Single molecule studies of physiologically relevant telomeric tails reveal POT1 mechanism for promoting G-quadruplex unfolding

Journal of Biological Chemistry

Volumn 286, Issue 9, 2011, Pages 7479-7489

  Wang, Hong ^a,b   Nora, Gerald J ^c,d   Ghodke, Harshad ^a,d   Opresko, Patricia L ^c,d,e  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF PITTSBURGH CANCER INSTITUTE   (United States)

^c UNIVERSITY OF PITTSBURGH GRADUATE SCHOOL OF PUBLIC HEALTH   (United States)

^d UNIVERSITY OF PITTSBURGH   (United States)

^e Bridgeside Point   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTISENSE OLIGONUCLEOTIDES; ATOMIC FORCE; DNA MOLECULES; G-QUADRUPLEXES; HUMAN CELLS; QUADRUPLEXES; SINGLE MOLECULE; SINGLE-MOLECULE STUDIES; SINGLE-STRANDED DNA; STRUCTURAL BASIS; STRUCTURAL STUDIES; TELOMERE LENGTH; TELOMERES; TELOMERIC DNA;

ATOMIC FORCE MICROSCOPY; DNA; MOLECULES; OLIGONUCLEOTIDES; PHYSIOLOGY;

NUCLEIC ACIDS;

ANTISENSE OLIGONUCLEOTIDE; GUANINE QUADRUPLEX; POT1 PROTEIN; PROTECTION OF TELOMERE PROTEIN; PROTEIN; SHELTERIN; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

ARTICLE; ATOMIC FORCE MICROSCOPY; CONTROLLED STUDY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DNA BINDING; TANDEM REPEAT; TELOMERE;

ANIMALS; CELL LINE; COMBINATORIAL CHEMISTRY TECHNIQUES; DNA, SINGLE-STRANDED; G-QUADRUPLEXES; HUMANS; INSECTS; MICROSCOPY, ATOMIC FORCE; MODELS, CHEMICAL; OLIGONUCLEOTIDES, ANTISENSE; PROTEIN BINDING; TELOMERE; TELOMERE-BINDING PROTEINS;

EID: 79953219455     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.205641     Document Type: Article

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