Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Charlotte S. Sørensen"'
Autor:
Giulia Monti, Lars Friis Mikkelsen, Marianne Lundsgaard Kristensen, Kirsten R Jacobsen, Charlotte E. Teunissen, David J. Brooks, Lars Bolund, Anne M. Landau, Christoffer Laustsen, Scott A. Small, Yonglun Luo, Anne Mette G. Jensen, Laura Breidenbach, Gro Grunnet Pløen, Jens R. Nyengaard, Margarita Melnikova Jørgensen, Hanne Skovsgaard Pedersen, Esben Søvsø Szocska Hansen, Charlotte S. Sørensen, Nikolaj Bøgh, Ying Liu, Mathias Droescher, Henrik Callesen, Benedicte Parm Ulhøi, Ida Elisabeth Holm, Olav M. Andersen
Publikováno v:
SSRN Electronic Journal.
The few established causal genes in Alzheimer’s disease (AD), mutations in APP and PSENs, have been functionally characterized using biomarkers, capturing an in vivo profile reflecting the disease’s initial preclinical phase. SORL1, a gene encodi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c889777cc95690fcd8e7edfc98005a51
https://doi.org/10.2139/ssrn.3911555
https://doi.org/10.2139/ssrn.3911555
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2141
Intrinsically disordered linkers control avidity, auto-inhibition, catalysis, and liquid-liquid phase separation in multidomain proteins. Linkers enforce effective concentrations that directly affect the kinetics and equilibrium positions of intramol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::63eefa751ab3b64acddac97631a0f902
https://pubmed.ncbi.nlm.nih.gov/32696374
https://pubmed.ncbi.nlm.nih.gov/32696374
Publikováno v:
Methods in Molecular Biology ISBN: 9781071605233
Sørensen, C S & Kjaergaard, M 2020, Measuring Effective Concentrations Enforced by Intrinsically Disordered Linkers . in B B Kragelund & K Skriver (eds), Intrinsically Disordered Proteins : Methods and protocols . Humana Press, New York, Methods in Molecular Biology, vol. 2141, pp. 505-518 . https://doi.org/10.1007/978-1-0716-0524-0_25
Sørensen, C S & Kjaergaard, M 2020, Measuring Effective Concentrations Enforced by Intrinsically Disordered Linkers . in B B Kragelund & K Skriver (eds), Intrinsically Disordered Proteins : Methods and protocols . Humana Press, New York, Methods in Molecular Biology, vol. 2141, pp. 505-518 . https://doi.org/10.1007/978-1-0716-0524-0_25
Intrinsically disordered linkers control avidity, auto-inhibition, catalysis, and liquid-liquid phase separation in multidomain proteins. Linkers enforce effective concentrations that directly affect the kinetics and equilibrium positions of intramol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f29b94bf340b56a68cd77fd0aa7caebc
https://doi.org/10.1007/978-1-0716-0524-0_25
https://doi.org/10.1007/978-1-0716-0524-0_25
Publikováno v:
Sørensen, C S & Kjaergaard, M 2019, ' Effective concentrations enforced by intrinsically disordered linkers are governed by polymer physics ', PNAS (Proceedings of the National Academy of Sciences of the United States of America), vol. 116, no. 46, pp. 23124-23131 . https://doi.org/10.1073/pnas.1904813116
Many multidomain proteins contain disordered linkers that regulate interdomain contacts, and thus the effective concentrations that govern intramolecular reactions. Effective concentrations are rarely measured experimentally, and therefore little is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46b90783c6b3c6ca9833b05613d57331
https://pure.au.dk/portal/da/publications/effective-concentrations-enforced-by-intrinsically-disordered-linkers-are-governed-by-polymer-physics(a5ae3509-c42b-4a49-bfa1-535b0ca7f008).html
https://pure.au.dk/portal/da/publications/effective-concentrations-enforced-by-intrinsically-disordered-linkers-are-governed-by-polymer-physics(a5ae3509-c42b-4a49-bfa1-535b0ca7f008).html
Publikováno v:
Sørensen, C S, Jendroszek, A & Kjærgaard, M 2019, ' Linker Dependence of Avidity in Multivalent Interactions between Disordered Proteins ', Journal of Molecular Biology, vol. 431, no. 24, pp. 4784-4795 . https://doi.org/10.1016/j.jmb.2019.09.001
Multidomain proteins often interact through several independent binding sites connected by disordered linkers. The architecture of such linkers affect avidity by modulating the effective concentration of intra-molecular binding. The linker dependence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3654eb6daf56b3bb25bd8cc243343fc
Autor:
Morten Jensen, Jan J. Enghild, Kasper Runager, Gunna Christiansen, Steen V. Petersen, Carsten Scavenius, Charlotte S. Sørensen, Nadia Sukusu Nielsen, Henrik Karring, Kristian W. Sanggaard
Publikováno v:
Sørensen, C S, Runager, K, Scavenius, C, Jensen, M M, Nielsen, N S, Christiansen, G, Petersen, S V, Karring, H, Sanggaard, K W & Enghild, J J 2015, ' Fibril Core of Transforming Growth Factor Beta-Induced Protein (TGFBIp) Facilitates Aggregation of Corneal TGFBIp ', Biochemistry, vol. 54, no. 19, pp. 2943-2956 . https://doi.org/10.1021/acs.biochem.5b00292
Sørensen, C S, Runager, K S, Scavenius, C, Jensen, M M, Nielsen, N S, Christiansen, G, Petersen, S V, Karring, H, Sanggaard, K W & Enghild, J J 2015, ' Fibril core of transforming growth factor beta-induced protein (TGFBIp) facilitates aggregation of corneal TGFBIp ', Biochemistry, vol. 19, no. 54, pp. 2943-2956 . https://doi.org/10.1021/acs.biochem.5b00292
Sørensen, C S, Runager, K S, Scavenius, C, Jensen, M M, Nielsen, N S, Christiansen, G, Petersen, S V, Karring, H, Sanggaard, K W & Enghild, J J 2015, ' Fibril core of transforming growth factor beta-induced protein (TGFBIp) facilitates aggregation of corneal TGFBIp ', Biochemistry, vol. 19, no. 54, pp. 2943-2956 . https://doi.org/10.1021/acs.biochem.5b00292
Mutations in the transforming growth factor beta-induced (TGFBI) gene result in a group of hereditary diseases of the cornea that are collectively known as TGFBI corneal dystrophies. These mutations translate into amino acid substitutions mainly with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7baa2361acbf34cf249463f1fa0157df
https://doi.org/10.1021/acs.biochem.5b00292
https://doi.org/10.1021/acs.biochem.5b00292
Publikováno v:
Biophysical Journal. 114:368a-369a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::edfb5001405ad97005fc06a952cd2bf8
https://doi.org/10.1016/j.bpj.2017.11.2042
https://doi.org/10.1016/j.bpj.2017.11.2042
Autor:
Ole Juul Andersen, Carsten Scavenius, Heidi Koldsø, Charlotte S. Sørensen, Birgit Schiøtt, Jan J. Enghild, Niels Chr. Nielsen, Camilla Lund Nikolajsen, Kasper Runager, Jarl Underhaug
Publikováno v:
Koldsø, H, Andersen, O J, Nikolajsen, C L, Scavenius, C, Sørensen, C S, Underhaug, J, Runager, K, Nielsen, N C, Enghild, J J & Schiøtt, B 2015, ' Early Events in the Amyloid Formation of the A546T Mutant of Transforming Growth Factor Beta Induced Protein (TGFBIp) in Corneal Dystrophies Compared to the Non-Fibrillating R555W and R555Q Mutants ', Biochemistry, vol. 54, no. 36, pp. 55546-5556 . https://doi.org/10.1021/acs.biochem.5b00473
The human transforming growth factor beta induced protein (TGFBIp) is involved in several types of corneal dystrophies where protein aggregation and amyloid fibril formation severely impairs vision. Most disease-causing mutations are located in the l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::beb5d39ffda2e177123988d8bf66ead0
https://pure.au.dk/portal/da/publications/early-events-in-the-amyloid-formation-of-the-a546t-mutant-of-transforming-growth-factor-beta-induced-protein-tgfbip-in-corneal-dystrophies-compared-to-the-nonfibrillating-r555w-and-r555q-mutants(65d5948f-754e-4371-a36b-a6502a85d156).html
https://pure.au.dk/portal/da/publications/early-events-in-the-amyloid-formation-of-the-a546t-mutant-of-transforming-growth-factor-beta-induced-protein-tgfbip-in-corneal-dystrophies-compared-to-the-nonfibrillating-r555w-and-r555q-mutants(65d5948f-754e-4371-a36b-a6502a85d156).html
Autor:
Maria Andreasen, Frans A. A. Mulder, Jan J. Enghild, Kasper Runager, Morten Bjerring, Natalia Kulminskaya, Yuichi Yoshimura, Niels Chr. Nielsen, Charlotte S. Sørensen, Daniel E. Otzen
Publikováno v:
Kulminskaya, N V, Yoshimura, Y, Runager, K, Sørensen, C S, Bjerring, M, Andreasen, M, Otzen, D E, Enghild, J J, Nielsen, N C & Mulder, F A A 2016, ' Near-complete 1 H, 13 C, 15 N resonance assignments of dimethylsulfoxide-denatured TGFBIp FAS1-4 A546T ', Biomolecular N M R Assignments, vol. 10, no. 1, pp. 25-29 . https://doi.org/10.1007/s12104-015-9630-2
The transforming growth factor beta induced protein (TGFBIp) is a major protein component of the human cornea. Mutations occurring in TGFBIp may cause corneal dystrophies, which ultimately lead to loss of vision. The majority of the disease-causing m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd8f6b0965cc82cdeee0fc7b82b1b471
https://pubmed.ncbi.nlm.nih.gov/26275916
https://pubmed.ncbi.nlm.nih.gov/26275916
Autor:
Henrik Karring, Ida B. Thøgersen, Gordon K. Klintworth, Jan J. Enghild, Rajiv Vaid Basaiawmoit, Jarl Underhaug, Niels Chr. Nielsen, Gunna Christiansen, Charlotte S. Sørensen, Taru Deva, Kasper Runager, Zuzana Valnickova, Torsten Nygaard Kristensen, Daniel E. Otzen, Maria Andreasen
Publikováno v:
Runager, K, Basaiawmoit, R V, Deva, T, Andreasen, M, Valnickova, Z, Sørensen, C S, Karring, H, Thøgersen, I B, Christiansen, G, Underhaug, J, Kristensen, T, Nielsen, N C, Klintworth, G K, Otzen, D E & Enghild, J J 2011, ' Human Phenotypically Distinct TGFBI Corneal Dystrophies Are Linked to the Stability of the Fourth FAS1 Domain of TGFBIp ', Journal of Biological Chemistry, vol. 286, no. 7, pp. 4951-8 . https://doi.org/10.1074/jbc.M110.181099
Runager, K, Basaiawmoit, R V, Deva, T, Andreasen, M, Valnickova, Z, Sorensen, C S, Karring, H, Thogersen, I B, Christiansen, G, Underhaug, J, Kristensen, T, Westergård-Nielsen, N C, Klintworth, G K, Otzen, D E & Enghild, J J 2011, ' Human phenotypically distinct TGFBI corneal dystrophies are linked to the stability of the fourth fas1 domain of TGFBIp ', Journal of Biological Chemistry, vol. 286, pp. 4951-4958 . https://doi.org/10.1074/jbc.M110.181099
Runager, K, Basaiawmoit, R V, Deva, T, Andreasen, M, Valnickova, Z, Sorensen, C S, Karring, H, Thogersen, I B, Christiansen, G, Underhaug, J, Kristensen, T, Westergård-Nielsen, N C, Klintworth, G K, Otzen, D E & Enghild, J J 2011, ' Human phenotypically distinct TGFBI corneal dystrophies are linked to the stability of the fourth fas1 domain of TGFBIp ', Journal of Biological Chemistry, vol. 286, pp. 4951-4958 . https://doi.org/10.1074/jbc.M110.181099
Mutations in the human TGFBI gene encoding TGFBIp have been linked to protein deposits in the cornea leading to visual impairment. The protein consists of an N-terminal Cys-rich EMI domain and four consecutive fasciclin 1 (FAS1) domains. We have comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc16b73edf114c6f4c84f42c93ed11f4
https://pure.au.dk/portal/da/publications/human-phenotypically-distinct-tgfbi-corneal-dystrophies-are-linked-to-the-stability-of-the-fourth-fas1-domain-of-tgfbip(0512b872-f21d-48cd-8bb9-7eff65dd1a9c).html
https://pure.au.dk/portal/da/publications/human-phenotypically-distinct-tgfbi-corneal-dystrophies-are-linked-to-the-stability-of-the-fourth-fas1-domain-of-tgfbip(0512b872-f21d-48cd-8bb9-7eff65dd1a9c).html