Results 221 to 230 of about 6,771,465 (361)

HSP70 governs permeability and mechanotransduction in primary human endothelial cells

open access: yesFEBS Open Bio, EarlyView.
HSP70 chemical inhibition reduces endothelial cell proliferation and increases permeability, the latter supported by normal interendothelial junctional protein distribution. HSP70 also plays a role in shear stress response, a hemodynamic force naturally present in blood vessels and correlated with vessel protection.
Andrea Pinto‐Martinez   +5 more
wiley   +1 more source

Protein folding as a jamming transition. [PDF]

open access: yesPRX Life
Grigas AT   +4 more
europepmc   +1 more source

Homologous expression and purification of human HAX‐1 for structural studies

open access: yesFEBS Open Bio, EarlyView.
This research protocol provides detailed instructions for cloning, expressing, and purifying large quantities of the intrinsically disordered human HAX‐1 protein, N‐terminally fused to a cleavable superfolder GFP, from mammalian cells. HAX‐1 is predicted to undergo posttranslational modifications and to interact with membranes, various cellular ...
Mariana Grieben
wiley   +1 more source

Energy landscape in protein folding and unfolding

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2016
F. Mallamace   +11 more
semanticscholar   +1 more source

Thrombolytic proteins profiling: High‐throughput activity, selectivity, and resistance assays

open access: yesFEBS Open Bio, EarlyView.
We present optimized biochemical protocols for evaluating thrombolytic proteins, enabling rapid and robust screening of enzymatic activity, inhibition resistance, and fibrin affinity, stimulation, and selectivity. The outcome translates to key clinical indicators such as biological half‐life and bleeding risk. These assays streamline the development of
Martin Toul   +3 more
wiley   +1 more source

Cooperativity and modularity in protein folding [PDF]

open access: green, 2016
Masaki Sasai   +2 more
openalex   +1 more source

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