Marcus Groettrup

The UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10.

Opposite fate of endocytosed CCR7 and its ligands: recycling versus degradation.

Prostaglandin E2 is a key factor for monocyte-derived dendritic cell maturation: enhanced T cell stimulatory capacity despite IDO.

A novel cytosolic class I antigen-processing pathway for endoplasmic-reticulum-targeted proteins.

Distinct motifs in the chemokine receptor CCR7 regulate signal transduction, receptor trafficking and chemotaxis.

Identification of homozygous transgenic mice by genomic real-time PCR.

Quantitative analysis of gene expression relative to 18S rRNA in carcinoma samples using the LightCycler instrument and a SYBR GreenI-based assay: determining FAT10 mRNA levels in hepatocellular carcinoma.

Prostaglandin E(2) enhances T-cell proliferation by inducing the costimulatory molecules OX40L, CD70, and 4-1BBL on dendritic cells.

Identification of the molecular composition of the 20S proteasome of mouse intestine by high-resolution mass spectrometric proteome analysis.

Substantial reduction of naïve and regulatory T cells following traumatic stress.

USE1 is a bispecific conjugating enzyme for ubiquitin and FAT10, which FAT10ylates itself in cis.

Cross-talk between TCR and CCR7 signaling sets a temporal threshold for enhanced T lymphocyte migration.

Immunoproteasome-specific inhibitors and their application.

Coencapsulation of tumor lysate and CpG-ODN in PLGA-microspheres enables successful immunotherapy of prostate carcinoma in TRAMP mice.

Ubiquitylation of the chemokine receptor CCR7 enables efficient receptor recycling and cell migration.

Prostaglandin E2 inhibits IL-23 and IL-12 production by human monocytes through down-regulation of their common p40 subunit.

Immunoproteasome subunit LMP7 deficiency and inhibition suppresses Th1 and Th17 but enhances regulatory T cell differentiation.

The immunoproteasome in antigen processing and other immunological functions.

Using protease inhibitors in antigen presentation assays.

FAT10ylation as a signal for proteasomal degradation.

Posttraumatic stress disorder is associated with an enhanced spontaneous production of pro-inflammatory cytokines by peripheral blood mononuclear cells.

Immuno- and constitutive proteasomes do not differ in their abilities to degrade ubiquitinated proteins.

The unique functions of tissue-specific proteasomes.

Inhibition of the immunoproteasome ameliorates experimental autoimmune encephalomyelitis.

Investigations into the auto-FAT10ylation of the bispecific E2 conjugating enzyme UBA6-specific E2 enzyme 1.

The effect of trauma-focused therapy on the altered T cell distribution in individuals with PTSD: evidence from a randomized controlled trial.

Subunit specific inhibitors of proteasomes and their potential for immunomodulation.

The ubiquitin-like modifier FAT10 decorates autophagy-targeted Salmonella and contributes to Salmonella resistance in mice.

No evidence for immunoproteasomes in chicken lymphoid organs and activated lymphocytes.

Conjugation of the ubiquitin activating enzyme UBE1 with the ubiquitin-like modifier FAT10 targets it for proteasomal degradation.

Analgesia in mice with experimental meningitis reduces pain without altering immune parameters.

The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense.

The ubiquitin-specific protease USP8 is critical for the development and homeostasis of T cells.

Cytotoxic T cell vaccination with PLGA microspheres interferes with influenza A virus replication in the lung and suppresses the infectious disease.

The Ubiquitin-like Modifier FAT10 Is Selectively Expressed in Medullary Thymic Epithelial Cells and Modifies T Cell Selection.

The immunoproteasome: a novel drug target for autoimmune diseases.

Inhibition and deficiency of the immunoproteasome subunit LMP7 attenuates LCMV-induced meningitis.

Chaperone BAG6 is dispensable for MHC class I antigen processing and presentation.

The STEAP1(262-270) peptide encapsulated into PLGA microspheres elicits strong cytotoxic T cell immunity in HLA-A*0201 transgenic mice--A new approach to immunotherapy against prostate carcinoma.

Inhibiting the immunoproteasome exacerbates the pathogenesis of systemic Candida albicans infection in mice.

A cascading activity-based probe sequentially targets E1-E2-E3 ubiquitin enzymes.

The ubiquitin-like modifier FAT10 in cancer development.

Analyzing structure-function relationships of artificial and cancer-associated PARP1 variants by reconstituting TALEN-generated HeLa PARP1 knock-out cells.

Newly translated proteins are substrates for ubiquitin, ISG15, and FAT10.

Immunoproteasome subunit deficiency has no influence on the canonical pathway of NF-κB activation.

Chronic stress suppresses anti-tumor T responses and tumor regression following cancer immunotherapy in a mouse model of melanoma.

No prolongation of skin allograft survival by immunoproteasome inhibition in mice.

Inhibition and deficiency of the immunoproteasome subunit LMP7 suppress the development and progression of colorectal carcinoma in mice.

Amelioration of autoimmunity with an inhibitor selectively targeting all active centres of the immunoproteasome.

The immunoproteasome subunit LMP7 is required in the murine thymus for filling up a hole in the T cell repertoire.

The 20S immunoproteasome and constitutive proteasome bind with the same affinity to PA28αβ and equally degrade FAT10.

Immunoproteasome inhibition prevents chronic antibody-mediated allograft rejection in renal transplantation.

The expression profile of the ubiquitin-like modifier FAT10 in immune cells suggests cell type-specific functions.

Defective immuno- and thymoproteasome assembly causes severe immunodeficiency.

The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation.

On the role of the immunoproteasome in transplant rejection.

Co-inhibition of immunoproteasome subunits LMP2 and LMP7 is required to block autoimmunity.

Author Correction: The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation.

Prevention of neuronal apoptosis by astrocytes through thiol-mediated stress response modulation and accelerated recovery from proteotoxic stress.

Immunoproteasome Inhibition Impairs T and B Cell Activation by Restraining ERK Signaling and Proteostasis.

Immunoproteasome inhibition induces plasma cell apoptosis and preserves kidney allografts by activating the unfolded protein response and suppressing plasma cell survival factors.

The ubiquitin-like modifier FAT10 stimulates the activity of deubiquitylating enzyme OTUB1.

The ubiquitin-like modifier FAT10 is required for normal IFN-γ production by activated CD8 T cells.

Analysis of modification and proteolytic targeting by the ubiquitin-like modifier FAT10.

Harnessing Dendritic Cells for Poly (D,L-lactide--glycolide) Microspheres (PLGA MS)-Mediated Anti-tumor Therapy.

Testing the Impact of Protease Inhibitors in Antigen Presentation Assays.

Immunoproteasome Inhibition Selectively Kills Human CD14 Monocytes and as a Result Dampens IL-23 Secretion.

The ubiquitin-like modifier FAT10 interferes with SUMO activation.

Competitive Metabolite Profiling of Natural Products Reveals Subunit Specific Inhibitors of the 20S Proteasome.

FAT10 localises in dendritic cell aggresome-like induced structures and contributes to their disassembly.

Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10.

Evidence for an involvement of the ubiquitin-like modifier ISG15 in MHC class I antigen presentation.

The ubiquitin-like modifier FAT10 - much more than a proteasome-targeting signal.

The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation.

Recent insights how combined inhibition of immuno/proteasome subunits enables therapeutic efficacy.

Parkin is an E3 ligase for the ubiquitin-like modifier FAT10, which inhibits Parkin activation and mitophagy.

Immunoproteasome Upregulation Is Not Required to Control Protein Homeostasis during Viral Infection.

Silencing of the proteasome and oxidative stress impair endoplasmic reticulum targeting and signal cleavage of a prostate carcinoma antigen.

PLGA-particle vaccine carrying TLR3/RIG-I ligand Riboxxim synergizes with immune checkpoint blockade for effective anti-cancer immunotherapy.

On the Role of the Immunoproteasome in Protein Homeostasis.