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Mark A. Hancock

Researcher at McGill University

Publications -  46
Citations -  2037

Mark A. Hancock is an academic researcher from McGill University. The author has contributed to research in topics: Receptor & Periplasmic space. The author has an hindex of 22, co-authored 44 publications receiving 1621 citations.

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The Mitochondrial Transcription Factor TFAM Coordinates the Assembly of Multiple DNA Molecules into Nucleoid-like Structures

TL;DR: It is shown that the mitochondrial transcription factor TFAM, an abundant and highly conserved High Mobility Group box protein, binds DNA cooperatively with nanomolar affinity as a homodimer and that it is capable of coordinating and fully compacting several DNA molecules together to form spheroid structures.
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Structural basis for allosteric PARP-1 retention on DNA breaks.

TL;DR: HXMS experiments revealed that a critical allosteric regulatory domain of PARP-1, the helical domain (HD), is affected in distinct ways depending on the particular PARPi engaged in the NAD+-binding site adjacent to the HD.
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Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

TL;DR: The present work is the first study, to the authors' knowledge, to demonstrate a fibronectin-binding activity of a bacterial enolase, and shows that, similar to other bacterial fibronECTin- binding proteins, SsEno may contribute to the virulence of S. suis.
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Allosteric folding correction of F508del and rare CFTR mutants by elexacaftor-tezacaftor-ivacaftor (Trikafta) combination.

TL;DR: In human bronchial epithelial cells, VX-445 synergistically restores F508del-CFTR processing in combination with type I or II correctors that target the nucleotide binding domain 1 (NBD1) membrane spanning domains (MSDs) interface and NBD2, respectively, consistent with a type III corrector mechanism.
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Inhibition of Plasminogen Activation by Lipoprotein(a) CRITICAL DOMAINS IN APOLIPOPROTEIN(a) AND MECHANISM OF INHIBITION ON FIBRIN AND DEGRADED FIBRIN SURFACES

TL;DR: To investigate the inhibition mechanism, the concentrations of plasminogen, cofactor, and a 12-kringle recombinant apo(a) species were systematically varied and it was revealed that additional sequences within kringle IV types 1–4 are required for maximal inhibition.