APPENDIX 3 DNA-ADDUCTION AND PROTEIN-ADDUCT IMMUNOASSAYS

1990 ◽  
pp. 353-360
Keyword(s):  
Protein Adduct ◽  
Dna Adduction

Probing the Paradigm of Promiscuity for N‐Heterocyclic Carbene Complexes and their Protein Adduct Formation

2021 ◽  
Author(s):  
Matthew P. Sullivan ◽  
Monika Cziferszky ◽  
Iogann Tolbatov ◽  
Dianna Truong ◽  
Davide Mercadante ◽  
...  
Keyword(s):  
Adduct Formation ◽  
Carbene Complexes ◽  
Protein Adduct

Probing the Paradigm of Promiscuity for N‐Heterocyclic Carbene Complexes and their Protein Adduct Formation

2021 ◽  
Author(s):  
Matthew P. Sullivan ◽  
Monika Cziferszky ◽  
Iogann Tolbatov ◽  
Dianna Truong ◽  
Davide Mercadante ◽  
...  
Keyword(s):  
Adduct Formation ◽  
Carbene Complexes ◽  
Protein Adduct

scholarly journals Protein adduct biomarkers: state of the art.

1996 ◽  
Vol 104 (suppl 5) ◽  
pp. 879-882 ◽  
Author(s):  
M J Meyer ◽  
W E Bechtold
Keyword(s):  
State Of The Art ◽  
Protein Adduct

scholarly journals Dietary phenolics as anti-mutagens and inhibitors of tobacco-related DNA adduction in the urothelium of smokers

1996 ◽  
Vol 17 (10) ◽  
pp. 2193-2200 ◽  
Author(s):  
Christian Malaveille ◽  
Agnfès Hautefeuille ◽  
Brigitte Pignatelli ◽  
Glenn Talaska ◽  
Paolo Vineis ◽  
...  
Keyword(s):  
Dna Adduction

scholarly journals PROTEIN ADDUCT SPECIES IN MUSCLE AND LIVER OF RATS FOLLOWING ACUTE ETHANOL ADMINISTRATION

2005 ◽  
Vol 40 (6) ◽  
pp. 485-493 ◽  
Author(s):  
VINOOD B. PATEL ◽  
SIMON WORRALL ◽  
PETER W. EMERY ◽  
VICTOR R. PREEDY
Keyword(s):  
Ethanol Administration ◽  
Protein Adduct ◽  
Acute Ethanol

scholarly journals The effects of changes in glutathione levels through exogenous agents on intracellular cysteine content and protein adduct formation in chronic alcohol-treated VL17A cells

2016 ◽  
Vol 27 (2) ◽  
pp. 128-135 ◽  
Author(s):  
S. Mathan Kumar ◽  
Madhumitha Haridoss ◽  
Kavitha Swaminathan ◽  
Ramesh Kumar Gopal ◽  
Dahn Clemens ◽  
...  
Keyword(s):  
Adduct Formation ◽  
Chronic Alcohol ◽  
Protein Adduct ◽  
Exogenous Agents ◽  
Cysteine Content

scholarly journals Isoleucine 44 Hydrophobic Patch Controls Toxicity of Unanchored, Linear Ubiquitin Chains through NF-κB Signaling

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1519 ◽  
Author(s):  
Jessica R. Blount ◽  
Kozeta Libohova ◽  
Gustavo M. Silva ◽  
Sokol V. Todi
Keyword(s):  
Drosophila Melanogaster ◽  
Fruit Fly ◽  
Post Translational Modification ◽  
Ubiquitin Chain ◽  
Interaction Site ◽  
Cellular Processes ◽  
Protein Adduct ◽  
Linear Chains ◽  
Linear Poly ◽  
Free Ubiquitin

Ubiquitination is a post-translational modification that regulates cellular processes by altering the interactions of proteins to which ubiquitin, a small protein adduct, is conjugated. Ubiquitination yields various products, including mono- and poly-ubiquitinated substrates, as well as unanchored poly-ubiquitin chains whose accumulation is considered toxic. We previously showed that transgenic, unanchored poly-ubiquitin is not problematic in Drosophila melanogaster. In the fruit fly, free chains exist in various lengths and topologies and are degraded by the proteasome; they are also conjugated onto other proteins as one unit, eliminating them from the free ubiquitin chain pool. Here, to further explore the notion of unanchored chain toxicity, we examined when free poly-ubiquitin might become problematic. We found that unanchored chains can be highly toxic if they resemble linear poly-ubiquitin that cannot be modified into other topologies. These species upregulate NF-κB signaling, and modulation of the levels of NF-κB components reduces toxicity. In additional studies, we show that toxicity from untethered, linear chains is regulated by isoleucine 44, which anchors a key interaction site for ubiquitin. We conclude that free ubiquitin chains can be toxic, but only in uncommon circumstances, such as when the ability of cells to modify and regulate them is markedly restricted.

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