Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Christian R. O. Bartling"'
Autor:
Christian R. O. Bartling, Flora Alexopoulou, Sarah Kuschert, Yanni K.-Y. Chin, Xinying Jia, Vita Sereikaite, Dennis Özcelik, Thomas M. Jensen, Palash Jain, Mads M. Nygaard, Kasper Harpsøe, David E. Gloriam, Mehdi Mobli, Kristian Strømgaard
Publikováno v:
Journal of Medicinal Chemistry. 66:3045-3057
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c54e256f27312b17a95a409e698c824b
https://doi.org/10.1021/acs.jmedchem.2c02017
https://doi.org/10.1021/acs.jmedchem.2c02017
Generation of amyloid-beta (Aβ) peptides through the proteolytic processing of the amyloid precursor protein (APP) is one pathogenic event in Alzheimer’s disease (AD). APP is a type I transmembrane protein and endocytosis of APP mediated by the en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0ab2dd79e435c967901defced7bbe9b2
https://doi.org/10.1101/2022.10.07.511363
https://doi.org/10.1101/2022.10.07.511363
Autor:
Per Jemth, Linda M. Haugaard-Kedström, Kristian Strømgaard, Andreas Karlsson, Christian R. O. Bartling, Thomas M T Jensen, Emma Åberg
Publikováno v:
ACS Chemical Biology
Jensen, T M T, Bartling, C R O, Karlsson, O A, Åberg, E, Haugaard-Kedström, L M, Strømgaard, K & Jemth, P 2021, ' Molecular Details of a Coupled Binding and Folding Reaction between the Amyloid Precursor Protein and a Folded Domain ', ACS chemical biology, vol. 16, no. 7, pp. 1191-1200 . https://doi.org/10.1021/acschembio.1c00176
Jensen, T M T, Bartling, C R O, Karlsson, O A, Åberg, E, Haugaard-Kedström, L M, Strømgaard, K & Jemth, P 2021, ' Molecular Details of a Coupled Binding and Folding Reaction between the Amyloid Precursor Protein and a Folded Domain ', ACS chemical biology, vol. 16, no. 7, pp. 1191-1200 . https://doi.org/10.1021/acschembio.1c00176
Intrinsically disordered regions in proteins often function as binding motifs in protein-protein interactions. The mechanistic aspects and molecular details of such coupled binding and folding reactions, which involve formation of multiple noncovalen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ae554c538e3b5818a15e91e44f89eff
https://doi.org/10.1021/acschembio.1c00176
https://doi.org/10.1021/acschembio.1c00176
Autor:
Nima Rajabi, Tobias N. Hansen, Alexander L. Nielsen, Huy T. Nguyen, Michael Bæk, Julie. E. Bolding, Oskar Ø. Bahlke, Sylvester E. G. Petersen, Christian R. O. Bartling, Kristian Strømgaard, Christian A. Olsen
Publikováno v:
Rajabi, N, Hansen, T N, Nielsen, A L, Nguyen, H T, Bæk, M, Bolding, J E, Bahlke, O, Petersen, S E G, Bartling, C R O, Strømgaard, K & Olsen, C A 2022, ' Investigation of Carboxylic Acid Isosteres and Prodrugs for Inhibition of the Human SIRT5 Lysine Deacylase Enzyme** ', Angewandte Chemie-International Edition, vol. 61, no. 22, e202115805 . https://doi.org/10.1002/anie.202115805
Sirtuin 5 (SIRT5) is a protein lysine deacylase enzyme that regulates diverse biology by hydrolyzing ϵ-N-carboxyacyllysine posttranslational modifications in the cell. Inhibition of SIRT5 has been linked to potential treatment of several cancers but
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::956ebf1e24bd8815528df1bf86d2fcfe
https://curis.ku.dk/portal/da/publications/investigation-of-carboxylic-acid-isosteres-and-prodrugs-for-inhibition-of-the-human-sirt5-lysine-deacylase-enzyme(30614323-0e9e-4a4a-a1f4-3ac1d53aea94).html
https://curis.ku.dk/portal/da/publications/investigation-of-carboxylic-acid-isosteres-and-prodrugs-for-inhibition-of-the-human-sirt5-lysine-deacylase-enzyme(30614323-0e9e-4a4a-a1f4-3ac1d53aea94).html
Autor:
Julie E. Bolding, Pablo Martín‐Gago, Nima Rajabi, Luke F. Gamon, Tobias N. Hansen, Christian R. O. Bartling, Kristian Strømgaard, Michael J. Davies, Christian A. Olsen
Publikováno v:
Angewandte Chemie
Bolding, J E, Martín-Gago, P, Rajabi, N, Gamon, L F, Hansen, T N, Bartling, C R O, Strømgaard, K, Davies, M J & Olsen, C A 2022, ' Aryl Fluorosulfate Based Inhibitors That Covalently Target the SIRT5 Lysine Deacylase** ', Angewandte Chemie-International Edition, vol. 61, no. 47, e202204565 . https://doi.org/10.1002/anie.202204565
Bolding, J E, Martín-Gago, P, Rajabi, N, Gamon, L F, Hansen, T N, Bartling, C R O, Strømgaard, K, Davies, M J & Olsen, C A 2022, ' Aryl Fluorosulfate Based Inhibitors That Covalently Target the SIRT5 Lysine Deacylase** ', Angewandte Chemie-International Edition, vol. 61, no. 47, e202204565 . https://doi.org/10.1002/anie.202204565
The sirtuin enzymes are a family of lysine deacylases that regulate gene transcription and metabolism. Sirtuin 5 (SIRT5) hydrolyzes malonyl, succinyl, and glutaryl ϵ-N-carboxyacyllysine posttranslational modifications and has recently emerged as a v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06aa4fc1a595c43733a8d29a8978f1a9
Investigation of Carboxylic Acid Isosteres for Inhibition of the Human SIRT5 Lysine Deacylase Enzyme
Autor:
Sylvester E. G. Petersen, Michael Bæk, Huy T. Nguyen, Christian R. O. Bartling, Nima Rajabi, Christian A. Olsen, Julie E. Bolding, Alexander L. Nielsen, Tobias Nikolaj Gress Hansen, Kristian Strømgaard, Oskar Ørts Bahlke
Sirtuin 5 (SIRT5) is a protein lysine deacylase enzyme that regulates diverse biology by hydrolyzing -N-carboxyacyllysine posttranslational modifications in the cell. Inhibition of SIRT5 has been linked to potential treatment of several cancers bu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5c0ba5190480559a31c8e30d497899af
https://doi.org/10.26434/chemrxiv-2021-29rtf
https://doi.org/10.26434/chemrxiv-2021-29rtf
Autor:
Christian R. O. Bartling, Maria Vistrup-Parry, Louise S. Clemmensen, Michael L. Nielsen, Sara C. Buch-Larsen, Sofie Bach, Thea L. Johansen, Kristian Strømgaard, Mingjie Zhang, Xudong Chen, Chenxue Ma
Publikováno v:
iScience, Vol 24, Iss 11, Pp 103268-(2021)
iScience
Vistrup-Parry, M, Chen, X, Johansen, T L, Bach, S, Buch-Larsen, S C, Bartling, C R O, Ma, C, Clemmensen, L S, Nielsen, M L, Zhang, M & Stromgaard, K 2021, ' Site-specific phosphorylation of PSD-95 dynamically regulates the postsynaptic density as observed by phase separation ', iScience, vol. 24, no. 11, 103268 . https://doi.org/10.1016/j.isci.2021.103268
iScience
Vistrup-Parry, M, Chen, X, Johansen, T L, Bach, S, Buch-Larsen, S C, Bartling, C R O, Ma, C, Clemmensen, L S, Nielsen, M L, Zhang, M & Stromgaard, K 2021, ' Site-specific phosphorylation of PSD-95 dynamically regulates the postsynaptic density as observed by phase separation ', iScience, vol. 24, no. 11, 103268 . https://doi.org/10.1016/j.isci.2021.103268
Summary Postsynaptic density protein 95 is a key scaffolding protein in the postsynaptic density of excitatory glutamatergic neurons, organizing signaling complexes primarily via its three PSD-95/Discs-large/Zona occludens domains. PSD-95 is regulate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3938bbac5b91c3938486fdcaa4b4a50
http://www.sciencedirect.com/science/article/pii/S2589004221012372
http://www.sciencedirect.com/science/article/pii/S2589004221012372
Autor:
Simon Erlendsson, Gith Noes-Holt, Kathrine L. Jensen, Sofie E Pedersen, Ulrik Gether, Lise Arleth, Søren Roi Midtgaard, Klaus B. Nissen, Kenneth L. Madsen, Mette Rathje, Nikolaj R. Christensen, Kristian Strømgaard, Christian Bjerggaard Vaegter, Marta De Luca, Mette Richner, Anders Bach, Dennis Bo Jensen, Andreas T. Sørensen, Michèle Schönauer, Ina Ammendrup-Johnsen, C. F. Meehan, Michael Brett Lever, Astrid B Hansen, Kaare Teilum, Christian R. O. Bartling
Publikováno v:
Christensen, N R, De Luca, M, Lever, M B, Richner, M, Hansen, A B, Noes-Holt, G, Jensen, K L, Rathje, M, Jensen, D B, Erlendsson, S, Bartling, C R, Ammendrup-Johnsen, I, Pedersen, S E, Schönauer, M, Nissen, K B, Midtgaard, S R, Teilum, K, Arleth, L, Sørensen, A T, Bach, A, Strømgaard, K, Meehan, C F, Vaegter, C B, Gether, U & Madsen, K L 2020, ' A high-affinity, bivalent PDZ domain inhibitor complexes PICK1 to alleviate neuropathic pain ', EMBO Molecular Medicine, vol. 12, 11248 . https://doi.org/10.15252/emmm.201911248
Christensen, N R, De Luca, M, Lever, M B, Richner, M, Hansen, A B, Noes-Holt, G, Jensen, K L, Rathje, M, Jensen, D B, Erlendsson, S, Bartling, C R O, Ammendrup-Johnsen, I, Pedersen, S E, Schönauer, M, Nissen, K B, Midtgaard, S R, Teilum, K, Arleth, L, Sørensen, A T, Bach, A, Strømgaard, K, Meehan, C F, Vægter, C B, Gether, U & Madsen, K L 2020, ' A high-affinity, bivalent PDZ domain inhibitor complexes PICK1 to alleviate neuropathic pain ', EMBO Molecular Medicine, vol. 12, no. 6, e11248 . https://doi.org/10.15252/emmm.201911248
EMBO molecular medicine 12(6), e11248 (2020). doi:10.15252/emmm.201911248
EMBO Molecular Medicine, Vol 12, Iss 6, Pp n/a-n/a (2020)
EMBO Molecular Medicine
Christensen, N R, De Luca, M, Lever, M B, Richner, M, Hansen, A B, Noes-Holt, G, Jensen, K L, Rathje, M, Jensen, D B, Erlendsson, S, Bartling, C R O, Ammendrup-Johnsen, I, Pedersen, S E, Schönauer, M, Nissen, K B, Midtgaard, S R, Teilum, K, Arleth, L, Sørensen, A T, Bach, A, Strømgaard, K, Meehan, C F, Vægter, C B, Gether, U & Madsen, K L 2020, ' A high-affinity, bivalent PDZ domain inhibitor complexes PICK1 to alleviate neuropathic pain ', EMBO Molecular Medicine, vol. 12, no. 6, e11248 . https://doi.org/10.15252/emmm.201911248
EMBO molecular medicine 12(6), e11248 (2020). doi:10.15252/emmm.201911248
EMBO Molecular Medicine, Vol 12, Iss 6, Pp n/a-n/a (2020)
EMBO Molecular Medicine
EMBO molecular medicine 12(6), e11248 (2020). doi:10.15252/emmm.201911248
Maladaptive plasticity involving increased expression of AMPA‐type glutamate receptors is involved in several pathologies, including neuropathic pain, but direct inhibit
Maladaptive plasticity involving increased expression of AMPA‐type glutamate receptors is involved in several pathologies, including neuropathic pain, but direct inhibit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24f2a79c35640aba4c47c10fe446bf83
https://pure.au.dk/portal/da/publications/a-highaffinity-bivalent-pdz-domain-inhibitor-complexes-pick1-to-alleviate-neuropathic-pain(1f97eff6-28ca-4b06-a6fe-7e8ac62e3100).html
https://pure.au.dk/portal/da/publications/a-highaffinity-bivalent-pdz-domain-inhibitor-complexes-pick1-to-alleviate-neuropathic-pain(1f97eff6-28ca-4b06-a6fe-7e8ac62e3100).html
Autor:
Kristian Strømgaard, Christian R. O. Bartling, Thomas M. T. Jensen, Louise Albertsen, Linda M. Haugaard-Kedström
Publikováno v:
ChemBioChem. 19:1119-1122
The intracellular adaptor protein Mint2 binds amyloid precursor protein (APP) and presenilin-1, which are both central constituents of the amyloidogenic pathway associated with Alzheimer's disease (AD). Additional interaction partners have also been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b7b68468adc78dbac84652776429e63
https://doi.org/10.1002/cbic.201800004
https://doi.org/10.1002/cbic.201800004
Autor:
Vita Sereikaitė, Thomas M. T. Jensen, Stephan A. Pless, Christian R. O. Bartling, Kristian Strømgaard, Per Jemth
Publikováno v:
Chembiochem : a European journal of chemical biology. 19(20)
All proteins contain characteristic backbones formed of consecutive amide bonds, which can engage in hydrogen bonds. However, the importance of these is not easily addressed by conventional technologies that only allow for side-chain substitutions. B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b3107b8d04da52eefa831d8cec39fab
https://pubmed.ncbi.nlm.nih.gov/30073762
https://pubmed.ncbi.nlm.nih.gov/30073762