Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Guru KrishnaKumar Viswanathan"'
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 7 (2019)
A current challenge faced by researchers is the lack of disease-modifying therapeutics for amyloid formation that is associated with several human diseases. Although the monomeric proteins or peptides involved in various amyloidogenic diseases do not
Externí odkaz:
https://doaj.org/article/2f4144b318db4b478a875038e9128a84
Autor:
Guru KrishnaKumar Viswanathan, Satabdee Mohapatra, Ashim Paul, Elad Arad, Raz Jelinek, Ehud Gazit, Daniel Segal
Publikováno v:
Molecules, Vol 23, Iss 12, p 3279 (2018)
PAP248⁻286, a 39 amino acid peptide fragment, derived from the prostatic acid phosphatase secreted in human semen, forms amyloid fibrils and facilitates the attachment of retroviruses to host cells that results in the enhancement of viral infection
Externí odkaz:
https://doaj.org/article/8e786a2bcf174a50839dd720eaceeb04
Publikováno v:
ChemMedChem. 16:3565-3568
The von Hippel-Lindau tumor suppressor protein (pVHL) is involved in maintaining cellular oxygen homeostasis through the regulated degradation of HIF-α. The intrinsically disordered nature of pVHL makes it prone to aggregation that impairs its funct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2972b27afa690fbe0e4a99e3b4c95a6
https://doi.org/10.1002/cmdc.202100441
https://doi.org/10.1002/cmdc.202100441
Autor:
Guru KrishnaKumar Viswanathan, Ashim Paul, Ehud Gazit, Daniel L. Segal, Esraa Haj, Malak Abu-Hussien
Publikováno v:
International Journal of Biological Macromolecules. 157:424-433
The eye lens is rich in proteins called crystallins, whose native conformation is crucial for preserving its transparency. With aging, crystallins may be exposed to environmental changes, which could lead to their aggregation and eventually to catara
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e9ec96670c5a56fe8169f839ef57554
https://doi.org/10.1016/j.ijbiomac.2020.04.079
https://doi.org/10.1016/j.ijbiomac.2020.04.079
Autor:
Malak Abu-Hussien, Guru Krishnakumar Viswanathan, Luba Simhaev, Ashim Paul, Hamutal Engel, Ehud Gazit, Daniel Segal
Publikováno v:
International journal of biological macromolecules. 201
Human γD-crystallin protein is abundant in the lens and is essential for preserving lens transparency. With age the protein may lose its native structure resulting in the formation of cataract. We recently reported an aggregative peptide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d5fb36ab62418d91038c46fa75d118b
https://pubmed.ncbi.nlm.nih.gov/34998884
https://pubmed.ncbi.nlm.nih.gov/34998884
Autor:
Hamutal Engel, Fabien Gosselet, Elad Arad, Guru KrishnaKumar Viswanathan, Itzik Cooper, Dana Shwartz, Chen Shemesh, Avi Raveh, Yelena Losev, Raz Jelinek, Daniel L. Segal, Edward Pichinuk, Ehud Gazit
Publikováno v:
Cellular and Molecular Life Sciences
Cellular and Molecular Life Sciences, Springer Verlag, 2019, ⟨10.1007/s00018-019-03312-0⟩
Cellular and Molecular Life Sciences, Springer Verlag, 2019, ⟨10.1007/s00018-019-03312-0⟩
International audience; Neurofibrillary tangles of the Tau protein and plaques of the amyloid β peptide are hallmarks of Alzheimer's disease (AD), which is characterized by the conversion of monomeric proteins/peptides into misfolded β-sheet rich f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd0427d33b2371643803bc263498a6f9
https://doi.org/10.1007/s00018-019-03312-0
https://doi.org/10.1007/s00018-019-03312-0
Autor:
Ehud Gazit, Ashim Paul, Daniel L. Segal, Salvatore Pacifico, Guru KrishnaKumar Viswanathan, Gianfranco Balboni, Satabdee Mahapatra
Publikováno v:
ACS Chemical Neuroscience. 10:3510-3520
Protein misfolding and amyloid formation are associated with various human diseases including Alzheimer's disease (AD), Parkinson's disease (PD), and Type-2 Diabetes mellitus (T2DM). No disease-modifying therapeutics are available for them. Despite t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df7895495e992d436ba83aeaee6c9914
https://doi.org/10.1021/acschemneuro.9b00123
https://doi.org/10.1021/acschemneuro.9b00123
Autor:
Wen-Hao Li, Raz Jelinek, Ehud Gazit, Ashim Paul, Yan-Mei Li, Elad Arad, Guru KrishnaKumar Viswanathan, Gao Li, Daniel L. Segal, Satabdee Mohapatra
Publikováno v:
Chemical Communications. 55:14621-14624
Glycosylation of amyloidogenic proteins enhances their solubility and reduces propensity for aggregation. We therefore, prepared tryptophan-glucosamine conjugates to modulate aggregation of tau-derived PHF6-peptide. Combined in vitro and in silico ap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09d4614436ce7ba4204cfdc73eb6ef92
https://doi.org/10.1039/c9cc06868f
https://doi.org/10.1039/c9cc06868f
Autor:
Daniel L. Segal, Lukas Wettstein, Vijay Kumar, Satabdee Mohapatra, Jan Münch, Ashim Paul, Elad Arad, Guru KrishnaKumar Viswanathan, Raz Jelinek
Publikováno v:
RSC Chemical Biology
Human semen contains various amyloidogenic peptides derived from Prostatic Acid Phosphatase (PAP) and Semenogelin proteins that are capable of enhancing HIV-1 infection when assembled into fibrils. The best characterized among them is a 39 amino acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4df9ae43d90aedea11b265a29068795c
https://pubmed.ncbi.nlm.nih.gov/34704058
https://pubmed.ncbi.nlm.nih.gov/34704058
