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Person

Benedikt Goretzki (1989-)

Chemiker

Name	Benedikt Goretzki
Zeit	1989- (Lebensdaten)
Ort	Deutschland
Akademischer Grad bzw. Titel	Dr. rer. nat. (Dissertation am Fachbereich Chemie, Pharmazie, Geographie und Geowissenschaften der Johannes Gutenberg-Universität Mainz und am Max Planck Graduate Center) (2020)
Beruf	Chemiker (charakteristischer Beruf)
Variante	B. Goretzki
Beziehung	Friedrich-Schiller-Universität Jena. Institut für Organische Chemie und Makromolekulare Chemie
Datensatztyp	Person
GND-Nummer	122623951X
Datensatz-ID	122623951X
Beteiligt an alle anzeigen Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding. Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels Crosstalk between regulatory elements in the disordered TRPV4 N-terminus modulates lipid-dependent channel activity Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels Multiubiquitination of TRPV4 reduces channel activity independent of surface localization Interactions of the ion channel TRPV4 with regulatory lipids and proteins - An (un)structural study NMR assignments of a dynamically perturbed and dimerization inhibited N-terminal domain variant of a spider silk protein from E. australis

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Katalog der Deutschen Nationalbibliothek

Benedikt Goretzki (1989-)

Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity

Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity

Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding

Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding

Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding.

Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels

Crosstalk between regulatory elements in the disordered TRPV4 N-terminus modulates lipid-dependent channel activity

Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels

Multiubiquitination of TRPV4 reduces channel activity independent of surface localization

Interactions of the ion channel TRPV4 with regulatory lipids and proteins - An (un)structural study

NMR assignments of a dynamically perturbed and dimerization inhibited N-terminal domain variant of a spider silk protein from E. australis