Farnusch Kaschani

Head of Analytics Core Facility Essen

Universität Duisburg-Essen

Germany

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Farnusch Kaschani is the Head of the Analytics Core Facility at the University of Duisburg-Essen, Germany. Her research focuses on protein analysis and modification, as evidenced by her recent publications examining topics such as protein polyubiquitination, chaperone complexes, and the interaction of bacterial pathogens with plant glycobiology. She contributes significantly to the understanding of protein dynamics and their implications in various biological contexts.

Articles (19)

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2025

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2022

Collaborators (17)

Lana Buzuk

PhD Student in the lab of Prof Dr Doris Hellerschmied

Universität Duisburg-Essen

GERMANY

Farnusch Kaschani

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Articles (19)

Conformational plasticity of a BiP–GRP94 chaperone complex

Bacterial pathogen deploys the iminosugar glycosyrin to manipulate plant glycobiology

The Actin‐Binding Prolyl‐Isomerase Par17 Sustains Its Substrate Selectivity by Interdomain Allostery

Sulphostin-inspired N-phosphonopiperidones as selective covalent DPP8 and DPP9 inhibitors

Intraoperative Biologization of β-TCP and PCL-TCP by Autologous Proteins

Small Molecule‐Induced Alterations of Protein Polyubiquitination Revealed by Mass‐Spectrometric Ubiquitome Analysis

Small Molecule‐Induced Alterations of Protein Polyubiquitination Revealed by Mass‐Spectrometric Ubiquitome Analysis

The proteome of Nicotiana benthamiana is shaped by extensive protein processing

High resolution analysis of proteolytic substrate processing

Differences in the Synovial Fluid Proteome of Septic and Aseptic Implant Failure

TopBP1 utilises a bipartite GINS binding mode to support genome replication

Subtilase SBT5.2 inactivates flagellin immunogenicity in the plant apoplast

Extracellular plant subtilases dampen cold-shock peptide elicitor levels

Taspase1 Facilitates Topoisomerase IIβ-Mediated DNA Double-Strand Breaks Driving Estrogen-Induced Transcription

Activity‐based proteomics uncovers suppressed hydrolases and a neo‐functionalised antibacterial enzyme at the plant–pathogen interface

The UBX domain in UBXD1 organizes ubiquitin binding at the C-terminus of the VCP/p97 AAA-ATPase.

Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate

Author Correction: Identification of fungal lignocellulose-degrading biocatalysts secreted by Phanerochaete chrysosporium via activity-based protein profiling

Identification of fungal lignocellulose-degrading biocatalysts secreted by Phanerochaete chrysosporium via activity-based protein profiling

Collaborators (17)

Lana Buzuk

Chris Schofield

Christos Gatsogiannis

Sabrina Ninck

Christopher Schofield

Doris Hellerschmied

Matthew Day

Bettina Siebers

Renier A L van der Hoorn

Peter Bayer

Stephan Barcikowski

Hemmo Meyer

Atsushi Kato

Shirley Knauer

David Podlesainski

Pierre Buscaill

Michael Ehrmann

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