Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Jacob H. Martinsen"'
Autor:
Pernille Seiffert, Katrine Bugge, Mads Nygaard, Gitte W. Haxholm, Jacob H. Martinsen, Martin N. Pedersen, Lise Arleth, Wouter Boomsma, Birthe B. Kragelund
Publikováno v:
Cell Communication and Signaling, Vol 18, Iss 1, Pp 1-30 (2020)
Abstract Background Class 1 cytokine receptors (C1CRs) are single-pass transmembrane proteins responsible for transmitting signals between the outside and the inside of cells. Remarkably, they orchestrate key biological processes such as proliferatio
Externí odkaz:
https://doaj.org/article/da80cd82ba2c4e498f5a4570acf51ca8
Autor:
Wouter Boomsma, Gitte W. Haxholm, Pernille Seiffert, Katrine Bugge, Jacob H. Martinsen, Martin Nors Pedersen, Birthe B. Kragelund, Lise Arleth, Mads Nygaard
Publikováno v:
Seiffert, P, Bugge, K, Nygaard, M, Haxholm, G W, Martinsen, J H, Pedersen, M N, Arleth, L, Boomsma, W & Kragelund, B B 2020, ' Orchestration of signaling by structural disorder in class 1 cytokine receptors ', Cell Communication and Signaling, vol. 18, no. 1, 132 . https://doi.org/10.1186/s12964-020-00626-6
Cell communication and signaling 18(1), 1-30 (2020). doi:10.1186/s12964-020-00626-6
Cell Communication and Signaling, Vol 18, Iss 1, Pp 1-30 (2020)
Cell Communication and Signaling : CCS
Cell communication and signaling 18(1), 1-30 (2020). doi:10.1186/s12964-020-00626-6
Cell Communication and Signaling, Vol 18, Iss 1, Pp 1-30 (2020)
Cell Communication and Signaling : CCS
Cell communication and signaling 18(1), 1-30 (2020). doi:10.1186/s12964-020-00626-6
Background:Class 1 cytokine receptors (C1CRs) are single-pass transmembrane proteins responsible for transmitting signals between the outside and the inside of c
Background:Class 1 cytokine receptors (C1CRs) are single-pass transmembrane proteins responsible for transmitting signals between the outside and the inside of c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3f28389f0c225061a45f73311a81fbc
https://doi.org/10.21203/rs.3.rs-23462/v2
https://doi.org/10.21203/rs.3.rs-23462/v2
Autor:
Synnøve Brandt Ræder, Kirsten Skarstad, Aina Nedal, Emily Helgesen, Magnar Bjørås, Balagra Kasim Sumabe, Jacob H. Martinsen, Bjørn Dalhus, Birthe B. Kragelund, Marit Otterlei, Kim Lindland, Rune Johansen Forstrøm
Publikováno v:
Nucleic Acids Research
Nedal, A, Ræder, S B, Dalhus, B, Helgesen, E, Forstrøm, R J, Lindland, K, Sumabe, B K, Martinsen, J H, Kragelund, B B, Skarstad, K, Bjørås, M & Otterlei, M 2020, ' Peptides containing the PCNA interacting motif APIM bind to the β-clamp and inhibit bacterial growth and mutagenesis ', Nucleic Acids Research, vol. 48, no. 10, pp. 5540-5554 . https://doi.org/10.1093/nar/gkaa278
Nedal, A, Ræder, S B, Dalhus, B, Helgesen, E, Forstrøm, R J, Lindland, K, Sumabe, B K, Martinsen, J H, Kragelund, B B, Skarstad, K, Bjørås, M & Otterlei, M 2020, ' Peptides containing the PCNA interacting motif APIM bind to the β-clamp and inhibit bacterial growth and mutagenesis ', Nucleic Acids Research, vol. 48, no. 10, pp. 5540-5554 . https://doi.org/10.1093/nar/gkaa278
In the fight against antimicrobial resistance, the bacterial DNA sliding clamp, β-clamp, is a promising drug target for inhibition of DNA replication and translesion synthesis. The β-clamp and its eukaryotic homolog, PCNA, share a C-terminal hydrop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1166f160e0f70964f9dd1e874599634
https://hdl.handle.net/11250/2679696
https://hdl.handle.net/11250/2679696
Autor:
Katrine Bugge, Saskia Bucciarelli, Birthe B. Kragelund, Line K Skaanning, Angelo Santoro, Bente Vestergaard, Thomas Skamris, Anna Maria D'Ursi, Jacob H. Martinsen, Annette Eva Langkilde
Publikováno v:
Biomolecules
Biomolecules 10(8), 1192-(2020). doi:10.3390/biom10081192
Biomolecules, Vol 10, Iss 1192, p 1192 (2020)
Volume 10
Issue 8
Skaanning, L K, Santoro, A, Skamris, T, Martinsen, J H, D’Ursi, A M, Bucciarelli, S, Vestergaard, B, Bugge, K, Langkilde, A E & Kragelund, B B 2020, ' The Non-Fibrillating N-Terminal of α-Synuclein Binds and Co-Fibrillates with Heparin ', Biomolecules, vol. 10, no. 8, 1192 . https://doi.org/10.3390/biom10081192
Biomolecules 10(8), 1192-(2020). doi:10.3390/biom10081192
Biomolecules, Vol 10, Iss 1192, p 1192 (2020)
Volume 10
Issue 8
Skaanning, L K, Santoro, A, Skamris, T, Martinsen, J H, D’Ursi, A M, Bucciarelli, S, Vestergaard, B, Bugge, K, Langkilde, A E & Kragelund, B B 2020, ' The Non-Fibrillating N-Terminal of α-Synuclein Binds and Co-Fibrillates with Heparin ', Biomolecules, vol. 10, no. 8, 1192 . https://doi.org/10.3390/biom10081192
The intrinsically disordered protein &alpha
synuclein (aSN) is, in its fibrillated state, the main component of Lewy bodies&mdash
hallmarks of Parkinson&rsquo
s disease. Additional Lewy body components include glycosaminoglycans, inclu
synuclein (aSN) is, in its fibrillated state, the main component of Lewy bodies&mdash
hallmarks of Parkinson&rsquo
s disease. Additional Lewy body components include glycosaminoglycans, inclu
Autor:
Benjamin Schuler, Birthe B. Kragelund, Catarina B. Fernandes, Katrine Bugge, Jacob H. Martinsen, Robert B. Best
Publikováno v:
Biophysical Journal. 118:371a