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William K. Holloman

Researcher at Cornell University

Publications -  107
Citations -  5741

William K. Holloman is an academic researcher from Cornell University. The author has contributed to research in topics: DNA & DNA repair. The author has an hindex of 34, co-authored 104 publications receiving 5506 citations. Previous affiliations of William K. Holloman include University of Florida & National Institute for Medical Research.

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Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis

Jörg Kämper, +80 more
- 02 Nov 2006 - 
TL;DR: The discovery of the secreted protein gene clusters and the functional demonstration of their decisive role in the infection process illuminate previously unknown mechanisms of pathogenicity operating in biotrophic fungi.
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Correction of the Mutation Responsible for Sickle Cell Anemia by an RNA-DNA Oligonucleotide

TL;DR: A chimeric oligonucleotide composed of DNA and modified RNA residues was used to direct correction of the mutation in the hemoglobin βS allele and there was a detectable level of gene conversion of the mutant allele to the normal sequence.
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The BRCA2 homologue Brh2 nucleates RAD51 filament formation at a dsDNA-ssDNA junction.

TL;DR: It is shown that a full-length BRCA2 homologue (Brh2) stimulates Rad51-mediated recombination at substoichiometric concentrations relative to Rad51, establishing a BRC a2 function in RAD51- mediated DSB repair and explaining the loss of this repair capacity in BRCa2-associated cancers.
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Isolation and characterization of an autonomously replicating sequence from Ustilago maydis.

TL;DR: DNA fragments that function as autonomously replicating sequences (ARSs) have been isolated from Ustilago maydis and when inserted into an integrative transforming vector, the fragments increased the frequency of U. maydis transformation several-thousandfold.
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Binding and melting of D-loops by the Bloom syndrome helicase.

TL;DR: A model in which BLM selectively dissociates recombination intermediates likely to be unfavorable for recombination-promoted replication is proposed and found that BLM preferentially melts those D-loops that are formed more favorably by the strand exchange protein Rad51, but whose polarity could be less favorable for enabling restoration of an active replication fork.