Results 161 to 170 of about 4,213 (194)

Decoding cuproptosis and cuproplasia: implications for therapeutic strategies in renal cell carcinoma. [PDF]

Cell Death Discov
Abraham Gnanadass S, Pandey S, Viswanathan P.   +2 more
europepmc   +1 more source

Copper in the colorectal cancer microenvironment: pioneering a new era of cuproptosis-based therapy. [PDF]

Front Oncol
Feng Q, Sun Y, Yang Z, Wang Z, Chen Z, Liu F, Liu L.   +6 more
europepmc   +1 more source

Cuproplasia and cuproptosis, two sides of the coin. [PDF]

Cancer Commun (Lond)
Lu K, Wijaya CS, Yao Q, Jin H, Feng L.
europepmc   +1 more source

Epigenetic modification of cuproptosis by non-coding RNAs in cancer drug resistance. [PDF]

Mol Cancer
Du F, Tang L, Wang F, Jiang X, Li J, Wang G, Zhang Z.   +6 more
europepmc   +1 more source

Hybrid Biological Hydrogel Provides Favorable Bioenergetic, Adhesive, and Antioxidative Effects on Wound Healing. [PDF]

ACS Biomater Sci Eng
Zhang X, Hu Z, Pörtner R, Zeng AP.
europepmc   +1 more source

ABHD11 mediated deglutarylation regulates the TCA cycle and T cell metabolism

Grice GL, Minogue E, Coates HW, Debela M, Kaneider-Kaser N, Antrobus PR, Johnson RS, Nathan JA.   +7 more
europepmc   +1 more source

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Chemical Tagging of Protein Lipoylation

Angewandte Chemie, 2020
AbstractProtein lipoylation is a post‐translational modification of emerging importance in both prokaryotes and eukaryotes. However, labeling and large‐scale profiling of protein lipoylation remain challenging. Here, we report the development of iLCL (iodoacetamide‐assisted lipoate‐cyclooctyne ligation), a chemoselective reaction that enables chemical ...
Qi Tang, Yilan Guo, Liying Meng, Xing Chen   +3 more
openaire   +2 more sources

N-lipoyl glucosamine and N-lipoyl glucosaminitol: Substrates for lipoyl dehydrogenase

Archives of Biochemistry and Biophysics, 1969
Abstract N - dl -Lipoyl- d -glucosamine and N - dl -lipoyl- d -glucosaminitol were prepared and tested as substrates for lipoyl dehydrogenase (reduced nicotinamide adenine dinucleotide: Lipoamide oxidoreductase, EC 1.6.4.3). It was anticipated that such lipoateamino carbohydrate derivatives would be superior substrates for the enzyme, having ...
A L, Fluharty, G L, Adelson, B P, Gaber
openaire   +2 more sources

Quantitative Site-Specific Chemoproteomic Profiling of Protein Lipoylation

Journal of the American Chemical Society, 2022
Protein lipoylation is an evolutionarily conserved post-translational modification from prokaryotes to eukaryotes. Lipoylation is implicated with several human diseases, including metabolic disorders, cancer, and Alzheimer's disease. While individual lipoylated proteins have been biochemically studied, a strategy for globally quantifying lipoylation ...
Shuchang Lai, Ying Chen, Fan Yang, Weidi Xiao, Yuan Liu, Chu Wang   +5 more
openaire   +2 more sources