J
Jeremy D. Henson
Researcher at University of New South Wales
Publications - 34
Citations - 2783
Jeremy D. Henson is an academic researcher from University of New South Wales. The author has contributed to research in topics: Telomere & Telomerase. The author has an hindex of 17, co-authored 29 publications receiving 2448 citations. Previous affiliations of Jeremy D. Henson include Children's Medical Research Institute & University of Sydney.
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Journal ArticleDOI
Alternative lengthening of telomeres in mammalian cells
TL;DR: The existence of ALT adds some complexity to proposed uses of telomere-related parameters in cancer diagnosis and prognosis, and poses challenges for the design of anticancer therapeutics designed to inhibit telomeres maintenance.
Journal ArticleDOI
DNA C-circles are specific and quantifiable markers of alternative-lengthening-of-telomeres activity
Jeremy D. Henson,Ying Cao,Lily I. Huschtscha,Andy C.-M. Chang,Amy Y.M. Au,Hilda A. Pickett,Roger R. Reddel +6 more
TL;DR: It is shown that partially single-stranded telomeric (CCCTAA)n DNA circles (C-circles) are ALT specific, and the C-circle assay (CC assay) may have clinical utility for diagnosis and management of ALT+ tumors.
Journal Article
A robust assay for alternative lengthening of telomeres in tumors shows the significance of alternative lengthening of telomeres in sarcomas and astrocytomas.
Jeremy D. Henson,Jonathan A. F. Hannay,Stanley W. McCarthy,Janice A. Royds,Janice A. Royds,Thomas Yeager,Robert A. Robinson,Stephen B. Wharton,D A Jellinek,Susan Arbuckle,Jinyoung Yoo,Bruce G. Robinson,Diana L. Learoyd,Paul Stalley,S. Fiona Bonar,Dihua Yu,Raphael E. Pollock,Roger R. Reddel,Roger R. Reddel +18 more
TL;DR: It showed that a substantial proportion of STS, osteosarcomas, and astrocytomas, but not papillary thyroid carcinomas use ALT, and the APB assay for ALT is suitable for paraffin-embedded tumors.
Journal ArticleDOI
Assaying and investigating Alternative Lengthening of Telomeres activity in human cells and cancers
TL;DR: Each of the current ALT assays and their implications for understanding the ALT mechanism are assessed.
Journal ArticleDOI
Suppression of Alternative Lengthening of Telomeres by Sp100-Mediated Sequestration of the MRE11/RAD50/NBS1 Complex
Wei-Qin Jiang,Ze-Huai Zhong,Jeremy D. Henson,Axel A. Neumann,Andy C.-M. Chang,Roger R. Reddel +5 more
TL;DR: It is demonstrated here that overexpression of Sp100, a constituent of promyelocytic leukemia nuclear bodies, sequestered the MRE11, RAD50, and NBS1 recombination proteins away from APBs, which resulted in repression of the ALT mechanism, as evidenced by progressive telomere shortening at 121 bp per population doubling.