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Frank Stein

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Name	Frank Stein
Ort	Malchin (Geburtsort) Deutschland
Geschlecht	männlich
Akademischer Grad bzw. Titel	Dr. (an der Naturwissenschaftlich-Mathematischen Gesamtfakultät der Ruprecht-Karls-Universität Heidelberg) (2014)
Beruf	Informatiker (charakteristischer Beruf) Chemiker
Beziehung	European Molecular Biology Laboratory Biowissenschaften (Studienfach)
Quelle	https://www.embl.de/services/core_facilities/members/index.php?s_personId=CP-60012409 (Homepage)
Datensatztyp	Person
GND-Nummer	1076138101
Datensatz-ID	1076138101
Beteiligt an alle anzeigen An atlas of the aging mouse proteome reveals the features of age-related post-transcriptional dysregulation Systematic analysis of RNA-binding proteins identifies targetable therapeutic vulnerabilities in osteosarcoma Increased levels of mitochondrial import factor Mia40 prevent the aggregation of polyQ proteins in the cytosol SARS‐CoV‐2 infection remodels the host protein thermal stability landscape Increased levels of mitochondrial import factor Mia40 prevent the aggregation of polyQ proteins in the cytosol SARS-CoV-2 infection remodels the host protein thermal stability landscape The functional proteome landscape of Escherichia coli Aggregation and disaggregation features of the human proteome Thermal proteome profiling for interrogating protein interactions Effect of Sec61 interaction with Mpd1 on endoplasmic reticulum-associated degradation. Discovery of RNA-binding proteins and characterization of their dynamic responses by enhanced RNA interactome capture Thermal proteome profiling in bacteria: probing protein state in vivo Lipid and image analysis tools for studying lipid-protein binding dynamics in living cells

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Frank Stein

An atlas of the aging mouse proteome reveals the features of age-related post-transcriptional dysregulation

Systematic analysis of RNA-binding proteins identifies targetable therapeutic vulnerabilities in osteosarcoma

Increased levels of mitochondrial import factor Mia40 prevent the aggregation of polyQ proteins in the cytosol

SARS‐CoV‐2 infection remodels the host protein thermal stability landscape

Increased levels of mitochondrial import factor Mia40 prevent the aggregation of polyQ proteins in the cytosol

SARS-CoV-2 infection remodels the host protein thermal stability landscape

The functional proteome landscape of Escherichia coli

Aggregation and disaggregation features of the human proteome

Thermal proteome profiling for interrogating protein interactions

Effect of Sec61 interaction with Mpd1 on endoplasmic reticulum-associated degradation.

Discovery of RNA-binding proteins and characterization of their dynamic responses by enhanced RNA interactome capture

Thermal proteome profiling in bacteria: probing protein state in vivo

Lipid and image analysis tools for studying lipid-protein binding dynamics in living cells