Articles with "protease domain" as a keyword



Photo from wikipedia

Structure-based drug repositioning over the human TMPRSS2 protease domain: search for chemical probes able to repress SARS-CoV-2 Spike protein cleavages

Sign Up to like & get
recommendations!
Published in 2020 at "European Journal of Pharmaceutical Sciences"

DOI: 10.1016/j.ejps.2020.105495

Abstract: Abstract In December 2019, a new coronavirus was identified in the Hubei province of central china and named SARS-CoV-2. This new virus induces COVID-19, a severe respiratory disease with high death rate. A putative target… read more here.

Keywords: protease; tmprss2; structure; sars cov ... See more keywords
Photo by daniele_franchi from unsplash

ATPase and Protease Domain Movements in the Bacterial AAA+ Protease FtsH Are Driven by Thermal Fluctuations.

Sign Up to like & get
recommendations!
Published in 2018 at "Journal of molecular biology"

DOI: 10.1016/j.jmb.2018.07.023

Abstract: AAA+ proteases are essential players in cellular pathways of protein degradation. Elucidating their conformational behavior is key for understanding their reaction mechanism and, importantly, for elaborating our understanding of mutation-induced protease deficiencies. Here, we study… read more here.

Keywords: protease; atpase protease; domain movements; movements bacterial ... See more keywords
Photo by thavis_3d from unsplash

Mutations within the putative protease domain of the human FAM111B gene may predict disease severity and poor prognosis: A review of POIKTMP cases

Sign Up to like & get
recommendations!
Published in 2022 at "Experimental Dermatology"

DOI: 10.1111/exd.14537

Abstract: Mutations in the human FAM111B gene are associated with a rare, hereditary multi‐systemic fibrosing disease, POIKTMP. To date, there are ten POIKTMP‐associated FAM111B gene mutations reported in thirty‐six patients from five families globally. To investigate… read more here.

Keywords: mutations within; poiktmp; fam111b gene; protease domain ... See more keywords
Photo from wikipedia

Conformational Plasticity-Rigidity Axis of the Coagulation Factor VII Zymogen Elucidated by Atomistic Simulations of the N-Terminally Truncated Factor VIIa Protease Domain

Sign Up to like & get
recommendations!
Published in 2021 at "Biomolecules"

DOI: 10.3390/biom11040549

Abstract: The vast majority of coagulation factor VII (FVII), a trypsin-like protease, circulates as the inactive zymogen. Activated FVII (FVIIa) is formed upon proteolytic activation of FVII, where it remains in a zymogen-like state and it… read more here.

Keywords: protease; coagulation factor; factor; plasticity ... See more keywords