Poly Adp Ribose Polymerases
Mostrando 1-7 de 7 artigos, teses e dissertações.
-
1. ADP-ribosylation: from molecular mechanisms to human disease
Abstract Post-translational modification of proteins by ADP-ribosylation, catalysed by poly (ADP-ribose) polymerases (PARPs) using NAD+ as a substrate, plays central roles in DNA damage signalling and repair, modulates a range of cellular signalling cascades and initiates programmed cell death by parthanatos. Here, we present mechanistic aspects of ADP-ribos
Genet. Mol. Biol.. Publicado em: 13/12/2019
-
2. Vias de inibição da apoptose em macrófagos J774 infectados com Leishmania (Leishmania) chagasi / Apoptosis inhibition pathways in J774 macrophages infected by Leishmania (L.) chagasi
Macrófagos infectados com Leishmania são protegidos de apoptose, entretanto não se conhece o mecanismo de transdução de sinal intracelular que interfere neste processo de morte. Neste trabalho, células J 774 em cultura, com privação de nutrientes, sofrem apoptose, a qual aumenta na presença dos indutores camptotecina (CPT) ou fator de necrose tumora
Publicado em: 2006
-
3. Role for the Related Poly(ADP-Ribose) Polymerases Tankyrase 1 and 2 at Human Telomeres
Telomere maintenance is essential for the continuous growth of tumor cells. In most human tumors telomeres are maintained by telomerase, a specialized reverse transcriptase. Tankyrase 1, a human telomeric poly(ADP-ribose) polymerase (PARP), positively regulates telomere length through its interaction with TRF1, a telomeric DNA-binding protein. Tankyrase 1 AD
American Society for Microbiology.
-
4. Tankyrase Polymerization Is Controlled by Its Sterile Alpha Motif and Poly(ADP-Ribose) Polymerase Domains
Tankyrases are novel poly(ADP-ribose) polymerases that have SAM and ankyrin protein-interaction domains. They are found at telomeres, centrosomes, nuclear pores, and Golgi vesicles and have been shown to participate in telomere length regulation. Their other function(s) are unknown, and it has been difficult to envision a common role at such diverse cellular
American Society for Microbiology.
-
5. Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse
The DNA damage-dependent poly(ADP-ribose) polymerases, PARP-1 and PARP-2, homo- and heterodimerize and are both involved in the base excision repair (BER) pathway. Here, we report that mice carrying a targeted disruption of the PARP-2 gene are sensitive to ionizing radiation. Following alkylating agent treatment, parp-2–/–-derived mouse embryonic fibrobl
Oxford University Press.
-
6. Poly(ADP-ribosyl)ation accelerates DNA repair in a pathway dependent on Cockayne syndrome B protein
Activation of poly(ADP-ribose)polymerases 1 and 2 (PARP-1 and PARP-2) is one of the earliest responses of mammalian cells to DNA damage by numerous genotoxic agents. We have analysed the influence of PARP inhibition, either achieved by over-expression of the DNA binding domain of PARP-1 or by treatment with 3,4-dihydro-5-[4-(1-piperidinyl)butoxyl]-1(2H)-isoq
Oxford University Press.
-
7. A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells.
Replication factor C (RF-C), a complex of five polypeptides, is essential for cell-free SV40 origin-dependent DNA replication and viability in yeast. The cDNA encoding the large subunit of human RF-C (RF-Cp145) was cloned in a Southwestern screen. Using deletion mutants of RF-Cp145 we have mapped the DNA binding domain of RF-Cp145 to amino acid residues 369-