Zobrazeno 1 - 10
of 91
pro vyhledávání: '"Gaetano Irace"'
Publikováno v:
AIMS Biophysics, Vol 5, Iss 2, Pp 155-165 (2018)
Proteins and polypeptides containing a high proportion of β-sheets have been recently reported to exhibit, in their amyloid aggregated states, an intrinsic fluorescence in the blue-green range of wavelength where the aromatic residues do not emit. L
Externí odkaz:
https://doaj.org/article/54fd00dc5d2344e6bb32a35bf95e256d
Publikováno v:
Molecules, Vol 20, Iss 2, Pp 2510-2528 (2015)
Amyloidosis is a protein folding disorder in which normally soluble proteins are deposited extracellularly as insoluble fibrils, impairing tissue structure and function. Charged polyelectrolytes such as glycosaminoglycans (GAGs) are frequently found
Externí odkaz:
https://doaj.org/article/8fe42d91bca5422a8e7c111ef264302c
Publikováno v:
Frontiers in Molecular Biosciences, Vol 3 (2016)
Superoxide dismutase 1 (SOD1) has been implicated with familial amyotrophic lateral sclerosis (fALS) through accumulation of protein amyloid aggregates in motor neurons of patients. Amyloid aggregates and protein inclusions are a common pathological
Externí odkaz:
https://doaj.org/article/af4ee8032fa6493db335546a0171a2ab
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e80768 (2013)
Neurodegenerative diseases are associated with misfolding and deposition of specific proteins, either intra or extracellularly in the nervous system. Advanced glycation end products (AGEs) originate from different molecular species that become glycat
Externí odkaz:
https://doaj.org/article/7498b2863ba84f41b4bc584f61e3d859
Autor:
Silvia Vilasi, Rosalba Sarcina, Rosa Maritato, Antonella De Simone, Gaetano Irace, Ivana Sirangelo
Publikováno v:
PLoS ONE, Vol 6, Iss 7, p e22076 (2011)
Glycosaminoglycans (GAGs) are frequently associated with amyloid deposits in most amyloid diseases, and there is evidence to support their active role in amyloid fibril formation. The purpose of this study was to obtain structural insight into GAG-pr
Externí odkaz:
https://doaj.org/article/40c081ecf90a4a3bb659f73fbd2c7a52
Autor:
Lucia Altucci, Margherita Borriello, Roberto Vinciguerra, Ivana Sirangelo, Clara Iannuzzi, Vincenzo Carafa, Gaetano Irace
Publikováno v:
Journal of Cellular Physiology. 230:2807-2820
Protein glycation is a non-enzymatic, irreversible modification of protein amino groups by reactive carbonyl species leading to the formation of advanced glycation end products (AGEs). Several proteins implicated in neurodegenerative diseases have be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fed7cf6bd2a7eb9437006b205f7032e5
https://doi.org/10.1002/jcp.25011
https://doi.org/10.1002/jcp.25011
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences; Volume 18; Issue 12; Pages: 2551
International Journal of Molecular Sciences, Vol 18, Iss 12, p 2551 (2017)
International Journal of Molecular Sciences; Volume 18; Issue 12; Pages: 2551
International Journal of Molecular Sciences, Vol 18, Iss 12, p 2551 (2017)
Human insulin is a widely used model protein for the study of amyloid formation as both associated to insulin injection amyloidosis in type II diabetes and highly prone to form amyloid fibrils in vitro. In this study, we aim to gain new structural in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab06ffea121aadc395840c0dc01bf04c
http://europepmc.org/articles/PMC5751154
http://europepmc.org/articles/PMC5751154
Autor:
Antimo Di Maro, Ivana Sirangelo, Gaetano Irace, Margherita Borriello, Clara Iannuzzi, Marcella Cammarota
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
Curcumin is known for its anti-inflammatory, antioxidant and anticancer activity, as well as for its ability to interfere with amyloid aggregation and non-enzymatic glycation reaction, that makes it an attractive potential drug. However, curcumin the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0edb68509cf5180e587fe3454fed86c
https://pubmed.ncbi.nlm.nih.gov/29118444
https://pubmed.ncbi.nlm.nih.gov/29118444
Autor:
Nunzia D'Onofrio, Ivana Sirangelo, Alfonso Giovane, Gaetano Irace, Rosa Maritato, Maria Luisa Balestrieri, Clara Iannuzzi, Antonio Giordano
Publikováno v:
Journal of Cellular Biochemistry. 115:2116-2122
W7FW14F apomyoglobin (W7FW14F ApoMb) amyloid aggregates induce cytotoxicity in SH-SY5Y human neuroblastoma cells through a mechanism not fully elucidated. Amyloid neurotoxicity process involves calcium dyshomeostasis and reactive oxygen species (ROS)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c4bf249b9c9fc45f9c89129329e210cf
https://doi.org/10.1002/jcb.24888
https://doi.org/10.1002/jcb.24888
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 14, Iss 7, Pp 14287-14300 (2013)
International Journal of Molecular Sciences, Vol 14, Iss 7, Pp 14287-14300 (2013)
Apomyoglobin is an excellent example of a monomeric all α-helical globular protein whose folding pathway has been extensively studied and well characterized. Structural perturbation induced by denaturants or high temperature as well as amino acid su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::894bae0ce75c6234d24d936ef41f1ae2
https://doi.org/10.3390/ijms140714287
https://doi.org/10.3390/ijms140714287