Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Mohsin M, Naqvi"'
Autor:
Julien Marcoux, P Patrizia Mangione, Riccardo Porcari, Matteo T Degiacomi, Guglielmo Verona, Graham W Taylor, Sofia Giorgetti, Sara Raimondi, Sarah Sanglier‐Cianférani, Justin LP Benesch, Ciro Cecconi, Mohsin M Naqvi, Julian D Gillmore, Philip N Hawkins, Monica Stoppini, Carol V Robinson, Mark B Pepys, Vittorio Bellotti
Publikováno v:
EMBO Molecular Medicine, Vol 7, Iss 10, Pp 1337-1349 (2015)
Abstract The mechanisms underlying transthyretin‐related amyloidosis in vivo remain unclear. The abundance of the 49–127 transthyretin fragment in ex vivo deposits suggests that a proteolytic cleavage has a crucial role in destabilizing the tetra
Externí odkaz:
https://doaj.org/article/73bd04162dae41c1a8592516fd43e2e6
Autor:
Elham Babaei, Ghazal Hajisalem, Shohei Iwamoto, Burak Kaynak, Pemra Doruker, Mohsin M. Naqvi, Janet Kumita, Feng-Yu Wang, Jhih-Hong Cheng, Che-Min Wu, Shang-Hua Yang, Ivet Bahar, Laura Itzhaki, Reuven Gordon
Publikováno v:
2021 IEEE 16th Nanotechnology Materials and Devices Conference (NMDC).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3dd2efa888f35f6e3b59ca71e2185303
https://doi.org/10.1109/nmdc50713.2021.9677469
https://doi.org/10.1109/nmdc50713.2021.9677469
Publikováno v:
Nature chemical biology. 18(9)
Clustered regularly interspaced short palindromic repeats (CRISPR)-Cas12a is widely used for genome editing and diagnostics, so it is important to understand how RNA-guided DNA recognition activates the cleavage of the target strand (TS) following no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6c9732d616ff08bce2ebcb46fce135a3
https://pubmed.ncbi.nlm.nih.gov/35836018
https://pubmed.ncbi.nlm.nih.gov/35836018
CRISPR-Cas12a has been widely used for genome editing and diagnostic applications, yet it is not fully understood how RNA-guided DNA recognition activates the sequential cleavage of the non-target strand (NTS) followed by the target strand (TS). Here
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5faf43ff4ca326a40cdc88066b8a2a45
https://doi.org/10.1101/2021.06.18.448962
https://doi.org/10.1101/2021.06.18.448962
Autor:
Vanda Sunderlikova, Andrew Roth, Sander J. Tans, Mario J. Avellaneda, Mohsin M. Naqvi, Eline J. Koers, Hays S. Rye, Guenter Kramer
Unfolded proteins ubiquitously collapse into a compact yet dynamic state1,2. While this compaction is pivotal to protein folding3, aggregation4,5, intrinsic disorder6, and phase separation7, its role in protein quality control mechanisms remains obsc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::674ac0bbcf09312e36124ce52c42896c
https://doi.org/10.1101/2020.06.17.157057
https://doi.org/10.1101/2020.06.17.157057
Autor:
Grace E L Mullally, Kara van Aelst, Fiona M. Diffin, Virginijus Siksnys, Mohsin M. Naqvi, Mark D. Szczelkun, Tautvydas Karvelis, Giedrius Gasiunas
Publikováno v:
Nucleic acids research, Oxford : Oxford University Press, 2020, vol. 48, iss. 12, p. 6811-6823
Mullally, G E L, Van Aelst, K, Mubarak Naqvi, M, Diffin, F M, Karvelis, T, Gasiunas, G, Siksnys, V & Szczelkun, M D 2020, ' 5′ modifications to CRISPR Cas9 gRNA can change the dynamics and size of R-loops and inhibit DNA cleavage ', Nucleic Acids Research . https://doi.org/10.1093/nar/gkaa477
Nucleic Acids Research
Mullally, G E L, Van Aelst, K, Mubarak Naqvi, M, Diffin, F M, Karvelis, T, Gasiunas, G, Siksnys, V & Szczelkun, M D 2020, ' 5′ modifications to CRISPR Cas9 gRNA can change the dynamics and size of R-loops and inhibit DNA cleavage ', Nucleic Acids Research . https://doi.org/10.1093/nar/gkaa477
Nucleic Acids Research
A key aim in exploiting CRISPR–Cas is gRNA engineering to introduce additional functionalities, ranging from individual nucleotide changes that increase efficiency of on-target binding to the inclusion of larger functional RNA aptamers or ribonucle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c3714a1d69aef21584daee7a78cc1e4
https://repository.vu.lt/VU:ELABAPDB62158247&prefLang=en_US
https://repository.vu.lt/VU:ELABAPDB62158247&prefLang=en_US
Publikováno v:
Protein Science. 26:1291-1302
Protein folding is well known to be supervised by a dedicated class of proteins called chaperones. However, the core mode of action of these molecular machines has remained elusive due to several reasons including the promiscuous nature of the intera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a07e6414d405a23227e0ca4255f69551
https://doi.org/10.1002/pro.3161
https://doi.org/10.1002/pro.3161
Autor:
Sergey Bezrukavnikov, Kingshuk Ghosh, Fatemeh Moayed, Bastian Groitl, Sander J. Tans, Claudia M. Cremers, Guenter Kramer, Ursula Jakob, Mohsin M. Naqvi
Publikováno v:
Biophys J
Holdase chaperones are known to be central to suppressing aggregation, but how they affect substrate conformations remains poorly understood. Here, we use optical tweezers to study how the holdase Hsp33 alters folding transitions within single maltos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2ff46a8c5cc3b5a0f18669e81396491
https://pubmed.ncbi.nlm.nih.gov/31757359
https://pubmed.ncbi.nlm.nih.gov/31757359
Autor:
Sofia Giorgetti, Julien Marcoux, Palma Mangione, Ciro Cecconi, Graham W. Taylor, Monica Stoppini, Justin L. P. Benesch, Riccardo Porcari, Mohsin M. Naqvi, Guglielmo Verona, Philip N. Hawkins, Carol V. Robinson, Sarah Sanglier-Cianférani, Mark B. Pepys, Matteo T. Degiacomi, Sara Raimondi, Vittorio Bellotti, Julian D. Gillmore
Publikováno v:
EMBO Molecular Medicine
EMBO molecular medicine, 2015, Vol.7(10), pp.1337-1349 [Peer Reviewed Journal]
EMBO Molecular Medicine, Wiley Open Access, 2015, 7 (10), pp.1337-1349. ⟨10.15252/emmm.201505357⟩
EMBO molecular medicine (Online) 7 (2015): 1337–1349. doi:10.15252/emmm.201505357
info:cnr-pdr/source/autori:Marcoux, Julien[ 1,2 ] ; Mangione, P. Patrizia[ 3,4 ] ; Porcari, Riccardo[ 3 ] ; Degiacomi, Matteo T.[ 1 ] ; Verona, Guglielmo)ù[ 3,4 ] ; Taylor, Graham W.[ 3 ] ; Giorgetti, Sofia[ 4 ] ; Raimondi, Sara[ 4 ] ; Sanglier-Cianferani, Sarah[ 2 ] ; Benesch, Justin L. P.[ 1 ] ; Cecconi, Ciro[ 5,6 ] ; Naqvi, Mohsin M.[ 6 ] ; Gillmore, Julian D.[ 3 ] ; Hawkins, Philip N.[ 3 ] ; Stoppini, Monica[ 4 ] ; Robinson, Carol V.[ 1 ] ; Pepys, Mark B.[ 3 ] ; Bellotti, Vittorio[ 3,4 ]/titolo:A novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis/doi:10.15252%2Femmm.201505357/rivista:EMBO molecular medicine (Online)/anno:2015/pagina_da:1337/pagina_a:1349/intervallo_pagine:1337–1349/volume:7
EMBO molecular medicine, 2015, Vol.7(10), pp.1337-1349 [Peer Reviewed Journal]
EMBO Molecular Medicine, Wiley Open Access, 2015, 7 (10), pp.1337-1349. ⟨10.15252/emmm.201505357⟩
EMBO molecular medicine (Online) 7 (2015): 1337–1349. doi:10.15252/emmm.201505357
info:cnr-pdr/source/autori:Marcoux, Julien[ 1,2 ] ; Mangione, P. Patrizia[ 3,4 ] ; Porcari, Riccardo[ 3 ] ; Degiacomi, Matteo T.[ 1 ] ; Verona, Guglielmo)ù[ 3,4 ] ; Taylor, Graham W.[ 3 ] ; Giorgetti, Sofia[ 4 ] ; Raimondi, Sara[ 4 ] ; Sanglier-Cianferani, Sarah[ 2 ] ; Benesch, Justin L. P.[ 1 ] ; Cecconi, Ciro[ 5,6 ] ; Naqvi, Mohsin M.[ 6 ] ; Gillmore, Julian D.[ 3 ] ; Hawkins, Philip N.[ 3 ] ; Stoppini, Monica[ 4 ] ; Robinson, Carol V.[ 1 ] ; Pepys, Mark B.[ 3 ] ; Bellotti, Vittorio[ 3,4 ]/titolo:A novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis/doi:10.15252%2Femmm.201505357/rivista:EMBO molecular medicine (Online)/anno:2015/pagina_da:1337/pagina_a:1349/intervallo_pagine:1337–1349/volume:7
International audience; The mechanisms underlying transthyretin-related amyloidosis in vivo remain unclear. The abundance of the 49-127 transthyretin fragment in ex vivo deposits suggests that a proteolytic cleavage has a crucial role in destabilizin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5dda55b6a8c3e36783aa9813490d1102
http://europepmc.org/articles/PMC4604687
http://europepmc.org/articles/PMC4604687
Autor:
Ciro Cecconi, Mohsin M. Naqvi, Alessandro Mossa, Birthe B. Kragelund, Mariela R. Otazo, Pétur O. Heidarsson
Publikováno v:
Biophysical journal
info:cnr-pdr/source/autori:Naqvi, Mohsin M.[ 1,3 ] ; Heidarsson, Petur O.[ 2 ] ; Otazo, Mariela R.[ 3,4 ] ; Mossa, Alessandro[ 5,6 ] ; Kragelund, Birthe B.[ 2 ] ; Cecconi, Ciro[ 1,3 ]/titolo:Single-Molecule Folding Mechanisms of the apo-and Mg2+-Bound States of Human Neuronal Calcium Sensor-1/doi:10.1016%2Fj.bpj.2015.05.028/rivista:Biophysical journal (Print)/anno:2015/pagina_da:113/pagina_a:123/intervallo_pagine:113–123/volume:109
info:cnr-pdr/source/autori:Naqvi, Mohsin M.[ 1,3 ] ; Heidarsson, Petur O.[ 2 ] ; Otazo, Mariela R.[ 3,4 ] ; Mossa, Alessandro[ 5,6 ] ; Kragelund, Birthe B.[ 2 ] ; Cecconi, Ciro[ 1,3 ]/titolo:Single-Molecule Folding Mechanisms of the apo-and Mg2+-Bound States of Human Neuronal Calcium Sensor-1/doi:10.1016%2Fj.bpj.2015.05.028/rivista:Biophysical journal (Print)/anno:2015/pagina_da:113/pagina_a:123/intervallo_pagine:113–123/volume:109
Neuronal calcium sensor-1 (NCS-1) is the primordial member of a family of proteins responsible primarily for sensing changes in neuronal Ca(2+) concentration. NCS-1 is a multispecific protein interacting with a number of binding partners in both calc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c935d2573bf2534e164ddf011996dafa