Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Jessica Valle-Orero"'
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-9 (2021)
Rieu et al. present a magnetic tweezers based single-molecule manipulation method, called kinetic locking, for direct detection of biomolecular binding without use of fluorescent probes. By measuring dynamical interactions of E. coli RecQ helicase wi
Externí odkaz:
https://doaj.org/article/53d9b151442c49a496d43795d732b58f
Autor:
Shubhasis Haldar, Rafael Tapia-Rojo, Edward C. Eckels, Jessica Valle-Orero, Julio M. Fernandez
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-7 (2017)
Proteins fold under mechanical force during co-translational folding at the ribosome. Here, the authors use single molecule magnetic tweezers to study the influence of chaperones on protein folding and show that the ribosomal chaperone trigger factor
Externí odkaz:
https://doaj.org/article/c435eaed6d044a0d845d5ba987b97fa9
Autor:
Jessica Valle-Orero, Martin Rieu, Phong Lan Thao Tran, Alexandra Joubert, Saurabh Raj, Jean-François Allemand, Vincent Croquette, Jean-Baptiste Boulé
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, 2022, ⟨10.1093/nar/gkac667⟩
Nucleic Acids Research, 2022, ⟨10.1093/nar/gkac667⟩
G-rich sequences found at multiple sites throughout all genomes may form secondary structures called G-quadruplexes (G4), which act as roadblocks for molecular motors. Among the enzymes thought to process these structures, the Pif1 DNA helicase is co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd0f5df2f230b6bd16b867d639412cb6
https://hal.science/hal-03576966v2/file/gkac667.pdf
https://hal.science/hal-03576966v2/file/gkac667.pdf
Publikováno v:
Communications Biology
Communications Biology, 2021, 4, pp.1083. ⟨10.1038/s42003-021-02606-z⟩
Communications Biology, Nature Publishing Group, 2021, 4, pp.1083. ⟨10.1038/s42003-021-02606-z⟩
Communications Biology, Vol 4, Iss 1, Pp 1-9 (2021)
Communications Biology, 2021, 4, pp.1083. ⟨10.1038/s42003-021-02606-z⟩
Communications Biology, Nature Publishing Group, 2021, 4, pp.1083. ⟨10.1038/s42003-021-02606-z⟩
Communications Biology, Vol 4, Iss 1, Pp 1-9 (2021)
Fluorescence-free micro-manipulation of nucleic acids (NA) allows the functional characterization of DNA/RNA processing proteins, without the interference of labels, but currently fails to detect and quantify their binding. To overcome this limitatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e3b99af130472f5e5246c18ba10fec8
https://hal.sorbonne-universite.fr/hal-03355277
https://hal.sorbonne-universite.fr/hal-03355277
Fluorescence-free micro-manipulation of nucleic acids (NA) allows the functional characterization of DNA/RNA processing proteins, without the interference of labels, but currently fails to detect and quantify their binding. To overcome this limitatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::35dd0a6e1991315cb0a279ff09054729
https://doi.org/10.1101/2020.09.30.321232
https://doi.org/10.1101/2020.09.30.321232
Autor:
Vicente I. Fernandez, Jessica Valle-Orero, Guillaume Stirnemann, Julio M. Fernandez, Ronen Berkovich
Publikováno v:
The Journal of Physical Chemistry Letters. 9:4707-4713
Single-molecule force spectroscopy utilizes polyproteins, which are composed of tandem modular domains, to study their mechanical and structural properties. Under the application of external load, the polyproteins respond by unfolding and refolding d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28d12a018609289b3c83215d6f769523
https://doi.org/10.1021/acs.jpclett.8b01925
https://doi.org/10.1021/acs.jpclett.8b01925
Autor:
Jessica Valle-Orero, Julio M. Fernandez, Rafael Tapia-Rojo, Edward C. Eckels, Shubhasis Haldar
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-7 (2017)
Nature Communications
Nature Communications
Proteins fold under mechanical forces in a number of biological processes, ranging from muscle contraction to co-translational folding. As force hinders the folding transition, chaperones must play a role in this scenario, although their influence on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0bd27e34f04b413ebea211e47869b173
https://doaj.org/article/c435eaed6d044a0d845d5ba987b97fa9
https://doaj.org/article/c435eaed6d044a0d845d5ba987b97fa9
Autor:
Jessica Valle‐Orero, Jaime Andrés Rivas‐Pardo, Rafael Tapia‐Rojo, Ionel Popa, Daniel J. Echelman, Shubhasis Haldar, Julio M. Fernández
Publikováno v:
Angewandte Chemie. 129:9873-9878
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0befee21a18d673c9ed34f46e247944e
https://doi.org/10.1002/ange.201703630
https://doi.org/10.1002/ange.201703630
Autor:
N. Kyle Tanner, Jessica Valle Orero, Josette Banroques, Vincent Croquette, Debjani Bagchi, Saurabh Raj
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2019, 47 (7), pp.3699-3710. ⟨10.1093/nar/gkz057⟩
Nucleic Acids Research, Oxford University Press, 2019, 47 (7), pp.3699-3710. ⟨10.1093/nar/gkz057⟩
DEAD-box helicases are involved in all steps of RNA metabolism. They are ATP-dependent RNA binding proteins and RNA-dependent ATPases. They can displace short duplexes, but they lack processivity. Their mechanism and functioning are not clearly under
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fad8cec19c150ae5ac9b19de973d552
https://hal.archives-ouvertes.fr/hal-03059646
https://hal.archives-ouvertes.fr/hal-03059646
Autor:
Ionel Popa, Julio M. Fernandez, Jessica Valle-Orero, Rafael Tapia-Rojo, Jaime Andrés Rivas-Pardo, Edward C. Eckels
Publikováno v:
The journal of physical chemistry letters. 8(15)
Protein ageing may manifest as a mechanical disease that compromises tissue elasticity. As proved recently, while proteins respond to changes in force with an instantaneous elastic recoil followed by a folding contraction, aged proteins break bad, be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34d96a96f2d97dc62463e28fcb936ad3
https://pubmed.ncbi.nlm.nih.gov/28723106
https://pubmed.ncbi.nlm.nih.gov/28723106