Nucleolin interacts with telomerase (Q28282467)

1

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Kenkichi Masutomi

2

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Luvsanjav Delgermaa

3

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Kuniaki Arai

4

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Naoki Oishi

5

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Hideki Mizuno

6

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Naoyuki Hayashi

7

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Seishi Murakami

Journal of Biological Chemistry

9

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language of work or name

English

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publication date

3 December 2004

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published in

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volume

279

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page(s)

51508-15

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issue

49

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cites work

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Reconstitution of human telomerase activity in vitro

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The RNA component of human telomerase

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Telomerase activity reconstituted in vitro with purified human telomerase reverse transcriptase and human telomerase RNA component.

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Dissociation among in vitro telomerase activity, telomere maintenance, and cellular immortalization

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N-terminal domains of the human telomerase catalytic subunit required for enzyme activity in vivo

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C-terminal regions of the human telomerase catalytic subunit essential for in vivo enzyme activity

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Functional requirement of p23 and Hsp90 in telomerase complexes

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Stable association of hsp90 and p23, but Not hsp70, with active human telomerase

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Subnuclear shuttling of human telomerase induced by transformation and DNA damage.

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Nucleolar localization of hTERT protein is associated with telomerase function

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The nucleolar localization domain of the catalytic subunit of human telomerase

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The nucleolus: an old factory with unexpected capabilities

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The nucleolus and the four ribonucleoproteins of translation

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A box H/ACA small nucleolar RNA-like domain at the human telomerase RNA 3' end

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Nucleolar localization signals of box H/ACA small nucleolar RNAs

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Nucleolin: a multifunctional major nucleolar phosphoprotein

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Purification and characterization of nucleolin and its identification as a transcription repressor.

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Direct interaction between nucleolin and hepatitis C virus NS5B

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Two independent regions of human telomerase reverse transcriptase are important for its oligomerization and telomerase activity

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RNA-dependent RNA polymerase activity of the soluble recombinant hepatitis C virus NS5B protein truncated at the C-terminal region

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Telomerase maintains telomere structure in normal human cells.

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Telomerase RNA Accumulates in Cajal Bodies in Human Cancer Cells

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Nucleolar protein PinX1p regulates telomerase by sequestering its protein catalytic subunit in an inactive complex lacking telomerase RNA

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The telomere lengthening mechanism in telomerase-negative immortal human cells does not involve the telomerase RNA subunit

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Expression of mutant telomerase in immortal telomerase-negative human cells results in cell cycle deregulation, nuclear and chromosomal abnormalities and rapid loss of viability

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Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal.

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Telomerase RNA structure and function: implications for dyskeratosis congenita.

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