Evidence map›Paper›PMID 12853623›Full record

ArticleNucleic acids research2003

The C terminus of the human telomerase reverse transcriptase is a determinant of enzyme processivity.

Sylvain Huard, Tara J Moriarty, Chantal Autexier

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

47 citing papers in PubMed, 98 citations in OpenAlex.

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  4. Establishment of an Efficient Immortalization Strategy Using HMEJ-Based bInternational journal of molecular sciences · 2021
    Article
  5. Review
  6. Therapeutic Targets in Telomerase and Telomere Biology of Cancers.Indian journal of clinical biochemistry : IJCB · 2020
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Sylvain HuardDepartment of Anatomy and Cell Biology, McGill University, Montréal, Québec, Canada, H3A 2B4.
Tara J Moriarty
Chantal Autexier
McGill University · CA

Funding

CIHR 54638
6 · The paper itself

Abstract

The catalytic subunit of telomerase (TERT) contains conserved reverse transcriptase-like motifs but N- and C-terminal regions unique to telomerases. Despite weak sequence conservation, the C terminus of TERTs from various organisms has been implicated in telomerase-specific functions, including telomerase activity, functional multimerization with other TERT molecules, enzyme processivity and telomere length maintenance. We studied hTERT proteins containing small C-terminal deletions or substitutions to identify and characterize hTERT domains mediating telomerase activity, hTERT multimerization and processivity. Using sequence alignment of five vertebrate TERTs and Arabidopsis thaliana TERT, we identified blocks of highly conserved amino acids that were required for human telomerase activity and functional hTERT complementation. We adapted the non-PCR-based telomerase elongation assay to characterize telomerase expressed and reconstituted in the in vitro transcription/translation rabbit reticulocyte lysate system. Using this assay, we found that the hTERT C terminus, like the C terminus of Saccharomyces cerevisiae TERT, contributes to successive nucleotide addition within a single 6-base telomeric repeat (type I processivity). Certain mutations in the hTERT C terminus also reduced the repetitive addition of multiple telomeric repeats (type II processivity). Our results suggest a functionally conserved role for the TERT C terminus in telomerase enzyme processivity.

Indexed as

Amino Acid SequenceCatalysisCatalytic DomainDNA-Binding ProteinsHumansMolecular Sequence DataMutationProtein BiosynthesisSequence AlignmentSequence Homology, Amino AcidTelomeraseTelomereTranscription, GeneticDNA-Binding ProteinsTelomeraseTERT protein, human

Identifiers

PMID12853623
PMCPMC165952
OpenAlexW2073343115

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.