Results 81 to 90 of about 95,914 (208)

Estrogens promote misfolded proinsulin degradation to protect insulin production and delay diabetes [PDF]

, 2018
Summary: Conjugated estrogens (CE) delay the onset of type 2 diabetes (T2D) in postmenopausal women, but the mechanism is unclear. In T2D, the endoplasmic reticulum (ER) fails to promote proinsulin folding and, in failing to do so, promotes ER stress and
Allard, Camille, Alvarez-Mercado, Ana I, Arvan, Peter, Coons, Laurel A, Floyd, Z. Elizabeth, Fuselier, Taylor, Hewitt, Sylvia C, Kim, Jun Ho, Korach, Kenneth S, Levin, Ellis R, Mauvais-Jarvis, Franck, Urano, Fumihiko, Xu, Beibei   +12 more
core   +2 more sources

Misfolded Proteins and Retinal Dystrophies [PDF]

, 2009
Many mutations associated with retinal degeneration lead to the production of misfolded proteins by cells of the retina. Emerging evidence suggests that these abnormal proteins cause cell death by activating the Unfolded Protein Response, a set of conserved intracellular signaling pathways that detect protein misfolding within the endoplasmic reticulum
Jonathan H, Lin, Matthew M, Lavail
openaire   +2 more sources

Single-molecule digital sizing of proteins in solution

Nature Communications
The physical characterization of proteins in terms of their sizes, interactions, and assembly states is key to understanding their biological function and dysfunction.
Georg Krainer, Raphael P. B. Jacquat, Matthias M. Schneider, Timothy J. Welsh, Jieyuan Fan, Quentin A. E. Peter, Ewa A. Andrzejewska, Greta Šneiderienė, Magdalena A. Czekalska, Hannes Ausserwoeger, Lin Chai, William E. Arter, Kadi L. Saar, Therese W. Herling, Titus M. Franzmann, Vasilis Kosmoliaptsis, Simon Alberti, F. Ulrich Hartl, Steven F. Lee, Tuomas P. J. Knowles   +19 more
doaj   +1 more source

Mechanisms of mutant SOD1 induced mitochondrial toxicity in amyotrophic lateral sclerosis

Frontiers in Cellular Neuroscience, 2014
In amyotrophic lateral sclerosis (ALS) mitochondrial dysfunction is recognized as one of the key elements contributing to the pathology. Mitochondria are the major source of intracellular reactive oxygen species (ROS). Increased production of ROS as well
Piia eVehviläinen, Jari eKoistinaho, Gundars eGoldsteins   +2 more
doaj   +1 more source

The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation [PDF]

, 2002
Mutations in the photopigment rhodopsin are the major cause of autosomal dominant retinitis pigmentosa. The majority of mutations in rhodopsin lead to misfolding of the protein.
Cheetham, ME, Luthert, PJ, Munro, PMG, Saliba, RS   +3 more
core  

On the statistical mechanics of prion diseases

, 2001
We simulate a two-dimensional, lattice based, protein-level statistical mechanical model for prion diseases (e.g., Mad Cow disease) with concommitant prion protein misfolding and aggregation.
A. Coghlan, A. Slepoy, C. I. Lasmézas, D. J. Stekel, D. L. Cox, D. O. V. Alonso, F. Pázmándi, H. Rudyk, J. H. Come, J. Masel, J. N. Onuchic, J. S. Griffith, K. Post, M. A. Nowak, M. Beekes, M. Eigen, M. Horiuchi, M. Horiuchi, M. Laurent, R. Demaimay, R. M. Anderson, R. R. P. Singh, R. V. Kulkarni, S. B. Prusiner, T. R. Serio, W. Swietnicki   +25 more
core   +1 more source

Cotranslational folding of proteins on the ribosome.

, 2020
Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the ribosome can alter the folding trajectory in many different ways ...
Liutkute, M., Rodnina, M., Samatova, E.
core   +1 more source

Fibrillin-1 Misfolding and Disease

Antioxidants & Redox Signaling, 2006
Fibrillin-1 is a 350 kDa calcium-binding protein which assembles to form 10-12 nm microfibrils in the extracellular matrix (ECM). The structure of fibrillin-1 is dominated by two types of disulfide-rich motifs, the calcium- binding epidermal growth factor-like (cbEGF) and transforming growth factor beta binding protein-like (TB) domains.
Whiteman, P, Hutchinson, S, Handford, P
openaire   +3 more sources

Oncogenic Gain of Function in Glioblastoma Is Linked to Mutant p53 Amyloid Oligomers. [PDF]

, 2020
Tumor-associated p53 mutations endow cells with malignant phenotypes, including chemoresistance. Amyloid-like oligomers of mutant p53 transform this tumor suppressor into an oncogene.
de Oliveira, Guilherme AP, Ferretti, Giulia DS, Gratton, Enrico, Lima, Flavia RS, Motta, Michelle F, Norberto, Douglas R, Pedrote, Murilo M, Silva, Jerson L, Spohr, Tania CLS   +8 more
core   +1 more source

Chitosan-myristate nanogel as an artificial chaperone protects neuroserpin from misfolding

Advanced Biomedical Research, 2016
Background: Molecular chaperon-like activity for protein refolding was studied using nanogel chitosan-myristic acid (CMA) and the protein neuroserpin (NS), a member of the serine proteinase inhibitor superfamily (serpin).
Habib Nazem, Afshin Mohsenifar, Sahar Majdi   +2 more
doaj   +1 more source