C. H. Ihling

Twisting Urea- to Imide-Based Mass Spectrometry-Cleavable Cross-Linkers Enables Affinity Tagging

This paper introduces DSSI, a new class of MS-cleavable cross-linkers with affinity tags, and validates its use in structural biology.

Structural Assessment of the Full-Length Wild-Type Tumor Suppressor Protein p53 by Mass Spectrometry-Guided Computational Modeling

This study uses mass spectrometry and computational modeling to assess the structure of full-length wild-type p53, revealing compaction of the C-terminal region and supporting a model of DNA binding.

Structural surfaceomics reveals an AML-specific conformation of Integrin-β2 as a CAR-T therapy target

The paper identifies an AML-specific conformation of Integrin-β2 using structural surfaceomics and demonstrates its targeting by CAR-T cells.

First direct observation of 'elongated' conformational states in α-synuclein upon liquid-liquid phase separation

This study observes elongated conformational states of α-synuclein during liquid-liquid phase separation using XL-MS and COMPASS, providing insights into early stages of Parkinson's Disease.

Cross-linking/Mass Spectrometry Combined with Ion Mobility on a timsTOF Pro Instrument for Structural Proteomics

This paper demonstrates the use of XL-MS combined with ion mobility on a timsTOF Pro instrument to study protein conformations and interactions, identifying numerous cross-links and interactions in different protein systems.

First 3D-Structural Data of Full-length Rod-Outer-Segment Guanylyl Cyclase 1 in Bovine Retina by Cross-linking/Mass Spectrometry

The paper presents the first 3D-structural analysis of active, full-length ROS-GC1 in bovine retina using XL-MS and computational modeling, revealing a novel domain organization and dimeric architecture.

Structural Analysis of 70S Ribosomes by Cross-Linking/Mass Spectrometry Reveals Conformational Plasticity

This study uses XL-MS to analyze E. coli ribosome structures, revealing conformational plasticity and remodeling 2,057 residues with high accuracy.

Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies

The paper investigates how flexible intrinsically disordered regions in AUX/IAA proteins modulate auxin receptor assemblies by positioning AUX/IAAs on TIR1 for ubiquitylation.