An anchor site-type defect in human telomerase that disrupts telomere length maintenance and cellular immortalization
about
Finding the end: recruitment of telomerase to telomeresTelomerase Regulation from Beginning to the EndRegulation of cellular immortalization and steady-state levels of the telomerase reverse transcriptase through its carboxy-terminal domainThe TPR-containing domain within Est1 homologs exhibits species-specific roles in telomerase interaction and telomere length homeostasisCrystal structure of the essential N-terminal domain of telomerase reverse transcriptase.Telomeres in health and disease.The N-terminus of hTERT contains a DNA-binding domain and is required for telomerase activity and cellular immortalizationA novel motif in telomerase reverse transcriptase regulates telomere repeat addition rate and processivity.A mutation in the catalytic subunit of yeast telomerase alters primer-template alignment while promoting processivity and protein-DNA binding.The biogenesis and regulation of telomerase holoenzymesInTERTpreting telomerase structure and functionDirect involvement of the TEN domain at the active site of human telomerasePrediction of RNA binding sites in proteins from amino acid sequenceCharacterization of physical and functional anchor site interactions in human telomerase.Modeling and structure function analysis of the putative anchor site of yeast telomerase.A translocation-defective telomerase with low levels of activity and processivity stabilizes short telomeres and confers immortalization.Identification of an RNA aptamer binding hTERT-derived peptide and inhibiting telomerase activity in MCF7 cells.Multiple DNA-binding sites in Tetrahymena telomerase.Tracing the path of DNA substrates in active Tetrahymena telomerase holoenzyme complexes: mapping of DNA contact sites in the RNA subunitAn intact putative mouse telomerase essential N-terminal domain is necessary for proper telomere maintenance.Human Telomerase Reverse Transcriptase (hTERT) Positively Regulates 26S Proteasome Activity.Human telomerase domain interactions capture DNA for TEN domain-dependent processive elongation.Regulation of 5' template usage and incorporation of noncognate nucleotides by human telomerase.Striking similarities in diverse telomerase proteins revealed by combining structure prediction and machine learning approaches.Two-step mechanism involving active-site conformational changes regulates human telomerase DNA binding.
P2860
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P2860
An anchor site-type defect in human telomerase that disrupts telomere length maintenance and cellular immortalization
description
2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2005
@ast
im Juli 2005 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2005/07/01)
@sk
vědecký článek publikovaný v roce 2005
@cs
wetenschappelijk artikel (gepubliceerd op 2005/07/01)
@nl
наукова стаття, опублікована в липні 2005
@uk
مقالة علمية (نشرت في يوليو 2005)
@ar
name
An anchor site-type defect in ...... e and cellular immortalization
@ast
An anchor site-type defect in ...... e and cellular immortalization
@en
An anchor site-type defect in ...... e and cellular immortalization
@nl
type
label
An anchor site-type defect in ...... e and cellular immortalization
@ast
An anchor site-type defect in ...... e and cellular immortalization
@en
An anchor site-type defect in ...... e and cellular immortalization
@nl
prefLabel
An anchor site-type defect in ...... e and cellular immortalization
@ast
An anchor site-type defect in ...... e and cellular immortalization
@en
An anchor site-type defect in ...... e and cellular immortalization
@nl
P2093
P2860
P921
P3181
P356
P1476
An anchor site-type defect in ...... e and cellular immortalization
@en
P2093
Michael A. S. Taboski
Ryan J. Ward
Tara J. Moriarty
P2860
P304
P3181
P356
10.1091/MBC.E05-02-0148
P577
2005-07-01T00:00:00Z