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Cited by 1,012

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Tankyrase, a Poly(ADP-Ribose) Polymerase at Human Telomeres

Smith, Susan, Giriat, Izabela, Schmitt, Anja, de Lange, Titia·1998·Science

Abstract

Tankyrase, a protein with homology to ankyrins and to the catalytic domain of poly(adenosine diphosphate–ribose) polymerase (PARP), was identified and localized to human telomeres. Tankyrase binds to the telomeric protein TRF1 (telomeric repeat binding factor–1), a negative regulator of telomere length maintenance. Like ankyrins, tankyrase contains 24 ankyrin repeats in a domain responsible for its interaction with TRF1. Recombinant tankyrase was found to have PARP activity in vitro, with both TRF1 and tankyrase functioning as acceptors for adenosine diphosphate (ADP)–ribosylation. ADP-ribosylation of TRF1 diminished its ability to bind to telomeric DNA in vitro, suggesting that telomere function in human cells is regulated by poly(ADP-ribosyl)ation.

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Metadata

Authors
Smith, S., Giriat, I., Schmitt, A., & de Lange, T.
Venue
Science
Published
1998-11-20
Volume
282
Issue
5393
Pages
1484-1487
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2112671059
Cited by
1,012
References
4
FWCI
38.95
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Tankyrase, a Poly(ADP-Ribose) Polymerase at Human Telomeres. https://app.cochat.ai/papers/10.1126/science.282.5393.1484
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Smith, S., Giriat, I., Schmitt, A., & de Lange, T. (1998). Tankyrase, a Poly(ADP-Ribose) Polymerase at Human Telomeres. Science. https://doi.org/10.1126/science.282.5393.1484

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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