| D011088 |
DNA Ligases |
Poly(deoxyribonucleotide):poly(deoxyribonucleotide)ligases. Enzymes that catalyze the joining of preformed deoxyribonucleotides in phosphodiester linkage during genetic processes during repair of a single-stranded break in duplex DNA. The class includes both EC 6.5.1.1 (ATP) and EC 6.5.1.2 (NAD). |
DNA Joinases,DNA Ligase,Polydeoxyribonucleotide Ligases,Polydeoxyribonucleotide Synthetases,T4 DNA Ligase,DNA Ligase, T4,Joinases, DNA,Ligase, DNA,Ligase, T4 DNA,Ligases, DNA,Ligases, Polydeoxyribonucleotide,Synthetases, Polydeoxyribonucleotide |
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| D011485 |
Protein Binding |
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. |
Plasma Protein Binding Capacity,Binding, Protein |
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| D004260 |
DNA Repair |
The removal of DNA LESIONS and/or restoration of intact DNA strands without BASE PAIR MISMATCHES, intrastrand or interstrand crosslinks, or discontinuities in the DNA sugar-phosphate backbones. |
DNA Damage Response |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D000072481 |
DNA Ligase ATP |
ATP-dependent cellular enzyme which catalyzes DNA replication, repair and recombination through formation of internucleotide ester bonds between phosphate and deoxyribose moieties. Vertebrate cells encode three well-characterized DNA ligases, DNA ligase I, III and IV, all of which are related in structure and sequence. DNA ligases either require ATP or NAD. However, archaebacterial, viral, and some eubacterial DNA ligases are ATP-dependent. |
ATP-Dependent DNA Ligase,DNA Ligase I,DNA Ligase II,DNA Ligase III,DNA Ligase IIIalpha,DNA Ligase IV,DNA Ligases, ATP-Dependent,LIGIIIalpha Protein,Polydeoxyribonucleotide Synthase ATP,ATP Dependent DNA Ligase,ATP, DNA Ligase,ATP, Polydeoxyribonucleotide Synthase,ATP-Dependent DNA Ligases,DNA Ligase, ATP-Dependent,DNA Ligases, ATP Dependent,IIIalpha, DNA Ligase,Ligase ATP, DNA,Ligase I, DNA,Ligase II, DNA,Ligase III, DNA,Ligase IIIalpha, DNA,Ligase IV, DNA,Ligase, ATP-Dependent DNA,Ligases, ATP-Dependent DNA,Synthase ATP, Polydeoxyribonucleotide |
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| D000089804 |
Shelterin Complex |
A TELOMERE cap complex consisting of telomere-specific proteins in association with telomeric DNA such as telomeric dsDNA-sDNA junction. They are involved in the protection of chromosome ends and TELOMERASE regulation and play a role in CELLULAR SENESCENCE and ageing-related pathology. In general it consists of six mostly TELOMERE-BINDING PROTEINS (POT1, RAP1, TIN2, TPP1, TRF1, and TRF2). |
CST Complex,Ctc1-Stn1-Ten1 Complex,POT1-TPP1 Shelterin Complex,Telomere Cap Complex,Telomere POT1-TPP1 Complex,Telomeric Capping Complex,Telomeric Stn1-Ten1 Capping Complex,Telosome,Capping Complex, Telomeric,Complex, CST,Complex, Ctc1-Stn1-Ten1,Complex, POT1-TPP1 Shelterin,Complex, Shelterin,Complex, Telomere POT1-TPP1,Complex, Telomeric Capping,Ctc1 Stn1 Ten1 Complex,POT1 TPP1 Shelterin Complex,POT1-TPP1 Complex, Telomere,Shelterin Complex, POT1-TPP1,Telomere POT1 TPP1 Complex,Telomeric Stn1 Ten1 Capping Complex,Telosomes |
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| D013379 |
Substrate Specificity |
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. |
Specificities, Substrate,Specificity, Substrate,Substrate Specificities |
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| D016615 |
Telomere |
A terminal section of a chromosome which has a specialized structure and which is involved in chromosomal replication and stability. Its length is believed to be a few hundred base pairs. |
Telomeres |
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| D043603 |
DNA-(Apurinic or Apyrimidinic Site) Lyase |
A DNA repair enzyme that catalyses the excision of ribose residues at apurinic and apyrimidinic DNA sites that can result from the action of DNA GLYCOSYLASES. The enzyme catalyzes a beta-elimination reaction in which the C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. This enzyme was previously listed under EC 3.1.25.2. |
Apurinic DNA Endonuclease,DNA Lyase (Apurinic or Apyrimidinic),Endodeoxyribonuclease (Apurinic or Apyrimidinic),AP Endonuclease,AP Lyase,Apurine-Apyrimidine Endonuclease,Apurinic Endonuclease,Apurine Apyrimidine Endonuclease,DNA Endonuclease, Apurinic,Endonuclease, AP,Endonuclease, Apurine-Apyrimidine,Endonuclease, Apurinic,Endonuclease, Apurinic DNA |
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| D045585 |
Flap Endonucleases |
Endonucleases that remove 5' DNA sequences from a DNA structure called a DNA flap. The DNA flap structure occurs in double-stranded DNA containing a single-stranded break where the 5' portion of the downstream strand is too long and overlaps the 3' end of the upstream strand. Flap endonucleases cleave the downstream strand of the overlap flap structure precisely after the first base-paired nucleotide, creating a ligatable nick. |
Flap Endonuclease,FEN-1,Fen1 Protein,Flap Endonuclease-1,RAD2 Homolog-1 Nuclease,RTH-1 Nuclease,Endonuclease, Flap,Endonuclease-1, Flap,Endonucleases, Flap,Flap Endonuclease 1,Nuclease, RTH-1,RAD2 Homolog 1 Nuclease,RTH 1 Nuclease |
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