M
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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Journal ArticleDOI
The Mitochondrial Transcription Factor TFAM Coordinates the Assembly of Multiple DNA Molecules into Nucleoid-like Structures
Brett A. Kaufman,Nela Durisic,Jeffrey M. Mativetsky,Santiago Costantino,Mark A. Hancock,Peter Grutter,Eric A. Shoubridge,Eric A. Shoubridge +7 more
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.
Levani Zandarashvili,Marie-France Langelier,Uday Kiran Velagapudi,Mark A. Hancock,Jamin D. Steffen,Ramya Billur,Zain M. Hannan,Andrew J. Wicks,Dragomir B. Krastev,Stephen J. Pettitt,Christopher J. Lord,Tanaji T. Talele,John M. Pascal,Ben E. Black +13 more
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.
Guido Veit,Ariel Roldan,Mark A. Hancock,Dillon F. Da Fonte,Haijin Xu,Maytham Hussein,Saul Frenkiel,Elias Matouk,Tony Velkov,Gergely L. Lukacs +9 more
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
Mark A. Hancock,Michael B. Boffa,Santica M. Marcovina,Michael E. Nesheim,Marlys L. Koschinsky +4 more
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.