Results 71 to 80 of about 92,941 (293)

Protein evolution speed depends on its stability and abundance and on chaperone concentrations. [PDF]

open access: yes, 2018
Proteins evolve at different rates. What drives the speed of protein sequence changes? Two main factors are a protein's folding stability and aggregation propensity. By combining the hydrophobic-polar (HP) model with the Zwanzig-Szabo-Bagchi rate theory,
Agozzino, Luca, Dill, Ken A
core   +1 more source

The proteasome biogenesis regulator Rpn4 cooperates with the unfolded protein response to promote ER stress resistance

open access: yes, 2019
Misfolded proteins in the endoplasmic reticulum (ER) activate the unfolded protein response (U PR), which enhances protein folding to restore homeostasis.
Aviram   +87 more
core   +1 more source

Missense mutations in the perforin (PRF1) gene as a cause of hereditary cancer predisposition [PDF]

open access: yes, 2016
Perforin, a pore-forming toxin released from secretory granules of NK cells and CTLs, is essential for their cytotoxic activity against infected or cancerous target cells.
Chaudhry, MS   +7 more
core   +1 more source

Kelvin Probe Force Microscopy in Bionanotechnology: Current Advances and Future Perspectives

open access: yesAdvanced Materials, EarlyView.
Kelvin probe force microscopy (KPFM) enables the nanoscale mapping of electrostatic surface potentials. While widely applied in materials science, its use in biological systems remains emerging. This review presents recent advances in KPFM applied to biological samples and provides a critical perspective on current limitations and future directions for
Ehsan Rahimi   +4 more
wiley   +1 more source

TOM40 Mediates Mitochondrial Dysfunction Induced by α-Synuclein Accumulation in Parkinson's Disease. [PDF]

open access: yes, 2013
Alpha-synuclein (α-Syn) accumulation/aggregation and mitochondrial dysfunction play prominent roles in the pathology of Parkinson's disease. We have previously shown that postmortem human dopaminergic neurons from PD brains accumulate high levels of ...
A Bender   +60 more
core   +3 more sources

Integrating Vibrio natriegens for Photon Manipulation in Living Lighting Devices

open access: yesAdvanced Materials, EarlyView.
Rationalization of genetic and material engineering tools has enabled the engineering of fluorescent Vibrio natriegens (V. natriegens) to fabricate straightforward, highly emissive and stable V. natriegens‐silicones color filters for the first red‐emitting bacteria‐hybrid light‐emitting diodes. This pinpoints V. natriegens as a high‐performance protein
Stephanie Willeit   +6 more
wiley   +1 more source

Na+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction.

open access: yesPLoS ONE, 2011
Transmissible spongiform encephalopathies are characterised by widespread deposition of fibrillar and/or plaque-like forms of the prion protein. These aggregated forms are produced by misfolding of the normal prion protein, PrP(C), to the disease ...
James F Graham   +8 more
doaj   +1 more source

Turning Unpredictable Biomolecule Adsorption to Controlled Corona Formation: Focus on Carbon Nanomaterials

open access: yesAdvanced Materials, EarlyView.
Controlling the protein corona formation onto carbon nanomaterials (CNMs) enhances their functionalities as platforms for cancer theranostics. Here, we reviewed the effects of the intrinsic and acquired properties of CNMs on protein corona formation, the consequent biological and toxicological outcomes, and the strategies to reshape corona formation ...
Yajuan Zou   +5 more
wiley   +1 more source

The Role of Protein S-Nitrosylation in Protein Misfolding-Associated Diseases

open access: yesLife, 2021
Abnormal and excessive nitrosative stress contributes to neurodegenerative disease associated with the production of pathological levels of misfolded proteins.
Yun-Jin Ju   +3 more
doaj   +1 more source

QBP1 Peptide as a Potential Anti‐Amyloidogenic Therapy for Type 2 Diabetes: An In Vitro Study

open access: yesAdvanced Science, EarlyView.
The anti‐amyloidogenic peptide QBP1 effectively halts human islet amyloid polypeptide (hIAPP) aggregation, preventing the formation of toxic β‐structured intermediates. Through a combination of biophysical assays, molecular dynamics, and cell‐based studies, QBP1 is shown to preserve β‐cell viability and metabolic homeostasis, positioning it as a ...
María M. Tejero‐Ojeda   +8 more
wiley   +1 more source

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