Results 91 to 100 of about 3,392,726 (209)

Inhibition of KDEL Receptors Remodels the Tumor Microenvironment for T Cell Independent Tumor Regression

open access: yesAdvanced Science, Volume 13, Issue 51, 14 September 2026.
Inhibition of KDELR2 in a small fraction of tumor cells generates sustainable immunogenic cell death conditions within the tumor microenvironment. These conditions promote the regression of tumors in a T cell independent manner. During regression, macrophages prime T cells that subsequently provide systemic protection against recurrence. The potency of
Shakti P Pattanayak   +6 more
wiley   +1 more source

Pharmacologic ATF6 activating compounds are metabolically activated to selectively modify endoplasmic reticulum proteins

open access: yeseLife, 2018
Pharmacologic arm-selective unfolded protein response (UPR) signaling pathway activation is emerging as a promising strategy to ameliorate imbalances in endoplasmic reticulum (ER) proteostasis implicated in diverse diseases.
Ryan Paxman   +6 more
doaj   +1 more source

Quantitative Structure–Activity Relationship Approaches for Exploring the Anticancer Potential of Flavonoids

open access: yesChemistry &Biodiversity, Volume 23, Issue 9, September 2026.
QSAR‐based analysis of flavonoids to identify structural determinants of anticancer activity and prioritize promising candidates. ABSTRACT Flavonoids are structurally diverse polyphenolic compounds widely distributed in fruits, vegetables, grains, and beverages, with considerable potential as anticancer agents.
Mukta Gupta   +4 more
wiley   +1 more source

Oxidative Stress in Fungi: Its Function in Signal Transduction, Interaction with Plant Hosts, and Lignocellulose Degradation

open access: yesBiomolecules, 2015
In this review article, we want to present an overview of oxidative stress in fungal cells in relation to signal transduction, interaction of fungi with plant hosts, and lignocellulose degradation.
Michael Breitenbach   +4 more
doaj   +1 more source

Selective Inhibition of Protein Disulfide Isomerase by Estrogens

open access: yesJournal of Biological Chemistry, 1989
Protein disulfide isomerase (PDI) is a multifunctional microsomal enzyme that participates in the formation of protein disulfide bonds. PDI catalyzes the reduction of protein disulfide bonds in the presence of excess reduced glutathione and has been implicated in the reductive degradation of insulin; E.
J C, Tsibris   +5 more
openaire   +2 more sources

A New Vista of Opportunity in Diabetes Management: Natural Product‐Based β‐cell Preservation

open access: yesFood Chemistry International, Volume 2, Issue 3, Page 334-351, September 2026.
Preserving functional β‐cells via natural products offers promising strategy for diabetes treatment. ABSTRACT A defining characteristic of diabetes is β‐cell failure, in which β‐cells cannot modulate insulin secretion to compensate for escalating insulin resistance, pushing forward disease development.
Yi‐San Lee   +4 more
wiley   +1 more source

Smart Design: Integrating Artificial Intelligence and Gene Editing for Advanced mRNA Therapeutics

open access: yesMedComm – Biomaterials and Applications, Volume 5, Issue 3, September 2026.
The challenges of mRNA therapy and the application of artificial intelligence and gene editing in the field of mRNA drugs. ABSTRACT Artificial intelligence (AI) and gene editing are increasingly being applied to the design and evaluation of mRNA therapeutics.
Haixing Shi   +11 more
wiley   +1 more source

Natural Products Targeting Protein Disulfide Isomerases: New Frontiers for Diabetes, Cancer, and Coagulation

open access: yesFood Frontiers
The protein disulfide isomerase (PDI) family comprises 21 members that have oxidase, reductase, isomerase, and foldase activities essential for human health and disease. Protein disulfide isomerase A4 (PDIA4) is the largest member in this family.
Yi‐San Lee   +4 more
doaj   +1 more source

High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility [PDF]

open access: yes, 2013
ERp27 (endoplasmic reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase) localized to the endoplasmic reticulum. ERp27 is predicted to consist of two thioredoxin-fold domains homologous with the non-catalytic b and b' domains of
Freedman, R. B.   +15 more
core   +1 more source

Mitochondria as the Hub of Apoptosis: A Comprehensive Insight From Mitochondria to Interactions With Other Organelles

open access: yesMedComm, Volume 7, Issue 9, September 2026.
Mitochondria is the hub of apoptosis in various diseases. The disruption of mitochondrial structure (including membrane rupture, cristae remodeling, and mitochondrial membrane lipid redistribution), the imbalance of mitochondrial dynamics (including fusion and fission, autophagy), the release, disruption, and mutation of mitochondria DNA, as well as ...
Rubin Tan   +9 more
wiley   +1 more source

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