A calmodulin-like protein (LCALA) is a new Leishmania amazonensis candidate for telomere end-binding protein

Morea, Edna G.O; Viviescas, Maria Alejandra; Fernandes, Carlos A.H; Matioli, Fabio F; Lira, Cristina B.B; Fernandez, Maribel F; Moraes, Barbara S; Silva, Marcelo Santos da; Storti, Camila B; Fontes, Marcos R.M; Cano, Maria Isabel N.
Biochim. Biophys. Acta-Gen. Subj. ; 1861(11): 2583-2597, 2017.
Artículo en Inglés | SES-SP, SESSP-IBPROD, SES-SP | ID: but-ib15571

Documentos relacionados

  1. A calmodulin-like protein (LCALA) is a new Leishmania amazonensis candidate for telomere end-binding protein.
  2. RPA engages telomeric G-quadruplexes more effectively than CST.
  3. Models for human telomere C-strand fill-in by CST-Polα-primase.
  4. Shelterin reduces the accessibility of telomeric overhangs.
  5. The natural absence of RPA1N domain did not impair Leishmania amazonensis RPA-1 participation in DNA damage response and telomere protection.
  6. Interrogating accessibility of telomeric sequences with FRET-PAINT: evidence for length-dependent telomere compaction.
  7. Investigating the Effect of Mono- and Dimeric 360A G-Quadruplex Ligands on Telomere Stability by Single Telomere Length Analysis (STELA).
  8. C. elegans telomeres contain G-strand and C-strand overhangs that are bound by distinct proteins.
  9. Reconstitution of a telomeric replicon organized by CST.
  10. DNA-RNA hybrid G-quadruplex tends to form near the 3' end of telomere overhang.