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Axel Knebel

Researcher at University of Dundee

Publications -  78
Citations -  6620

Axel Knebel is an academic researcher from University of Dundee. The author has contributed to research in topics: Ubiquitin & Ubiquitin ligase. The author has an hindex of 39, co-authored 72 publications receiving 5524 citations.

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Journal ArticleDOI

Biophysical Studies on Interactions and Assembly of Full-size E3 Ubiquitin Ligase SUPPRESSOR OF CYTOKINE SIGNALING 2 (SOCS2)-ELONGIN BC-CULLIN 5-RING BOX PROTEIN 2 (RBX2)

TL;DR: It is demonstrated that the components of CRL5SOCS2 can be specifically pulled from K562 human cell lysates using beads decorated with phosphorylated growth hormone receptor peptides, and a structural model for full-size neddylated and unneddylated CRL3-Rbx2 complexes is supported by traveling wave ion mobility mass spectrometry data.
Journal ArticleDOI

Identification of a phosphorylation site on skeletal muscle myosin light chain kinase that becomes phosphorylated during muscle contraction

TL;DR: Results indicate that contraction-induced phosphorylation is probably catalyzed by MLCK and not MAPKAP-K2, and that an arginine located three residues N-terminal to the site of phosphorylated was thought to be critical for the specificity of MAPK AP-K1.
Journal ArticleDOI

Radiation-induced signal transduction. Mechanisms and consequences.

TL;DR: Although accurate determinations of low-dose inductions have not been achieved for technical reasons, the dose-response curves of induced signal transduction likely show threshold characteristics, in contrast to the direct consequences of DNA damage.
Book ChapterDOI

Radiation-induced signal transduction.

TL;DR: Some of the methodology that has been employed to study radiation-induced signaling and that led to the recognition of radiation- induced pathways and of some of the primary target molecules are addressed.
Journal ArticleDOI

Orthogonal Thiol Functionalization at a Single Atomic Center for Profiling Transthiolation Activity of E1 Activating Enzymes

TL;DR: This work characterize biocompatible chemistry that enables sequential functionalization of cysteines within proteins at a single atomic center and develops a new class of activity-based probe that profiles transthiolation activity of human E1 activating enzymes.