POT1-TPP1 enhances telomerase processivity by slowing primer dissociation and aiding translocation (Q30449985)

13 September 2017

POT1-TPP1 enhances telomerase processivity by slowing primer dissociation and aiding translocation (English)

1 reference

13 September 2017

2

Thomas R Cech

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13 September 2017

Chrysa M Latrick

1

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language of work or name

English

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publication date

21 January 2010

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13 September 2017

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13 September 2017

29

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13 September 2017

5

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13 September 2017

924-933

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PMC publication ID

2837173

describes a project that uses

13 September 2017

ImageQuant

1 reference

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2837173/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

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Telomere extension occurs at most chromosome ends and is uncoupled from fill-in in human cancer cells

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The POT1-TPP1 telomere complex is a telomerase processivity factor

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TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase

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Loss of hPot1 function leads to telomere instability and a cut-like phenotype

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20 June 2018

Telomerase is processive

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20 June 2018

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Human telomerase RNA accumulation in Cajal bodies facilitates telomerase recruitment to telomeres and telomere elongation

21 January 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/20094033

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Low- to high-throughput analysis of telomerase modulators with Telospot

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/20094033

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/EMBOJ.2009.409

1 reference

13 September 2017

1 reference

PMC publication ID

2837173

13 September 2017

PubMed publication ID

20094033

1 reference

PMC publication ID

2837173