Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Manuel F. Rosario-Alomar"'
Autor:
Tatiana Quiñones-Ruiz, Manuel F. Rosario-Alomar, Maruda Shanmugasundaram, Muhammad M. Ali, Igor K. Lednev
Publikováno v:
Biochemistry. 61(14)
Here, we report a new phenomenon in which lysozyme fibrils formed in a solution of acetic acid spontaneously refold to a different polymorph through a disassembled intermediate upon the removal of acetic acid. The structural changes were revealed and
Autor:
Maruda Shanmugasundaram, Tatiana Quiñones-Ruiz, Vladimir M. Grigoryants, Karina Ruiz-Esteves, Juan López-Garriga, Igor K. Lednev, Manuel F. Rosario-Alomar, Charles P. Scholes
Publikováno v:
Journal of the American Chemical Society. 139:9755-9758
A purple color is formed during the fibrillation of lysozyme, a well-studied protein lacking a prosthetic group. The application of Raman spectroscopy, electron paramagnetic resonance and UV-vis absorption spectroscopy indicates the formation of a su
Autor:
Dmitry Kurouski, Igor K. Lednev, Samuel P. Hernández-Rivera, Manuel F. Rosario-Alomar, Tatiana Quiñones-Ruiz, Lorraine De Jesús-Kim, Valentin Sereda, Dmitri V. Zagorevski, Leishla M. Cruz-Collazo, Eduardo DeBarros-Ferreira, Juan López-Garriga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d98a86de355956cd74ef63a21375c04
https://doi.org/10.5772/intechopen.86221
https://doi.org/10.5772/intechopen.86221
Autor:
Tatiana Quiñones Ruiz, Juan López Garriga, Manuel F. Rosario Alomar, Igor K. Lednev, Indra Gonzalez Ojeda
Publikováno v:
The FASEB Journal. 33
Publikováno v:
The FASEB Journal. 33
Autor:
Tatiana Quiñones-Ruiz, Frank T. Robb, Manuel F. Rosario-Alomar, Igor K. Lednev, Alberto J.L. Macario, Everly Conway de Macario, Donatella Bulone, Pier Luigi San Biagio
Publikováno v:
Methods in Molecular Biology ISBN: 9781493988198
pp. 69–92. London: Springer, 2019
info:cnr-pdr/source/autori:Bulone D.; San Biagio P.L.; Quinones-Ruiz T.; Rosario-Alomar M.; Lednev I.K.; Robb F.T.; Conway de Macario E.; Macario A.J.L./titolo:A multipronged method for unveiling subtle structural-functional defects of mutant chaperone molecules causing human chaperonopathies/titolo_volume:/curatori_volume:/editore: /anno:2019
pp. 69–92. London: Springer, 2019
info:cnr-pdr/source/autori:Bulone D.; San Biagio P.L.; Quinones-Ruiz T.; Rosario-Alomar M.; Lednev I.K.; Robb F.T.; Conway de Macario E.; Macario A.J.L./titolo:A multipronged method for unveiling subtle structural-functional defects of mutant chaperone molecules causing human chaperonopathies/titolo_volume:/curatori_volume:/editore: /anno:2019
Chaperonopathies are diseases in which abnormal chaperones play an etiopathogenic role. A chaperone is mutated or otherwise abnormal (e.g., modified by an aberrant posttranslational modification) in structure/ function. To understand the pathogenic m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b38123fc6260644f7f41210d1158f453
https://doi.org/10.1007/978-1-4939-8820-4_5
https://doi.org/10.1007/978-1-4939-8820-4_5
Autor:
Alani Aldarondo‐Torres, Daniel Andres Colon‐Rios, Manuel F. Rosario-Alomar, Juan López-Garriga
Publikováno v:
The FASEB Journal. 32
Autor:
Dmitri V. Zagorevski, Manuel F. Rosario-Alomar, Igor K. Lednev, Lorraine De Jesús-Kim, Eduardo B. Ferreira, Tatiana Quiñones-Ruiz, Valentin Sereda, Dmitry Kurouski, Samuel P. Hernández-Rivera, Juan López-Garriga
Publikováno v:
The Journal of Physical Chemistry. B
Amyloid fibrils are large aggregates of misfolded proteins, which are often associated with various neurodegenerative diseases such as Alzheimer's, Parkinson's, Huntington's, and vascular dementia. The amount of hydrogen sulfide (H2S) is known to be