-1 proteaseDirect AFM Visualization of the Nanoscale Dynamics of Biomolecular ComplexesAPOBEC3B Activity Is Prevalent in Urothelial Carcinoma Cells and Only Slightly Affected by LINE-1 Expression
P2860
Q33587739-B6FAD0E0-D53A-48F2-8A06-10773479D62AQ33878087-566C07E1-DAB4-4BC5-987F-1DC495770A7DQ37591195-CD02F28F-574D-4823-B09E-ACC8CB7CC27EQ37593573-42F92AE6-42A3-4143-A8AA-179E364724D4Q38708725-D2B5F4B8-5D0D-46C2-BCFF-15C09853E513Q39015203-5E527068-B793-44A1-9448-60A01DE48800Q39059117-CA5795E2-5188-41DA-8CF2-850FBCC97017Q40076776-B54195E1-4EEA-4F46-99C5-2E16704DF157Q41552553-68284243-3177-4091-96D4-4FBA90E5BED5Q45324625-0EC3BE34-44B0-47D1-B363-AC4314420EC9Q45839282-AFD0DB42-AC90-4DAE-9BEF-18D60296C9B6Q46172691-7DCF07E4-9110-4D67-A4DC-4C8D6E4F484DQ47130583-52BE5AE7-6518-4B9A-8A9E-EDCBC6795BE7Q47132528-EB6E421D-55BD-40EC-8C2E-C0EE2BE658A6Q47152216-50F30D67-58B3-489C-84DB-C97D1A67CB26Q47240892-FE20B374-CCD3-408E-B10D-2FF5782E274BQ47380909-3FD49837-C91C-4DD9-8627-3E4331C489C7Q47568875-528EAB8E-4E44-4132-8C57-2FC166378CD5Q47587699-97744450-57F0-4FAE-A2E7-D688EB9D4305Q47973346-52986436-BEA7-41FE-93D7-8345CF17A127Q48262515-2FA72F67-05D5-41C8-98BB-EEF30D97BB10Q50204211-EE378350-E9B8-42AD-929F-F66737EA83D0Q51146554-840F9A38-243B-46BA-B091-1B647204BC8EQ52600967-6142B11E-EB22-4FEF-950D-41272447B907Q52655516-67C9B2FB-36B6-407A-B2BD-D4E722474E53Q52719995-1ED91BEE-4B98-4571-8EE7-602CA6E9528CQ54215480-0D9AC1C6-E666-4F0C-8884-347C10BC80DBQ54253085-8A786B38-1DC7-43A2-8C15-8D5140F657F8Q55092316-305C8F90-DBB4-436B-A0C9-7AE77DB3F676Q57173759-23F45775-0FB2-4ABB-B159-C61E996A5DE1Q57295397-FFDE7F6B-9DFB-41CE-923D-AE4B5B658590Q58581575-C01959BA-F778-4D1C-BC21-A0B806640DB8Q58764658-F8873916-26C9-4BC3-A1A0-01445F7A0581
P2860
The APOBEC Protein Family: United by Structure, Divergent in Function.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年学术文章
@wuu
2016年学术文章
@zh-cn
2016年学术文章
@zh-hans
2016年学术文章
@zh-my
2016年学术文章
@zh-sg
2016年學術文章
@yue
2016年學術文章
@zh
2016年學術文章
@zh-hant
name
The APOBEC Protein Family: United by Structure, Divergent in Function.
@en
type
label
The APOBEC Protein Family: United by Structure, Divergent in Function.
@en
prefLabel
The APOBEC Protein Family: United by Structure, Divergent in Function.
@en
P2860
P1476
The APOBEC Protein Family: United by Structure, Divergent in Function.
@en
P2093
Jason D Salter
Ryan P Bennett
P2860
P304
P356
10.1016/J.TIBS.2016.05.001
P50
P577
2016-05-30T00:00:00Z