Results 91 to 100 of about 3,418,558 (223)
Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway
Disulfide bonds are an abundant feature of proteins across all domains of life that are important for structure, stability, and function. In eukaryotic cells, a major site of disulfide bond formation is the endoplasmic reticulum (ER).
Philip J. Robinson, Neil J. Bulleid
doaj +1 more source
The Lord of the Rings: Cysteine bonds crosslink the tail of siphovirus
Abstract Long, non‐contractile tails composed of helical hexameric protein repeats that assemble into continuous tubular structures characterize siphoviruses. The siphovirus tail tube protein gp39 contains two cysteine residues per monomer. Cryo‐electron microscopy revealed that these cysteines are oriented toward the interface between the rings, which
Simona Povilonienė +9 more
wiley +1 more source
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
RNA‐seq and Batelli gland proteomics of fifth‐instar Mahanarva spectabilis nymphs reveal transcripts and proteins associated with xylem feeding, foam production and environmental interaction. Functional annotation identified genes involved in osmoregulation, detoxification, chemosensation and stress responses, while proteomic analysis confirmed ...
Monique da Silva Bonjour +8 more
wiley +1 more source
Cardioprotective hormone relaxin‐2 showed relevant effects on rat skeletal muscle by altering proteins linked to muscle function, regeneration, differentiation, mitochondrial function, glucose metabolism, and structural integrity and organization. Specifically, relaxin‐2 reduced the expression of 95 proteins, increased 32, and elicited unique proteins ...
Xocas Vázquez‐Abuín +11 more
wiley +1 more source
Protein Disulfide Isomerase Modulates the Activation of Thyroid Hormone Receptors
Thyroid hormone receptors (TRs) are responsible for mediating thyroid hormone (T3 and T4) actions at a cellular level. They belong to the nuclear receptor (NR) superfamily and execute their main functions inside the cell nuclei as hormone-regulated ...
Jessica L. O. Campos +17 more
doaj +1 more source
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
Aims: Thioredoxin (TRX)-fold proteins are ubiquitous in nature. This redox scaffold has evolved to enable a variety of functions, including redox regulation, protein folding, and oxidative stress defense.
Totsika, Makrina +16 more
core +1 more source
Apolipoprotein (apo) B is an obligatory component of very low density lipoprotein (VLDL), and its cotranslational and posttranslational modifications are important in VLDL synthesis, secretion, and hepatic lipid homeostasis. ApoB100 contains 25 cysteine residues and eight disulfide bonds. Although these disulfide bonds were suggested to be important in
Wang, Shiyu +7 more
openaire +3 more sources
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

