about
4-Hydroxynonenal (HNE) modified proteins in metabolic diseasesLipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblastsAccumulation of modified proteins and aggregate formation in aging.Reprint of "accumulation of modified proteins and aggregate formation in aging".Iron oxide particles for molecular magnetic resonance imaging cause transient oxidative stress in rat macrophages.Advanced glycation end products and oxidative stress in type 2 diabetes mellitus.Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease.Oxidized proteins: intracellular distribution and recognition by the proteasome.The proteasome and its role in nuclear protein maintenance.The proteasomal system.The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome.Happily (n)ever after: Aging in the context of oxidative stress, proteostasis loss and cellular senescence.Structure of the proteasome.The proteasome and the degradation of oxidized proteins: Part I-structure of proteasomes.Pathophysiological importance of aggregated damaged proteins.The proteasome and the degradation of oxidized proteins: Part II - protein oxidation and proteasomal degradation.Tau protein degradation is catalyzed by the ATP/ubiquitin-independent 20S proteasome under normal cell conditions.Metabolism-induced oxidative stress is a mediator of glucose toxicity in HT22 neuronal cells.Nitrotyrosine and protein carbonyls are equally distributed in HT22 cells after nitrosative stress.Intracellular distribution of oxidized proteins and proteasome in HT22 cells during oxidative stress.Distribution of oxidized and HNE-modified proteins in U87 cells.Protein oxidation and degradation during postmitotic senescence.Proteostasis, oxidative stress and aging.Mitochondrial contribution to lipofuscin formation.Macroautophagy is impaired in old murine brain tissue as well as in senescent human fibroblasts.An experimental setup for the measurement of nonthermal effects during water-filtered infrared A-irradiation of mammalian cell cultures.Oxidative stress related changes in the brain of hypercholesterolemic rabbits.Actual Isothermal Effects of Water-Filtered Infrared A-Irradiation."Cyt/Nuc", a customizable and documenting ImageJ macro for evaluation of protein distributions between cytosol and nucleus.SIPS as a model to study age-related changes in proteolysis and aggregate formation.Hyperammonemia causes protein oxidation and enhanced proteasomal activity in response to mitochondria-mediated oxidative stress in rat primary astrocytes.Impact of magnetic labeling on human and mouse stem cells and their long-term magnetic resonance tracking in a rat model of Parkinson disease.Tocopherol-mediated modulation of age-related changes in microglial cells: turnover of extracellular oxidized protein material.Age-related oxidative changes in pancreatic islets are predominantly located in the vascular system.Reduced autophagy leads to an impaired ferritin turnover in senescent fibroblasts.Identification of an unstable 4-hydroxynoneal modification on the 20S proteasome subunit α7 by recombinant antibody technology.Protein aggregates and proteostasis in aging: Amylin and β-cell function.Lipofuscin-bound iron is a major intracellular source of oxidants: role in senescent cells.Carbonylation of the cytoskeletal protein actin leads to aggregate formation.Degradation of glycated bovine serum albumin in microglial cells.
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description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
ricercatore
@it
հետազոտող
@hy
name
Tobias Jung
@ast
Tobias Jung
@en
Tobias Jung
@es
Tobias Jung
@nl
Tobias Jung
@sl
type
label
Tobias Jung
@ast
Tobias Jung
@en
Tobias Jung
@es
Tobias Jung
@nl
Tobias Jung
@sl
prefLabel
Tobias Jung
@ast
Tobias Jung
@en
Tobias Jung
@es
Tobias Jung
@nl
Tobias Jung
@sl
P106
P21
P214
8150468182104171590
P31
P496
0000-0002-9159-8444