Results 111 to 120 of about 3,418,558 (223)

Nitric Oxide in Cancer: Mechanisms, Dual Role, and Therapeutic Strategies

open access: yesMedComm – Oncology, Volume 5, Issue 3, September 2026.
Nitric oxide exerts concentration‐dependent dual roles in cancer, functioning as either a tumor promoter or suppressor. This review comprehensively examines NO's multifaceted regulation of tumor biology, including S‐nitrosylation signaling, metabolic reprogramming, immunemodulation, and therapy resistance, and highlights emerging therapeutic strategies
Jia Shao   +8 more
wiley   +1 more source

Protein disulfide isomerase blocks CEBPA translation and is up-regulated during the unfolded protein response in AML

open access: yes, 2011
Deregulation of the myeloid key transcription factor CEBPA is a common event in acute myeloid leukemia (AML). We previously reported that the chaperone calreticulin is activated in subgroups of AML patients and that calreticulin binds to the stem loop ...
Schaubitzer, Kerstin   +13 more
core   +1 more source

Edible Insect Allergens: An Emerging Food Safety Challenge

open access: yesSustainable Food Proteins, Volume 4, Issue 3, September 2026.
Allergic responses to edible insects arise via two main pathways: cross‐reactivity with homologous arthropod allergens and primary sensitization to edible insect proteins, both leading to IgE‐mediated immune activation. ABSTRACT Edible insects are increasingly promoted as sustainable protein sources; however, their allergenic potential remains a ...
Changqi Liu   +5 more
wiley   +1 more source

Antibody Conjugates via Disulfide Bridging: Towards therapeutic and diagnostic applications [PDF]

open access: yes, 2015
Antibodies play a prominent role in chemical and biological research and the largest application of chemical bioconjugation reagents is in the production of antibody conjugates.
Hull, EA
core  

Folding of peptides and proteins: role of disulfide bonds, recent developments

open access: yesBiomolecular Concepts, 2013
Disulfide-containing proteins are ideal models for studies of protein folding as the folding intermediates can be observed, trapped, and separated by HPLC during the folding reaction.
Hidaka Yuji, Shimamoto Shigeru
doaj   +1 more source

Identification and Functional Analysis of a Protein Disulfide Isomerase (AtPDI1) in Arabidopsis thaliana

open access: yesFrontiers in Plant Science, 2018
Protein disulfide isomerase (PDI) catalyzes the conversion of thiol-disulfide and plays an important role in various physiological events in animals. A PDI (OaPDI) from a tropical plant was detailed studied and it was found to be involved in response of ...
Zhengrong Zhang   +5 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

Genomic and evolutionary analysis reveals dynamic variations of MKK3 gene, a key regulator for seed dormancy in barley

open access: yesThe Plant Genome, Volume 19, Issue 3, September 2026.
Abstract Barley (Hordeum vulgare L.) is an important crop in the world, and its seed dormancy is primarily controlled by a mitogen‐activated protein kinase kinase 3 (MKK3) gene. Although kinase activity of MKK3 and its roles in barley post‐domestication have been widely studied, the pre‐domestication evolution of MKK3 and the spread of nondormant ...
Lydia G. Tressel   +3 more
wiley   +1 more source

FUNCTIONAL PROPERTIES OF THE PROTEIN DISULFIDE OXIDOREDUCTASE FROM THE ARCHAEON PYROCOCCUS FURIOSUS: A MEMBER OF A NOVEL PROTEIN FAMILY RELATED TO PROTEIN DISULFIDE-ISOMERASE.

open access: yes, 2004
Protein disulfide oxidoreductases are ubiquitous redox enzymes that catalyse dithiol-disulfide exchange reactions with a CXXC sequence motif at their active site.
Ladenstein R   +4 more
core   +1 more source

Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols

open access: yesAntioxidants
Thiol isomerases are a family of enzymes that participate in oxidative protein folding. They contain highly reactive vicinal thiols in a CXXC motif within their catalytic domains to mediate thiol-disulfide switching as part of their reductase, oxidase ...
Osamede C. Owegie   +3 more
doaj   +1 more source

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