Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Faezeh Moosavi"'
Autor:
Deyhim Atarod, Fatemeh Mamashli, Atiyeh Ghasemi, Faezeh Moosavi-Movahedi, Mitra Pirhaghi, Hadi Nedaei, Vladimir Muronetz, Thomas Haertlé, Jörg Tatzelt, Gholamhossein Riazi, Ali Akbar Saboury
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-12 (2022)
Abstract α-Synuclein (α-Syn) aggregates are key components of intracellular inclusion bodies characteristic of Parkinson’s disease (PD) and other synucleinopathies. Metal ions have been considered as the important etiological factors in PD since
Externí odkaz:
https://doaj.org/article/41350441dded4e119e8788cf12fedb76
Autor:
Payam Arghavani, Mitra Pirhaghi, Faezeh Moosavi-Movahedi, Fatemeh Mamashli, Elnaz Hosseini, Ali Akbar Moosavi-Movahedi
Publikováno v:
Current Research in Structural Biology, Vol 4, Iss , Pp 356-364 (2022)
Protein oligomerization has two notable aspects: it is crucial for the performing cellular and molecular processes accurately, and it produces amyloid fibril precursors. Although a clear explanation for amyloidosis as a whole is lacking, most studies
Externí odkaz:
https://doaj.org/article/f53eda1730914e8e95cc58bad02be0ba
Publikováno v:
Biotechnology Reports, Vol 34, Iss , Pp e00733- (2022)
In this study, Candida antarctica lipase B (CalB) was covalently immobilized on the surface of graphene oxide (GO) nanoparticles by sortase-mediated immobilization as well as a chemical attachment approach. Sortase is a transpeptidase that provides o
Externí odkaz:
https://doaj.org/article/ed5a4ebc55844bbd8589a0b40e4f9a21
Autor:
Somayyeh Ghareghomi, Faezeh Moosavi-Movahedi, Luciano Saso, Mehran Habibi-Rezaei, Ali Khatibi, Jun Hong, Ali A. Moosavi-Movahedi
Publikováno v:
Antioxidants, Vol 12, Iss 3, p 735 (2023)
Oxidative stresses (OSs) are considered a pivotal factor in creating various pathophysiological conditions. Cells have been able to move forward by modulating numerous signaling pathways to moderate the defects of these stresses during their evolutio
Externí odkaz:
https://doaj.org/article/f86495cbd40644649d25ecde43b9fa0d
Autor:
Mahtab Hafizi, Natalia A Chebotareva, Maryam Ghahramani, Faezeh Moosavi-Movahedi, Seyed Hossein Khaleghinejad, Boris I Kurganov, Ali Akbar Moosavi-Movahedi, Reza Yousefi
Publikováno v:
PLoS ONE, Vol 16, Iss 11, p e0260306 (2021)
αB-crystallin (heat shock protein β5/HSPB5) is a member of the family of small heat shock proteins that is expressed in various organs of the human body including eye lenses and muscles. Therefore, mutations in the gene of this protein (CRYAB) migh
Externí odkaz:
https://doaj.org/article/2a1fa7cc4dec48de81ecdd8034460955
Autor:
Fatemeh Mamashli, Ali Akbar Meratan, Atiyeh Ghasemi, Nahal Obeidi, Bahram Salmani, Deyhim Atarod, Mitra Pirhaghi, Faezeh Moosavi-Movahedi, Mahya Mohammad-Zaheri, Mohammad Bagher Shahsavani, Zahra Habibi-Kelishomi, Bahram Goliaei, Mahdi Gholami, Ali Akbar Saboury
Publikováno v:
ACS Chemical Neuroscience. 14:851-863
Autor:
Mitra, Pirhaghi, Zahra, Najarzadeh, Faezeh, Moosavi-Movahedi, Mahshid, Shafizadeh, Fatemeh, Mamashli, Deyhim, Atarod, Atiyeh, Ghasemi, Dina, Morshedi, Ali Akbar, Meratan, Daniel E, Otzen, Ali Akbar, Saboury
Publikováno v:
Pirhaghi, M, Najarzadeh, Z, Moosavi-Movahedi, F, Shafizadeh, M, Mamashli, F, Atarod, D, Ghasemi, A, Morshedi, D, Meratan, A A, Otzen, D E & Saboury, A A 2023, ' The anti-platelet drug ticlopidine inhibits FapC fibrillation and biofilm production : Highlighting its antibiotic activity ', Biochimica et Biophysica Acta-Proteins and Proteomics, vol. 1871, no. 2, 140883 . https://doi.org/10.1016/j.bbapap.2022.140883
Multidrug resistance of bacteria and persistent infections related to biofilms, as well as the low availability of new antibacterial drugs, make it urgent to develop new antibiotics. Here, we evaluate the antibacterial and anti-biofilm properties of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c783bae4f81abd4bae5ec230b48fbfc
https://pure.au.dk/portal/da/publications/the-antiplatelet-drug-ticlopidine-inhibits-fapc-fibrillation-and-biofilm-production(73eeea64-02c1-4f5a-b527-d61f3565bb38).html
https://pure.au.dk/portal/da/publications/the-antiplatelet-drug-ticlopidine-inhibits-fapc-fibrillation-and-biofilm-production(73eeea64-02c1-4f5a-b527-d61f3565bb38).html
Various metal ions promote formation of α-Synuclein fibrils with different shapes and cytotoxicities
Autor:
Ali Akbar Saboury, Deyhim Atarod, Fatemeh Mamashli, Atiyeh Ghasemi, Faezeh Moosavi-Movahedi, Mitra Pirhaghi, Hadi Nedaei, Gholamhossein Riazi, Vladimir Muronetz, Thomas Haertlé, Jörg Tatzelt
α-Synuclein (α-Syn) aggregates are key components of intracellular inclusion bodies characteristic of Parkinson’s disease (PD) and other synucleinopathies. Metal ions have been considered as the important etiological factors in PD since their int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13ae6553f005f2a04e7eb34cb13390da
https://doi.org/10.21203/rs.3.rs-1401511/v1
https://doi.org/10.21203/rs.3.rs-1401511/v1
Inhibiting mTTR Aggregation/Fibrillation by a Chaperone-like Hydrophobic Amino Acid-Conjugated SPION
Autor:
Payam Arghavani, Alireza Badiei, Seyyed Abolghasem Ghadami, Mehran Habibi-Rezaei, Faezeh Moosavi-Movahedi, Ladan Delphi, Ali Akbar Moosavi-Movahedi
Publikováno v:
The journal of physical chemistry. B. 126(8)
Transthyretin (TTR) aggregation via misfolding of a mutant or wild-type protein leads to systemic or partial amyloidosis (ATTR). Here, we utilized variable biophysical assays to characterize two distinct aggregation pathways for mTTR (a synthesized m
Autor:
Natalia A. Chebotareva, Faezeh Moosavi-Movahedi, Reza Yousefi, Maryam Ghahramani, Ali Akbar Moosavi-Movahedi, Boris I. Kurganov, Seyed Hossein Khaleghinejad, Mahtab Hafizi
Publikováno v:
PLoS ONE
PLoS ONE, Vol 16, Iss 11, p e0260306 (2021)
PLoS ONE, Vol 16, Iss 11, p e0260306 (2021)
αB-crystallin (heat shock protein β5/HSPB5) is a member of the family of small heat shock proteins that is expressed in various organs of the human body including eye lenses and muscles. Therefore, mutations in the gene of this protein (CRYAB) migh