about
Lipofuscin 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".Protein oxidation in aging and the removal of oxidized proteins.Advanced glycation end products and oxidative stress in type 2 diabetes mellitus.Lipofuscin: formation, effects and role of macroautophagyHappily (n)ever after: Aging in the context of oxidative stress, proteostasis loss and cellular senescence.Oxidative protein damage and the proteasome.Pathophysiological importance of aggregated damaged proteins.The proteasome and the degradation of oxidized proteins: Part II - protein oxidation and proteasomal degradation.Metabolic Syndrome, Redox State, and the Proteasomal System.Insulin-degrading enzyme: new therapeutic target for diabetes and Alzheimer's disease?Advanced-glycation-end-product-induced formation of immunoproteasomes: involvement of RAGE and Jak2/STAT1.Quantification of age-related changes of α-tocopherol in lysosomal membranes in murine tissues and human fibroblasts.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.Cathepsin D is one of the major enzymes involved in intracellular degradation of AGE-modified proteins.An experimental setup for the measurement of nonthermal effects during water-filtered infrared A-irradiation of mammalian cell cultures.Diet-derived advanced glycation end products or lipofuscin disrupts proteostasis and reduces life span in Drosophila melanogaster.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.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.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.Lipofuscin inhibits the proteasome by binding to surface motifsAge-related differences in oxidative protein-damage in young and senescent fibroblastsEndogenous advanced glycation end products in pancreatic islets after short-term carbohydrate intervention in obese, diabetes-prone miceSugar-derived AGEs accelerate pharyngeal pumping rate and increase the lifespan of Caenorhabditis elegansThe "MYOCYTER" - Convert cellular and cardiac contractions into numbers with ImageJLipofuscin-dependent stimulation of microglial cellsRole of Advanced Glycation End Products in Carcinogenesis and their Therapeutic ImplicationsProteostasis Failure in Neurodegenerative Diseases: Focus on Oxidative StressCharacterization of Black Pigmenturia in a Cat with Apocrine Gland Cystadenocarcinoma
P50
Q28118094-C65C9CFF-FA53-45CF-8529-A70AF68FF4C9Q30363025-49058812-7F64-49DB-9BC5-E8F205B9B336Q30367729-18B88BA8-FFC8-4007-A1CB-9B3F9BCE0D53Q30426117-854F57FA-A97A-44DB-9AD5-033B4F9C9378Q35255473-612DDA39-B47B-4219-A092-72058413D8DAQ37133485-71CA13DE-F69E-497D-AD71-E43B375234CBQ37581663-D65EEE91-36CB-4E5B-838D-88512ACE2219Q37765860-146BBB2C-27CF-4529-8BD4-8FF83D60B72EQ38196251-9DB6181F-6F5C-45E0-B562-0A4DAE10F358Q38280561-5E2E188E-6049-4DDC-81B2-D1ACD112A379Q38842149-A9063CC6-9EFF-48E3-9B9B-7CA3AC64E471Q38869928-1F980838-90A6-4A73-8CF2-BF84CF60A15DQ39297671-E05C972E-3C3E-4ABA-99CA-42381E165163Q39837797-0C17C275-949A-4A21-B17C-6B08BADC9738Q41189449-2F2DA51D-DF40-4B24-8B98-D4027A99F07EQ42042230-5C515201-C2E3-45B1-9FD0-8A4C7EDE242CQ42372625-AADEFC4B-622B-4463-A31B-67B73D91152BQ43013056-EF1FAE12-C192-4A98-9325-B778673C6912Q44506506-D4FAE5F1-DED4-4394-89C1-07B853DA0F69Q45991660-2F5D5D36-7155-4A08-8A59-269758C85CB5Q46768781-AD1829D1-41EE-4388-B77D-93A53178E16DQ47214493-52922665-41C3-420E-80CE-0C78BCB9B444Q48013447-38341817-C2A2-456E-BA4D-ED40B0CD8BB1Q49210690-E999C9D6-57E8-42F9-8C6B-A58872941B78Q51358844-49656656-958E-4DBB-AA69-246897A7494CQ51759297-4F882883-369A-4CCD-BF01-721909EA2A49Q52701159-D374457A-710B-4BE1-A49A-0776DB32423BQ59240639-0B29254A-A968-4F76-B5BC-344FFA8CE36DQ60705157-27FC350D-A4E0-429E-9396-34BC030A776CQ64108807-EB0E8F12-12AB-414B-B066-4FEE502301A6Q90080661-16E5DD97-58D8-4ED1-AF8C-FCB35CAFAC0DQ90885024-D8787CE4-3AC0-4452-AE87-A3A852408BB3Q91261550-3546929E-ED05-4FE0-AAB3-6B82EB8E298DQ91301958-C5028FCC-E201-4D6C-8906-E99FED9B422BQ92063917-D7578F9A-59D2-4614-80B2-43134790C0E7Q94487759-7AB2FA7E-EB75-4629-97D9-06FB10F81205
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Annika Höhn
@ast
Annika Höhn
@en
Annika Höhn
@es
Annika Höhn
@nl
Annika Höhn
@sl
type
label
Annika Höhn
@ast
Annika Höhn
@en
Annika Höhn
@es
Annika Höhn
@nl
Annika Höhn
@sl
prefLabel
Annika Höhn
@ast
Annika Höhn
@en
Annika Höhn
@es
Annika Höhn
@nl
Annika Höhn
@sl
P106
P21
P31
P496
0000-0003-1306-2668