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Reagents for your SARS-CoV-2 research
Reagents for your SARS-CoV-2 research The SARS-CoV-2 coronavirus encodes a papain-like cysteine protease PLpro (NSP3) that cleaves the viral polyprotein, removes ubiquitin-like ISG15 protein modifications and (with lower activity) Lys48-linked polyubiquitin chains. As PLPro is essential for SARS-CoV-2 replication, it represents a promising target for...
In memoriam: Professor Huib Ovaa
On the 19th of May 2020, our co-founder and dear friend Professor Dr. Huib Ovaa passed away from prostate cancer at the age of 46 years. In the past year, Huib has undergone a...
Public-private partnership grant by Health-Holland: New drug therapies by a better understanding of ubiquitin metalloprotease activity Tools to study ubiquitin metalloprotease activity.
17 December 2019 Public-private partnership grant awarded by Health-Holland We are happy to announce that UbiQ and Prof Titia Sixma (Netherlands Cancer Institute, Netherlands) were recently awarded a public-private partnership...
Antibody development by using monoubiquitinated peptides as antigens.
24 April 2019 Antibody development by using monoubiquitinated peptides as antigens Conserved from yeast to human, the histone methyltransferase Dot1 methylates lysine 79 of histone H3 (H3K79) on the nucleosome core. This methylation affects gene expression and DNA damage...
A collaborative effort between scientists at UbiQ, Genentech, Boston Biochem (Bio-Techne) and Stanford University.
28 January 2019 Bio-orthogonally tagged activity-based probes forproteomics of deubiquitinating enzymes A recent paper in Nature Communications describes a collaborative effort between scientists at UbiQ, Genentech, Boston Biochem (Bio-Techne) and Stanford University (1). Here a reactive-site-centric chemoproteomics protocol is presented...
Launch of an activity-based probe for the deubiquitinating enzyme OTULIN.
23 October, 2017 UbiQ-121 (Biotin-Ahx-Ub(1-75)-Dha-Ub) an activity-based probe for the deubiquitinating enzyme OTULIN Hereby we present UbiQ-121 (1, 2) as an activity-based probe for OTULIN, a deubiquitinating enzyme that is specific for Met1 linked ubiquitin...
UbiQ secures 2.7 mioEUR EUROSTARS grant to tackle SUMOylation.
UbiQ secures 2.7 mioEUR EUROSTARS grant to tackle SUMOylation. Amsterdam, The Netherlands, September 12th, 2017: UbiQ, a biotech company focused on the development and commercialization of research tools and small molecule drugs targeting the ubiquitin...
where to meet us
EMBO conference on Ubiquitin 2022
September 9 - 13, 2022 Cavtat, Croatia Ubiquitin and ubiquitin-like proteins in health and disease. Contact: Alfred Nijkerk (CEO)
GRK2243 Symposium, University of Würzburg (cancelled by COVID19)
May 4 - 6, 2020 Würzburg, Germany Understanding Ubiquitylation: From Molecular Mechanisms to Disease Contact: Farid El Oualid (CSO) More info conference: https://www.ubiquitin-wuerzburg-2020.de/
EMBO conference on Ubiquitin 2019
September 13 - 17, 2019 Cavtat, Croatia The ubiquitin system: Biology, mechanisms and roles in disease. Contact: Alfred Nijkerk (CEO)
BIO-Europe 2018
UbiQ will attend BIO-Europe 2018. November 5 - 7, 2018 Amsterdam, Denmark Contact: Alfred Nijkerk BIO-Europe: https://ebdgroup.knect365.com/bioeurope/
BIO-Europe Spring 2018
UbiQ will attend BIO-Europe Spring. March 12 - 14, 2018 Amsterdam, the Netherlands Contact: Alfred Nijkerk BIO-Europe: https://ebdgroup.knect365.com/bioeurope-spring/
Bio-Europe 2017
UbiQ will attend BIO-Europe. November 6 - 8, 2017 Berlin, Germany Contact: Alfred Nijkerk BIO-Europe: https://ebdgroup.knect365.com/bioeurope/
EMBO conference on Ubiquitin 2017
September 15 - 19, 2017 Cavtat, Croatia Ubiquitin and SUMO: From molecular mechanisms to system-wide responses Contact: Boris Rodenko (VP Translational Drug Discovery) / Alfred Nijkerk (CEO) / Oana Onciu (Scientist) More info conference: http://meetings.embo.org/event/17-ubiquitin
publications
Collaborative research between the University of York, University of Glasgow and UbiQ looks into the (essential) roles of ubiquitin proteases (DUBs) and ubiquitin conjugation in Leishmania parasites.
21st Royal Society of Chemistry - Medicinal Chemistry Symposium, 13 - 15 September 2021, Cambridge UK. Poster title: A ubiquitin activating enzyme as a novel therapeutic target for leishmaniasis. Daniel Harris (1), Dr Mads Gabrielson (2),...
Anti–COVID-19 Drug Design by targeting a molecular scissor of Ubiquitin and ISG15.
UbiQ is proud to have been part of a major collaboration reported recently by Rut et al. in Science Advances, describing the activity profiling and crystal structures of inhibitor bound SARS-CoV-2 PLpro: Activity profiling and...
Leishmania differentiation requires ubiquitin conjugation mediated by a UBC2-UEV1 E2 complex.
Collaborative research between the University of York, University of Glasgow and UbiQ looks into the (essential) roles of ubiquitin proteases (DUBs) and ubiquitin conjugation in Leishmania parasites. Leishmaniasis is a neglected tropical disease caused by...
Strategy for Development of Site-Specific Ubiquitin Antibodies.
As part of collaborative research between The Netherlands Cancer Institute, Leiden University Medical Centre, UbiQ and the University of Amsterdam, van Kruijsbergen et al. report in Frontiers in Chemistry detailed protocols for the development...
Diubiquitin-Based NMR Analysis: Interactions Between Lys6-Linked diUb and UBA Domain of UBXN1.
As part of collaborative research carried out by The Netherlands Cancer Institute, Leiden University Medical Centre, Utrecht University, UbiQ and the University of Cologne, Hameed et al. report in Frontiers in Chemistry the synthesis...
Regulation of the endosomal SNX27-retromer by OTULIN.
An international collaboration led by Prof Daniel Krappmann (Helmholtz Zentrum München) reported in Nature Communications the identification of the DUB Otulin as a regulator of the levels of nutrient transporters on the cell surface....
Metabolic control of BRISC–SHMT2 assembly regulates immune signalling
An international collaboration led by Dr Elton Zeqiraj (University of Leeds, UK) and Prof Roger Greenberg (University of Pennsylvania, US) reported in Nature the cryo-electron microscopy structure of the human BRISC–SHMT2 complex, which is...