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Research paper thumbnail of Soft equations of state for neutron-star matter ruled out by EXO 0748-676

NATURE-LONDON-, Jan 1, 2006

The interiors of neutron stars contain matter at very high densities, in a state that differs gre... more The interiors of neutron stars contain matter at very high densities, in a state that differs greatly from those found in the early Universe or achieved in terrestrial experiments 1 . Matter in these conditions can only be probed through astrophysical observations that measure the mass and radius of neutron stars with sufficient precision 2 . Here I report a determination of the mass and radius of the neutron star EXO 07482676 that appears to rule out all the soft equations of state of neutron-star matter. If this object is typical, then condensates 2 and unconfined quarks 1 do not exist in the centres of neutron stars.

Research paper thumbnail of The discovery of 3.8 hour periodic intensity dips and eclipses from the transient low-mass X-ray binary EXO 0748-676

The Astrophysical …, Jan 1, 1986

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Research paper thumbnail of Aging-dependent large accumulation of point mutations in the human mtDNA control region for replication

Research paper thumbnail of Calf 5′ to 3′ exo/endonuclease must slide from a 5′ end of the substrate to perform structure-specific cleavage

Journal of Biological Chemistry, Jan 1, 1995

Calf 5 to 3 exo/endonuclease, the counterpart of the human FEN-1 and yeast RTH-1 nucleases, perfo... more Calf 5 to 3 exo/endonuclease, the counterpart of the human FEN-1 and yeast RTH-1 nucleases, performs structure-specific cleavage of both RNA and DNA and is implicated in Okazaki fragment processing and DNA repair. The substrate for endonuclease activity is a primer annealed to a template but with a 5 unannealed tail. The results presented here demonstrate that the nuclease must enter the 5 end of the unannealed tail and then slide to the region of hybridization where the cleavage occurs. The presence of bound protein or a primer at any point on the single-stranded tail prevents cleavage. However, biotinylation of a nucleotide at the 5 end or internal to the tail does not prevent cleavage. The sliding process is bidirectional. If the nuclease slides onto the tail, later binding of a primer to the tail traps the nuclease between the primer binding site and the cleavage site, preventing the nuclease from departing from the 5 end. A model for 5 entry, sliding, and cleavage is presented. The possible role of this unusual mechanism in Okazaki fragment processing, DNA repair, and protection of the replication fork from inappropriate endonucleolytic cleavage is presented.

Research paper thumbnail of Soft equations of state for neutron-star matter ruled out by EXO 0748-676

NATURE-LONDON-, Jan 1, 2006

The interiors of neutron stars contain matter at very high densities, in a state that differs gre... more The interiors of neutron stars contain matter at very high densities, in a state that differs greatly from those found in the early Universe or achieved in terrestrial experiments 1 . Matter in these conditions can only be probed through astrophysical observations that measure the mass and radius of neutron stars with sufficient precision 2 . Here I report a determination of the mass and radius of the neutron star EXO 07482676 that appears to rule out all the soft equations of state of neutron-star matter. If this object is typical, then condensates 2 and unconfined quarks 1 do not exist in the centres of neutron stars.

Research paper thumbnail of The discovery of 3.8 hour periodic intensity dips and eclipses from the transient low-mass X-ray binary EXO 0748-676

The Astrophysical …, Jan 1, 1986

The user has requested enhancement of the downloaded file.

Research paper thumbnail of Aging-dependent large accumulation of point mutations in the human mtDNA control region for replication

Research paper thumbnail of Calf 5′ to 3′ exo/endonuclease must slide from a 5′ end of the substrate to perform structure-specific cleavage

Journal of Biological Chemistry, Jan 1, 1995

Calf 5 to 3 exo/endonuclease, the counterpart of the human FEN-1 and yeast RTH-1 nucleases, perfo... more Calf 5 to 3 exo/endonuclease, the counterpart of the human FEN-1 and yeast RTH-1 nucleases, performs structure-specific cleavage of both RNA and DNA and is implicated in Okazaki fragment processing and DNA repair. The substrate for endonuclease activity is a primer annealed to a template but with a 5 unannealed tail. The results presented here demonstrate that the nuclease must enter the 5 end of the unannealed tail and then slide to the region of hybridization where the cleavage occurs. The presence of bound protein or a primer at any point on the single-stranded tail prevents cleavage. However, biotinylation of a nucleotide at the 5 end or internal to the tail does not prevent cleavage. The sliding process is bidirectional. If the nuclease slides onto the tail, later binding of a primer to the tail traps the nuclease between the primer binding site and the cleavage site, preventing the nuclease from departing from the 5 end. A model for 5 entry, sliding, and cleavage is presented. The possible role of this unusual mechanism in Okazaki fragment processing, DNA repair, and protection of the replication fork from inappropriate endonucleolytic cleavage is presented.

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