Results 61 to 70 of about 281,561 (238)
Thiol/Disulfide homeostasis in patients with rheumatoid arthritis
Romanian Journal of Internal Medicine, 2019 Background. Oxidative stress may play an important role in rheumatoid arthritis (RA) etiopathogenesis. The thiol group is a very strong antioxidant. In this study, we aimed to investigate the presence of oxidative stress in patients with RA by evaluating
Tuzcu Ayca +9 more
doaj +1 more source
Smaller is better: nanobodies meet NMR
FEBS Letters, EarlyView.Nanobodies are single‐domain antigen‐binding fragments derived from camelid heavy chain antibodies. Their small size, high stability, and exceptional specificity make nanobodies uniquely useful probes for NMR studies of protein dynamics, transient conformational states, and protein–protein interactions.
Oleg Y. Dmitriev
wiley +1 more source
Molecular Oncology, EarlyView.Breast cancer remains a major cause of cancer death in women, frequently developing endocrine therapy resistance. This study demonstrates that upregulated p21‐activated kinase 1 (PAK1) activity drives resistance to tamoxifen and long‐term estrogen deprivation in ER+ breast cancer models.
Luisa Schwarzmüller +10 more
wiley +1 more source
Solvent Induced Disulfide Bond Formation in 2,5-dimercapto-1,3,4-thiadiazole [PDF]
, 2007 Disulfide bond formation is the decisive event in the protein folding to determine the conformation and stability of protein. To achieve this disulfide bond formation in vitro, we took 2,5-dimercapto-1,3,4-thiadiazole (DMcT) as a model compound. We found
Palraj Kalimuthu +2 more
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Electrocatalytic Reduction of Disulfide Bonds in Antibodies [PDF]
In most FDA-approved antibody-drug conjugates, cysteines generated through reduction of the native interchain di-sulfide bonds in monoclonal antibodies (mAbs) are conjugated with maleimide-based cytotoxic payloads.
Cecilia, Bottecchia +6 more
core +1 more source
Thiol-disulfide oxidoreductases: assays, inhibitors, and metabolic roles
, 2022 Thorpe, ColinDisulfide bonds are common post-translational modifications which serve to stabilize or impart function onto proteins. Although this product of oxidation between two cysteine thiols is relatively stable, disulfide bonds are able to undergo ...
Foster, Celia K.
core +1 more source
Frontiers in Plant Science, 2020 In proteins, hydrogen peroxide (H2O2) reacts with redox-sensitive cysteines to form cysteine sulfenic acid, also known as S-sulfenylation. These cysteine oxidation events can steer diverse cellular processes by altering protein interactions, trafficking,
Bo Wei +15 more
doaj +1 more source
PANoptosis in the pathogenesis of myelodysplastic syndromes
Molecular Oncology, EarlyView.PANoptosis, a combination of three types of programmed cell death, is mediated by a large protein complex called a PANoptosome. In healthy bone marrow hematopoietic cells, PANoptosis is restricted by inhibitory signaling. In MDS, bone marrow cells become sensitive to the PANoptotic stimuli due to the aberrant inactivation of inhibitory signaling or ...
Rohit Thalla +4 more
wiley +1 more source
Raman‐based label‐free microscopic analysis of the pancreas in living zebrafish larvae
FEBS Open Bio, EarlyView.Forward stimulated Raman scattering (F‐SRS) and epi coherent anti‐Stokes Raman scattering (E‐CARS) allow label‐free discrimination of distinct subcellular structures in the pancreas of living zebrafish larvae. Given the straightforward applicability, we anticipate broad implementation of Raman microscopy in other organs and across various biomedical ...
Noura Faraj +3 more
wiley +1 more source
Characterisation of the oxidoreductase Erol-Lß and the misfolding of the secretory pathway substrate HLA-B27 [PDF]
, 2007 The endoplasmic reticulum (ER) is the site of oxidative folding for proteins entering the secretory pathway. Here, nascent polypeptides acquire disulfide bonds, which confer both stability and functionality on secretory and ER-resident proteins.
Lemin, Andrew James
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