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Hongshan Zhang

Researcher at University of Texas at Austin

Publications -  22
Citations -  720

Hongshan Zhang is an academic researcher from University of Texas at Austin. The author has contributed to research in topics: Biology & Cohesin. The author has an hindex of 6, co-authored 15 publications receiving 460 citations. Previous affiliations of Hongshan Zhang include Shanxi University & Aix-Marseille University.

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Human cohesin compacts DNA by loop extrusion

TL;DR: It is shown that in the presence of the NIPBLMAU2 protein complex, the human cohesin complex can function as a molecular motor that extrudes DNA loops with high speed in vitro and compacts DNA in an ATP-dependent manner.
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Sliding sleeves of XRCC4–XLF bridge DNA and connect fragments of broken DNA

TL;DR: Observations suggest that XRCC4–XLF complexes form mobile sleeve-like structures around DNA that can reconnect the broken ends very rapidly and hold them together, which will lead to clarification of how NHEJ proteins are involved in generating chromosomal translocations.
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Photoassociative formation of ultracold RbCs molecules in the ( 2 ) 3 Π state

TL;DR: In this paper, the photoassociative formation of RbCs molecules in the excited state correlated to the vibrational level was investigated in detail, and the rotational constant and centrifugal distortion constant were derived to be 0.01304 cm and 0.000015 cm, respectively.
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Human RAD52 Captures and Holds DNA Strands, Increases DNA Flexibility, and Prevents Melting of Duplex DNA: Implications for DNA Recombination

TL;DR: RAD52 binding changes the nature of the overstretching transition of dsDNA and prevents DNA melting, which is advantageous for strand clamping during or after annealing, and may help key steps in DNA repair.
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Assessing Protein Dynamics on Low-Complexity Single-Stranded DNA Curtains.

TL;DR: Low-complexity ssDNA curtains are developed and characterize, a high-throughput single-molecule assay to simultaneously monitor protein binding and correlated ssDNA length changes on supported lipid bilayers is developed, and results indicate that RPA-ssDNA interactions are not significantly altered by these modifications.