Results 71 to 80 of about 3,672,982 (262)

Proteome-Wide Analyis of Chaperonin-Dependent Protein Folding in Escherichia coli [PDF]

open access: yes, 2006
In Escherichia coli, the cylindrical chaperonin GroEL and its cofactor GroES promote the folding of a fraction of newly synthesized polypeptide chains by acting as an Anfinsen cage.
Maier, Tobias
core   +1 more source

Rational design of structure‐based vaccines targeting misfolded alpha‐synuclein conformers of Parkinson's disease and related disorders

open access: yesBioengineering & Translational Medicine
Synucleinopathies, including Parkinson's disease (PD), multiple system atrophy (MSA), and dementia with Lewy bodies (DLB), are neurodegenerative disorders caused by the accumulation of misfolded alpha‐synuclein protein.
Jose Miguel Flores‐Fernandez   +13 more
doaj   +1 more source

Propagation of PrPSc in mice reveals impact of aggregate composition on prion disease pathogenesis

open access: yesCommunications Biology, 2023
Infectious prions consist of PrPSc, a misfolded, aggregation-prone isoform of the host’s prion protein. PrPSc assemblies encode distinct biochemical and biological properties.
Sheng Chun Chang   +6 more
doaj   +1 more source

Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation

open access: yesFEBS Letters, EarlyView.
Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang   +2 more
wiley   +1 more source

Distinct patterns of prion strain deposition and toxicity in a novel whole brain organotypic slice culture system

open access: yesScientific Reports
Prion diseases are fatal transmissible neurodegenerative diseases that affect many mammals, including humans, caused by the templated misfolding of the prion protein.
Hailey Pineau, Valerie L. Sim
doaj   +1 more source

The microbiome in human skin aging

open access: yesFEBS Letters, EarlyView.
Age‐related skin changes encompass the well‐known visible phenotypic alterations, together with microbiome dysbiosis and a series of molecular aging hallmarks. These hallmarks characterize not only a fully stablished aged phenotype but also the skin aging process itself.
Manuel Huerta Arana   +3 more
wiley   +1 more source

Relative domain folding and stability of a membrane transport protein [PDF]

open access: yes, 2014
There is a limited understanding of the folding of multidomain membrane proteins. Lactose permease (LacY) of Escherichia coli is an archetypal member of the major facilitator superfamily of membrane transport proteins, which contain two domains of six ...
Findlay, Heather E.   +8 more
core   +1 more source

An ancient conserved role for prion protein in learning and memory

open access: yesBiology Open, 2018
The misfolding of cellular prion protein (PrPC) to form PrP Scrapie (PrPSc) is an exemplar of toxic gain-of-function mechanisms inducing propagated protein misfolding and progressive devastating neurodegeneration. Despite this, PrPC function in the brain
Patricia L. A. Leighton   +4 more
doaj   +1 more source

Autophagy and mitophagy in pancreatic β‐cell homeostasis and their involvement in diabetes pathophysiology

open access: yesFEBS Letters, EarlyView.
This review focuses on the role of autophagy and mitophagy in maintaining pancreatic β‐cell function and homeostasis. We discuss how genetic defects affecting these pathways contribute to the development of type 1, type 2, monogenic, and gestational diabetes. We further explore their potential as therapeutic targets. Created in BioRender.
Yunkyeong Lee   +2 more
wiley   +1 more source

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