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ProteomicsMapping sites of carboxymethyllysine modification on proteins reveals consequences for proteostasis and cell proliferation
Posttranslational mechanisms play a key role in modifying the abundance and function of cellular proteins. Among these, modification by advanced glycation end products (AGEs) has been shown to accumulate during aging and age-associated diseases but specific protein targets and functional consequence...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2021-11-25 | PXD027526 | Pride
Heart Acetylation Mass spectrometry Tubulin Kidney Mice Endothelial cell Cell cycle Microtubules Advanced glycation end products Carboxymethyllysine Mitosis Liver Glyoxal Proteasome Aging Posttranslational modification 
UnknownInter- and Intraindividual Differences in the Capacity of the Human Intestinal Microbiome in Fecal Slurries to Metabolize Fructoselysine and Carboxymethyllysine.
Not available
S-EPMC9501902 | biostudies-literature
UnknownComprehensive Quantification of Carboxymethyllysine-Modified Peptides in Human Plasma.
Not available
S-EPMC8075102 | biostudies-literature
UnknownDiabetic nephropathy patients show hyper-responsiveness to N6-carboxymethyllysine.
Not available
S-EPMC9322834 | biostudies-literature
UnknownA novel monoclonal antibody targeting carboxymethyllysine, an advanced glycation end product in atherosclerosis and pancreatic cancer.
Not available
S-EPMC5805250 | biostudies-literature
UnknownAnaerobic Degradation of N-ε-Carboxymethyllysine, a Major Glycation End-Product, by Human Intestinal Bacteria.
Not available
S-EPMC6566499 | biostudies-literature
UnknownEffect of Nɛ-carboxymethyllysine on oxidative stress and the glutathione system in beta cells.
Not available
S-EPMC5598217 | biostudies-literature
ProteomicsMapping sites of carboxymethyllysine modification on proteins reveals consequences for proteostasis and cell proliferation
Posttranslational mechanisms play a key role in modifying the abundance and function of cellular proteins. Among these, modification by advanced glycation end products (AGEs) has been shown to accumulate during aging and age-associated diseases but specific protein targets and functional consequence...
ORGANISM(S): Homo sapiens (Human) 
2021-11-25 | PXD021891 | Pride
Heart Acetylation Mass spectrometry Tubulin Kidney Mice Endothelial cell Cell cycle Microtubules Advanced glycation end products Carboxymethyllysine Mitosis Liver Glyoxal Proteasome Aging Posttranslational modification 
ProteomicsMapping sites of carboxymethyllysine modification on proteins reveals consequences for proteostasis and cell proliferation
Posttranslational mechanisms play a key role in modifying the abundance and function of cellular proteins. Among these, modification by advanced glycation end products (AGEs) has been shown to accumulate during aging and age-associated diseases but specific protein targets and functional consequence...
ORGANISM(S): Mus musculus (Mouse) 
2021-11-25 | PXD021883 | Pride
Heart Acetylation Mass spectrometry Tubulin Kidney Mice Endothelial cell Cell cycle Microtubules Advanced glycation end products Carboxymethyllysine Mitosis Liver Glyoxal Proteasome Aging Posttranslational modification 
ProteomicsMapping sites of carboxymethyllysine modification on proteins reveals consequences for proteostasis and cell proliferation
Posttranslational mechanisms play a key role in modifying the abundance and function of cellular proteins. Among these, modification by advanced glycation end products (AGEs) has been shown to accumulate during aging and age-associated diseases but specific protein targets and functional consequence...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2021-11-25 | PXD021985 | Pride
Heart Acetylation Mass spectrometry Tubulin Kidney Mice Endothelial cell Cell cycle Microtubules Advanced glycation end products Carboxymethyllysine Mitosis Liver Glyoxal Proteasome Aging Posttranslational modification 
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