Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Helen B. Belato"'
Autor:
Helen B. Belato, George P. Lisi
Publikováno v:
Biomolecules, Vol 13, Iss 2, p 264 (2023)
The discovery of protein inhibitors of CRISPR-Cas systems, called anti-CRISPRs (Acrs), has enabled the development of highly controllable and precise CRISPR-Cas tools. Anti-CRISPRs share very little structural or sequential resemblance to each other
Externí odkaz:
https://doaj.org/article/db3a309f2530455ba9df38204a885388
Autor:
Helen B. Belato, Carmelissa Norbrun, Jinping Luo, Chinmai Pindi, Souvik Sinha, Alexandra M. D’Ordine, Gerwald Jogl, Giulia Palermo, George P. Lisi
Publikováno v:
The Journal of Chemical Physics. 157:225103
Allosteric signaling within multidomain proteins is a driver of communication between spatially distant functional sites. Understanding the mechanism of allosteric coupling in large multidomain proteins is the most promising route to achieving spatia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46a8ca0d6dd6cd713963090d83ce935b
https://doi.org/10.1063/5.0128815
https://doi.org/10.1063/5.0128815
Publikováno v:
Biomol NMR Assign
HNH is one of two endonuclease domains of the clustered regularly interspaced short palindromic repeats (CRISPR)-associated protein Cas9 that perform site-specific cleavage of double-stranded DNA. We engineered a novel construct of this critical nucl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc1fa251f28ddba3625f64326363ceff
https://doi.org/10.1007/s12104-019-09907-9
https://doi.org/10.1007/s12104-019-09907-9
Autor:
Helen B. Belato, Alexandra M. D'Ordine, Lukasz Nierzwicki, Pablo R. Arantes, Gerwald Jogl, Giulia Palermo, George P. Lisi
Publikováno v:
J Struct Biol
CRISPR-Cas9 is a widely used biochemical tool with applications in molecular biology and precision medicine. The RNA-guided Cas9 protein uses its HNH endonuclease domain to cleave the DNA strand complementary to its endogenous guide RNA. In this stud
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ed424c9a718b1772631e0d595e28e63
https://doi.org/10.1016/j.jsb.2021.107814
https://doi.org/10.1016/j.jsb.2021.107814
Publikováno v:
Biomolecular NMR Assignments. 12:339-343
Phage L encodes a trimeric 43 kDa decoration protein (Dec) that noncovalently binds and stabilizes the capsids of the homologous phages L and P22 in vitro. At physiological pH Dec was unsuitable for NMR. We were able to obtain samples amenable for NM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e091a21370b2910713654a21c54fffdc
https://doi.org/10.1007/s12104-018-9836-1
https://doi.org/10.1007/s12104-018-9836-1
Autor:
Kyle W. East, Brandon P. Mitchell, George P. Lisi, Rohaine V. Hsu, Jennifer Y. Cui, Erin Skeens, Giulia Palermo, Helen B. Belato, Victor S. Batista
Publikováno v:
Biophysical reviews, vol 12, iss 1
Allostery is a ubiquitous biological mechanism in which a distant binding site is coupled to and drastically alters the function of a catalytic site in a protein. Allostery provides a high level of spatial and temporal control of the integrity and ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0093e129a6d64f4984a78171729ebb9
https://pubmed.ncbi.nlm.nih.gov/31838649
https://pubmed.ncbi.nlm.nih.gov/31838649