Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Marina Rubini"'
Autor:
Marina Rubini
Publikováno v:
ACS Central Science, Vol 10, Iss 10, Pp 1813-1814 (2024)
Externí odkaz:
https://doaj.org/article/4d2eba91342a45598b1c5bc92aafa004
Autor:
Mario Mardirossian, Marina Rubini, Mauro F. A. Adamo, Marco Scocchi, Michele Saviano, Alessandro Tossi, Renato Gennaro, Andrea Caporale
Publikováno v:
Molecules, Vol 26, Iss 23, p 7401 (2021)
The 3D structure and surface characteristics of proteins and peptides are crucial for interactions with receptors or ligands and can be modified to some extent to modulate their biological roles and pharmacological activities. The introduction of hal
Externí odkaz:
https://doaj.org/article/dd85456c1f53459c90ce063c6e773a2e
Autor:
Maria D Crespo, Marina Rubini
Publikováno v:
PLoS ONE, Vol 6, Iss 5, p e19425 (2011)
BACKGROUND: Many strategies have been employed to increase the conformational stability of proteins. The use of 4-substituted proline analogs capable to induce pre-organization in target proteins is an attractive tool to deliver an additional conform
Externí odkaz:
https://doaj.org/article/a9549ae932c74671be253267bf638566
Publikováno v:
Organic & Biomolecular Chemistry. 20:6324-6328
A robust and highly diastereoselective route for the synthesis of (2S,4S)-methylproline was developed to facilitate peptide/protein engineering and design.
Publikováno v:
ChemBioChem, 22 (23)
C⁴-substituted fluoroprolines (4R)-fluoroproline ((4R)-Flp) and (4S)-fluoroproline ((4S)-Flp) have been used in protein engineering to enhance the thermodynamic stability of peptides and proteins. The electron-withdrawing effect of fluorine can bia
Autor:
Visakh V. S. Pillai, Pallavi Kumari, Srikanth Kolagatla, Victoria Garcia Sakai, Svemir Rudić, Brian J. Rodriguez, Marina Rubini, Katarzyna M. Tych, Antonio Benedetto
Publikováno v:
The Journal of Physical Chemistry Letters, 13, 7058-7064. AMER CHEMICAL SOC
Proteins aggregation into amyloid fibrils has been observed in several pathological conditions and exploited in nanotechnology. It is also key in several biochemical processes. In this work we show that ionic liquids (ILs) – a vast class of organic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de87489125df4f3469c8b46742f64464
https://eprints.whiterose.ac.uk/189679/1/acs.jpclett.2c01505.pdf
https://eprints.whiterose.ac.uk/189679/1/acs.jpclett.2c01505.pdf
Autor:
Visakh Pillai, Pallavi Kumari, Srikanth Kolagatla, Victoria Garcia Sakai, Svemir Rudić, Brian Rodriguez, Marina Rubini, Katarzyna Tych, Antonio Benedetto
Amyloidogenesis is the process by which proteins form aggregated structures known as amyloid fibrils. They play a key role in a variety of biological processes in healthy organisms, are a characteristic signature of several pathological conditions, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b04c551e92109fdd64b11b5b6953d39
https://doi.org/10.26434/chemrxiv-2022-cl7bh
https://doi.org/10.26434/chemrxiv-2022-cl7bh
Autor:
Philipp R. Spycher, Susanna M. Früh, Ingmar Schoen, Ralf Jungmann, Sebastian Lickert, Viola Vogel, Ulf Matti, Marina Rubini, Jonas Ries, Thomas Schlichthaerle
Publikováno v:
ACS Nano, 15 (7)
The precise spatial localization of proteins in situ by super-resolution microscopy (SRM) demands their targeted labeling. Positioning reporter molecules as close as possible to the target remains a challenge in primary cells or tissues from patients
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53b0d6632614e3e1b41c5aef8a843012
https://hdl.handle.net/20.500.11850/492108
https://hdl.handle.net/20.500.11850/492108
Autor:
Susanna M, Früh, Ulf, Matti, Philipp R, Spycher, Marina, Rubini, Sebastian, Lickert, Thomas, Schlichthaerle, Ralf, Jungmann, Viola, Vogel, Jonas, Ries, Ingmar, Schoen
Publikováno v:
ACS Nano
The precise spatial localization of proteins in situ by super-resolution microscopy (SRM) demands their targeted labeling. Positioning reporter molecules as close as possible to the target remains a challenge in primary cells or tissues from patients
Publikováno v:
The Journal of Biological Chemistry
Journal of Biological Chemistry, 294 (38)
Journal of Biological Chemistry, 294 (38)
Thioredoxin (Trx) is a conserved, cytosolic reductase in all known organisms. The enzyme receives two electrons from NADPH via thioredoxin reductase (TrxR) and passes them on to multiple cellular reductases via disulfide exchange. Despite the ubiquit