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» Authors » Reinhild Kappelhoff

Reinhild Kappelhoff

Explore the profile of Reinhild Kappelhoff including associated specialties, affiliations and a list of published articles. Areas
Snapshot
Articles 25
Citations 694
Followers 0
Related Specialties
Biochemistry
Molecular Biology
Biology
Top 10 Co-Authors
Christopher M Overall
Georgina S Butler
Ulrich Auf dem Keller
Antoine Dufour
Caroline L Bellac
Amanda E Starr
Philipp F Lange
Ulrich Eckhard
Oliver Schilling
Jennifer H Cox
Published In
Cell Rep
J Biol Chem
Curr Protoc Protein Sci
Nat Commun
J Virol
Affiliations
Soon will be listed here.
Recent Articles
1.
SARS-CoV-2 3CL (main protease) regulates caspase activation of gasdermin-D/E pores leading to secretion and extracellular activity of 3CL
Grin P, Baid K, de Jesus H, Kozarac N, Bell P, Jiang S, et al.
Cell Rep . 2024 Dec; 43(12):115080. PMID: 39673710
SARS-CoV-2 3C-like protease (3CL or M) cleaves the SARS-CoV-2 polyprotein and >300 intracellular host proteins to enhance viral replication. By lytic cell death following gasdermin (GSDM) pore formation in cell...
2.
Optimization of quenched fluorescent peptide substrates of SARS-CoV-2 3CL main protease (Mpro) from proteomic identification of P6-P6' active site specificity
Cesar Ramos de Jesus H, Solis N, Machado Y, Pablos I, Bell P, Kappelhoff R, et al.
J Virol . 2024 May; 98(6):e0004924. PMID: 38742901
SARS-CoV-2 3C-like main protease (3CL) is essential for protein excision from the viral polyprotein. 3CL inhibitor drug development to block SARS-CoV-2 replication focuses on the catalytic non-prime (P) side for...
3.
Mechanistic insights into COVID-19 by global analysis of the SARS-CoV-2 3CL substrate degradome
Pablos I, Machado Y, de Jesus H, Mohamud Y, Kappelhoff R, Lindskog C, et al.
Cell Rep . 2021 Oct; 37(4):109892. PMID: 34672947
The main viral protease (3CL) is indispensable for SARS-CoV-2 replication. We delineate the human protein substrate landscape of 3CL by TAILS substrate-targeted N-terminomics. We identify more than 100 substrates in...
4.
Persistent Salmonella enterica Serovar Typhimurium Infection Induces Protease Expression During Intestinal Fibrosis
Ehrhardt K, Steck N, Kappelhoff R, Stein S, Rieder F, Gordon I, et al.
Inflamm Bowel Dis . 2019 May; 25(10):1629-1643. PMID: 31066456
Background: Intestinal fibrosis is a common and serious complication of Crohn's disease characterized by the accumulation of fibroblasts, deposition of extracellular matrix, and formation of scar tissue. Although many factors...
5.
Proteases and their inhibitors as prognostic factors for high-grade serous ovarian cancer
Trudel D, Avarvarei L, Orain M, Turcotte S, Plante M, Gregoire J, et al.
Pathol Res Pract . 2019 Apr; 215(6):152369. PMID: 30987833
Ovarian carcinoma is one of the most lethal malignancies, but only very few prognostic biomarkers are known. The degradome, comprising proteases, protease non-proteolytic homologues and inhibitors, have been involved in...
6.
C-terminal truncation of IFN-γ inhibits proinflammatory macrophage responses and is deficient in autoimmune disease
Dufour A, Bellac C, Eckhard U, Solis N, Klein T, Kappelhoff R, et al.
Nat Commun . 2018 Jun; 9(1):2416. PMID: 29925830
Controlled macrophage differentiation and activation in the initiation and resolution of inflammation is crucial for averting progression to chronic inflammatory and autoimmune diseases. Here we show a negative feedback mechanism...
7.
Overview of transcriptomic analysis of all human proteases, non-proteolytic homologs and inhibitors: Organ, tissue and ovarian cancer cell line expression profiling of the human protease degradome by the CLIP-CHIP™ DNA microarray
Kappelhoff R, Puente X, Wilson C, Seth A, Lopez-Otin C, Overall C
Biochim Biophys Acta Mol Cell Res . 2017 Aug; 1864(11 Pt B):2210-2219. PMID: 28797648
The protease degradome is defined as the complete repertoire of proteases and inhibitors, and their nonfunctional homologs present in a cell, tissue or organism at any given time. We review...
8.
Novel grooved substrata stimulate macrophage fusion, CCL2 and MMP-9 secretion
Moon H, Cremmel C, Kulpa A, Jaeger N, Kappelhoff R, Overall C, et al.
J Biomed Mater Res A . 2016 Apr; 104(9):2243-54. PMID: 27102570
Rough surface topographies on implants attract macrophages but the influence of topography on macrophage fusion to produce multinucleated giant cells (MGC) and foreign body giant cells (FBGC) is unclear. Two...
9.
Active site specificity profiling datasets of matrix metalloproteinases (MMPs) 1, 2, 3, 7, 8, 9, 12, 13 and 14
Eckhard U, Huesgen P, Schilling O, Bellac C, Butler G, Cox J, et al.
Data Brief . 2016 Mar; 7:299-310. PMID: 26981551
The data described provide a comprehensive resource for the family-wide active site specificity portrayal of the human matrix metalloproteinase family. We used the high-throughput proteomic technique PICS (Proteomic Identification of...
10.
Active site specificity profiling of the matrix metalloproteinase family: Proteomic identification of 4300 cleavage sites by nine MMPs explored with structural and synthetic peptide cleavage analyses
Eckhard U, Huesgen P, Schilling O, Bellac C, Butler G, Cox J, et al.
Matrix Biol . 2015 Sep; 49:37-60. PMID: 26407638
Secreted and membrane tethered matrix metalloproteinases (MMPs) are key homeostatic proteases regulating the extracellular signaling and structural matrix environment of cells and tissues. For drug targeting of proteases, selectivity for...