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  • 1.
    Arvidsson, Per I.
    et al.
    Uppsala universitet, Science for Life Laboratory, SciLifeLab. Drug Discovery & Development Platform & Division of Translational Medicine and Chemical Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
    Sandberg, Kristian
    Uppsala universitet, Science for Life Laboratory, SciLifeLab. Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för läkemedelskemi, Avdelningen för organisk farmaceutisk kemi. Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, Sweden.
    Forsberg-Nilsson, Karin
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Neuroonkologi. Uppsala universitet, Science for Life Laboratory, SciLifeLab.
    Open for collaboration: an academic platform for drug discovery and development at SciLifeLab2016Inngår i: Drug Discovery Today, ISSN 1359-6446, E-ISSN 1878-5832, Vol. 21, nr 10, s. 1690-1698Artikkel, forskningsoversikt (Fagfellevurdert)
    Abstract [en]

    The Science for Life Laboratory Drug Discovery and Development (SciLifeLab DDD) platform reaches out to Swedish academia with an industry-standard infrastructure for academic drug discovery, supported by earmarked funds from the Swedish government. In this review, we describe the build-up and operation of the platform, and reflect on our first two years of operation, with the ambition to share learnings and best practice with academic drug discovery centers globally. We also discuss how the Swedish Teacher Exemption Law, an internationally unique aspect of the innovation system, has shaped the operation. Furthermore, we address how this investment in infrastructure and expertise can be utilized to facilitate international collaboration between academia and industry in the best interest of those ultimately benefiting the most from translational pharmaceutical research - the patients.

  • 2.
    Arvidsson, Per I.
    et al.
    Karolinska Inst, Sci Life Lab, Drug Discovery & Dev Platform, Stockholm, Sweden.;Karolinska Inst, Div Translat Med & Chem Biol, Dept Med Biochem & Biophys, Stockholm, Sweden.;Univ KwaZulu Natal, Catalysis & Peptide Res Unit, Durban, South Africa..
    Sandberg, Kristian
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för läkemedelskemi, Avdelningen för organisk farmaceutisk kemi. Uppsala universitet, Science for Life Laboratory, SciLifeLab. Karolinska Inst, Physiol & Pharmacol, Stockholm, Sweden..
    Sakariassen, Kjell S.
    KellSa Sas, Str Campo & Zampe 12, I-13900 Biella, BI, Italy..
    Institutional profile: the national Swedish academic drug discovery & development platform at SciLifeLab2017Inngår i: FUTURE SCIENCE OA, ISSN 2056-5623, Vol. 3, nr 2, artikkel-id FSO176Artikkel i tidsskrift (Annet (populærvitenskap, debatt, mm))
    Abstract [en]

    The Science for Life Laboratory Drug Discovery and Development Platform (SciLifeLab DDD) was established in Stockholm and Uppsala, Sweden, in 2014. It is one of ten platforms of the Swedish national SciLifeLab which support projects run by Swedish academic researchers with large-scale technologies for molecular biosciences with a focus on health and environment. SciLifeLab was created by the coordinated effort of four universities in Stockholm and Uppsala: Stockholm University, Karolinska Institutet, KTH Royal Institute of Technology and Uppsala University, and has recently expanded to other Swedish university locations. The primary goal of the SciLifeLab DDD is to support selected academic discovery and development research projects with tools and resources to discover novel lead therapeutics, either molecules or human antibodies. Intellectual property developed with the help of SciLifeLab DDD is wholly owned by the academic research group. The bulk of SciLifeLab DDD's research and service activities are funded from the Swedish state, with only consumables paid by the academic research group through individual grants.

  • 3.
    Drobin, Kimi
    et al.
    Royal Inst Technol, KTH, Sch Biotechnol, Affin Prote, SciLifeLab, Stockholm, Sweden.
    Assadi, Ghazaleh
    Karolinska Inst, Dept Biosci & Nutr, Stockholm, Sweden.
    Hong, Mun-Gwan
    Royal Inst Technol, KTH, Sch Biotechnol, Affin Prote, SciLifeLab, Stockholm, Sweden.
    Andersson, Eni
    Royal Inst Technol, KTH, Sch Biotechnol, Affin Prote, SciLifeLab, Stockholm, Sweden.
    Fredolini, Claudia
    Royal Inst Technol, KTH, Sch Biotechnol, Affin Prote, SciLifeLab, Stockholm, Sweden.
    Forsström, Björn
    Royal Inst Technol, KTH, Sch Biotechnol, Affin Prote, SciLifeLab, Stockholm, Sweden.
    Reznichenko, Anna
    Karolinska Inst, Dept Biosci & Nutr, Stockholm, Sweden.
    Akhter, Tahmina
    Karolinska Inst, Dept Biosci & Nutr, Stockholm, Sweden.
    Ek, Weronica E
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Medicinsk genetik och genomik. Uppsala universitet, Science for Life Laboratory, SciLifeLab. Karolinska Inst, Dept Biosci & Nutr, Stockholm, Sweden.
    Bonfiglio, Ferdinando
    Karolinska Inst, Dept Biosci & Nutr, Stockholm, Sweden; Biodonostia Hlth Res Inst, Dept Gastrointestinal & Liver Dis, San Sebastian, Spain.
    Berner Hansen, Mark
    AstraZeneca R&D, Innovat & Global Med, Mölndal, Sweden; Univ Copenhagen, Bispebjerg Hosp, Ctr Digest Dis, Copenhagen, Denmark.
    Sandberg, Kristian
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för läkemedelskemi. Uppsala universitet, Science for Life Laboratory, SciLifeLab. Karolinska Inst, Dept Physiol & Pharmacol, Stockholm, Sweden.
    Greco, Dario
    Univ Helsinki, Inst Biotechnol, Helsinki, Finland.
    Repsilber, Dirk
    Örebro Univ, Sch Med Sci, Örebro, Sweden.
    Schwenk, Jochen M.
    Royal Inst Technol, KTH, Sch Biotechnol, Affin Prote, SciLifeLab, Stockholm, Sweden.
    D’Amato, Mauro
    Karolinska Inst, Dept Biosci & Nutr, Stockholm, Sweden; BioDonostia Hlth Res Inst, San Sebastian, Spain; Ikerbasque, Basque Fdn Sci, Bilbao, Spain.
    Halfvarson, Jonas
    Örebro Univ, Fac Med & Hlth, Dept Gastroenterol, Örebro, Sweden.
    Targeted Analysis of Serum Proteins Encoded at Known Inflammatory Bowel Disease Risk Loci2019Inngår i: Inflammatory Bowel Diseases, ISSN 1078-0998, E-ISSN 1536-4844, Vol. 25, nr 2, s. 306-316Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Background: Few studies have investigated the blood proteome of inflammatory bowel disease (IBD). We characterized the serum abundance of proteins encoded at 163 known IBD risk loci and tested these proteins for their biomarker discovery potential.

    Methods: Based on the Human Protein Atlas (HPA) antibody availability, 218 proteins from genes mapping at 163 IBD risk loci were selected. Targeted serum protein profiles from 49 Crohn’s disease (CD) patients, 51 ulcerative colitis (UC) patients, and 50 sex- and age-matched healthy individuals were obtained using multiplexed antibody suspension bead array assays. Differences in relative serum abundance levels between disease groups and controls were examined. Replication was attempted for CD-UC comparisons (including disease subtypes) by including 64 additional patients (33 CD and 31 UC). Antibodies targeting a potentially novel risk protein were validated by paired antibodies, Western blot, immuno-capture mass spectrometry, and epitope mapping.

    Results: By univariate analysis, 13 proteins mostly related to neutrophil, T-cell, and B-cell activation and function were differentially expressed in IBD patients vs healthy controls, 3 in CD patients vs healthy controls and 2 in UC patients vs healthy controls (q < 0.01). Multivariate analyses further differentiated disease groups from healthy controls and CD subtypes from UC (P < 0.05). Extended characterization of an antibody targeting a novel, discriminative serum marker, the laccase (multicopper oxidoreductase) domain containing 1 (LACC1) protein, provided evidence for antibody on-target specificity.

    Conclusions: Using affinity proteomics, we identified a set of IBD-associated serum proteins encoded at IBD risk loci. These candidate proteins hold the potential to be exploited as diagnostic biomarkers of IBD.

  • 4.
    Orhan, F.
    et al.
    Karolinska Inst, Dept Physiol & Pharmacol, Stockholm, Sweden..
    Bhat, M.
    Prot Biomarkers Personalized Healthcare & Biomark, Innovat Med, Gothenburg, Sweden..
    Sandberg, Kristian
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för läkemedelskemi, Avdelningen för organisk farmaceutisk kemi. Uppsala universitet, Science for Life Laboratory, SciLifeLab. Karolinska Inst, Dept Physiol & Pharmacol, Stockholm, Sweden..
    Stahl, S.
    Prot Biomarkers Personalized Healthcare & Biomark, Innovat Med, Gothenburg, Sweden.;Karolinska Inst, Dept Clin Neurosci, Stockholm, Sweden..
    Piehl, F.
    Karolinska Inst, Dept Clin Neurosci, Ctr Psychiat Res, Stockholm, Sweden..
    Svensson, C.
    Karolinska Inst, Dept Physiol & Pharmacol, Stockholm, Sweden..
    Erhardt, S.
    Karolinska Inst, Dept Physiol & Pharmacol, Stockholm, Sweden..
    Schwieler, L.
    Karolinska Inst, Dept Physiol & Pharmacol, Stockholm, Sweden..
    Tryptophan Metabolism Along the Kynurenine Pathway Downstream of Toll-like Receptor Stimulation in Peripheral Monocytes2016Inngår i: Scandinavian Journal of Immunology, ISSN 0300-9475, E-ISSN 1365-3083, Vol. 84, nr 5, s. 262-271Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Tryptophan degradation along the kynurenine pathway is of central importance for the immune function. Toll-like receptors (TLRs), representing the first line of immune defence against pathogens, are expressed in various cell types. The most abundant expression is found on monocytes, macrophages and dendritic cells. The aim of this study was to investigate whether stimulation with different TLR ligands induces the kynurenine pathway in human peripheral monocytes. Cell supernatants were analysed using a liquid chromatography/mass spectrometry to measure kynurenine, kynurenic acid (KYNA), quinolinic acid (QUIN) and tryptophan. Stimulation of TLR-2, TLR-3, TLR-4, TLR-7/8 and TLR-9 was found to induce the production of kynurenine, but only stimulation of TLR-3 increased levels of further downstream metabolites, such as KYNA and QUIN. Stimulation of TLR-1, TLR-5 and TLR-6 did not induce the kynurenine pathway. Taken together, this study provides novel evidence demonstrating that TLR activation induces a pattern of downstream tryptophan degradation along the kynurenine pathway in monocytes. The results of this study may implicate that TLRs can be used as new drug targets for the regulation of aberrant tryptophan metabolism along this pathway, a potential therapeutic strategy that may be of importance in several disorders.

  • 5. Shalaly, Nancy Dekki
    et al.
    Aneiros, Eduardo
    Blank, Michael
    Mueller, Johan
    Nyman, Eva
    Blind, Michael
    Dabrowski, Michael A
    Andersson, Christin V
    Sandberg, Kristian
    Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Farmaceutiska fakulteten, Institutionen för läkemedelskemi, Avdelningen för organisk farmaceutisk kemi.
    Positive Modulation of the Glycine Receptor by Means of Glycine Receptor-Binding Aptamers2015Inngår i: Journal of Biomolecular Screening, ISSN 1087-0571, E-ISSN 1552-454X, Vol. 20, nr 9, s. 1112-1123Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    According to the gate control theory of pain, the glycine receptors (GlyRs) are putative targets for development of therapeutic analgesics. A possible approach for novel analgesics is to develop a positive modulator of the glycine-activated Cl(-) channels. Unfortunately, there has been limited success in developing drug-like small molecules to study the impact of agonists or positive modulators on GlyRs. Eight RNA aptamers with low nanomolar affinity to GlyRα1 were generated, and their pharmacological properties analyzed. Cytochemistry using fluorescein-labeled aptamers demonstrated GlyRα1-dependent binding to the plasma membrane but also intracellular binding. Using a fluorescent membrane potential assay, we could identify five aptamers to be positive modulators. The positive modulation of one of the aptamers was confirmed by patch-clamp electrophysiology on L(tk) cells expressing GlyRα1 and/or GlyRα1β. This aptamer potentiated whole-cell Cl(-) currents in the presence of low concentrations of glycine. To our knowledge, this is the first demonstration ever of RNA aptamers acting as positive modulators for an ion channel. We believe that these aptamers are unique and valuable tools for further studies of GlyR biology and possibly also as tools for assay development in identifying small-molecule agonists and positive modulators.

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