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Mark S. Hipp

Biochemiker

Name	Mark S. Hipp
Place	Deutschland
Gender	männlich
Academic degree	Dr.
Profession	Biochemiker (characteristic profession)
Variant	Mark Hipp
Related	Universitair Medisch Centrum Groningen (2019-) Carl von Ossietzky Universität Oldenburg (2020-)
Record type	Person
GND-Identifier	123624561X
Record ID	123624561X
Involved in show all Analysis of the chaperone-mediated remodeling of the amyloid protein Huntingtin : Analyse des durch Chaperone vermittelten Umbaus des Amyloidproteins Huntingtin Gel‐like inclusions of C‐terminal fragments of TDP‐43 sequester stalled proteasomes in neurons Fluc‐EGFP reporter mice reveal differential alterations of neuronal proteostasis in aging and disease Sis1 potentiates the stress response to protein aggregation and elevated temperature An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space Cell‐to‐cell transmission of C9orf72 poly‐(Gly‐Ala) triggers key features of ALS/FTD The proteostasis network and its decline in ageing A protein quality control pathway regulated by linear ubiquitination High capacity of the endoplasmic reticulum to prevent secretion and aggregation of amyloidogenic proteins Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments

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Mark S. Hipp

Analysis of the chaperone-mediated remodeling of the amyloid protein Huntingtin : Analyse des durch Chaperone vermittelten Umbaus des Amyloidproteins Huntingtin

Gel‐like inclusions of C‐terminal fragments of TDP‐43 sequester stalled proteasomes in neurons

Fluc‐EGFP reporter mice reveal differential alterations of neuronal proteostasis in aging and disease

Sis1 potentiates the stress response to protein aggregation and elevated temperature

An inventory of interactors of the human HSP60/HSP10 chaperonin in the mitochondrial matrix space

Cell‐to‐cell transmission of C9orf72 poly‐(Gly‐Ala) triggers key features of ALS/FTD

The proteostasis network and its decline in ageing

A protein quality control pathway regulated by linear ubiquitination

High capacity of the endoplasmic reticulum to prevent secretion and aggregation of amyloidogenic proteins

Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments