Zobrazeno 1 - 9 of 9 pro vyhledávání: '"Camilla Lund Nikolajsen"'
1
Coagulation Factor XIIIa Substrates in Human Plasma
Autor: Thomas F. Dyrlund, Jan J. Enghild, Camilla Lund Nikolajsen, Carsten Scavenius, Ebbe Toftgaard Poulsen
Publikováno v: Journal of Biological Chemistry. 289:6526-6534
Coagulation factor XIII (FXIII) is a transglutaminase with a well defined role in the final stages of blood coagulation. Active FXIII (FXIIIa) catalyzes the formation of ϵ-(γ-glutamyl)lysine isopeptide bonds between specific Gln and Lys residues. T
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3e53d9bc99c23cf2541fef50665dd63c
https://doi.org/10.1074/jbc.m113.517904
Zobrazit plný text záznamu
2
Human Cornea Proteome: Identification and Quantitation of the Proteins of the Three Main Layers Including Epithelium, Stroma, and Endothelium
Autor: Carsten Scavenius, Henrik Vorum, Jan J. Enghild, Thomas F. Dyrlund, Ida B. Thøgersen, Camilla Lund Nikolajsen, Ebbe Toftgaard Poulsen
Publikováno v: Journal of Proteome Research
Dyrlund, T F, Poulsen, E T, Sonne-Schmidt, C S, Nikolajsen, C L, Thøgersen, I B, Vorum, H & Enghild, J J 2012, ' Human cornea proteome : Identification and quantitation of the proteins of the three main layers including epithelium, stroma and endothelium ', Journal of Proteome Research, vol. 11, no. 8, pp. 4231–4239 . https://doi.org/10.1021/pr300358k
Diseases of the cornea are common and refer to conditions like infections, injuries and genetic defects. Morphologically, many corneal diseases affect only certain layers of the cornea and separate analysis of the individual layers is therefore of in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2e57171c1917d85a6414bab91c2ab9f
http://europepmc.org/articles/PMC3411198
Zobrazit plný text záznamu
3
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
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
Zobrazit plný text záznamu
4
The Compact and Biologically Relevant Structure of Inter-α-inhibitor Is Maintained by the Chondroitin Sulfate Chain and Divalent Cations
Autor: Jan J. Enghild, Camilla Lund Nikolajsen, Hans-Georg Wisniewski, Carsten Scavenius, Kristian W. Sanggaard, Daniel E. Otzen, Ida B. Thøgersen, Marcel Stenvang, Łukasz Wyrożemski
Publikováno v: Scavenius, C, Nikolajsen, C L, Stenvang, M, Thøgersen, I, Wyrozemski, L, Wisniewski, H-G, Otzen, D E, Sanggaard, K W & Enghild, J J 2016, ' The compact and biologically relevant structure of inter-α-inhibitor is maintained by the chondroitin sulfate chain and divalent cations ', Journal of Biological Chemistry, vol. 291, no. 9, pp. 4658-4670 . https://doi.org/10.1074/jbc.M115.678748
Inter-α-inhibitor is a proteoglycan of unique structure. The protein consists of three subunits, heavy chain 1, heavy chain 2, and bikunin covalently joined by a chondroitin sulfate chain originating at Ser-10 of bikunin. Inter-α-inhibitor interact
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4da9eb4f3bd842cd0006a71d7e218050
https://pubmed.ncbi.nlm.nih.gov/26728454
Zobrazit plný text záznamu
5
Coagulation factor XIIIa substrates in human plasma: identification and incorporation into the clot
Autor: Camilla Lund, Nikolajsen, Thomas F, Dyrlund, Ebbe Toftgaard, Poulsen, Jan J, Enghild, Carsten, Scavenius
Publikováno v: The Journal of biological chemistry. 289(10)
Coagulation factor XIII (FXIII) is a transglutaminase with a well defined role in the final stages of blood coagulation. Active FXIII (FXIIIa) catalyzes the formation of ε-(γ-glutamyl)lysine isopeptide bonds between specific Gln and Lys residues. T
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bbfa6a1a39c96ccbdedbe1c6f4a95998
https://pubmed.ncbi.nlm.nih.gov/24443567
Zobrazit plný text záznamu
8
Human complement C3 is a Substrate for Transglutaminases. A Functional Link between Non-Protease-Based Members of the Coagulation and Complement Cascades
Autor: Jan J. Enghild, Camilla Lund Nikolajsen, Carsten Scavenius
Publikováno v: Nikolajsen, C L, Scavenius, C & Enghild, J J 2012, ' Human complement C3 is a Substrate for Transglutaminases. A Functional Link between Non-Protease-Based Members of the Coagulation and Complement Cascades ', Biochemistry, vol. 51, no. 23, pp. 4735-4742 . https://doi.org/10.1021/bi3004022
In this study, we report the finding of functional cross-talk between two non-protease components of the complement and coagulation cascades. We show that complement C3, a central component of the complement system, is associated with the fibrin clot
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fd4521cdaad141ec7b107bed07adae7
https://pure.au.dk/portal/da/publications/human-complement-c3-is-a-substrate-for-transglutaminases-a-functional-link-between-nonproteasebased-members-of-the-coagulation-and-complement-cascades(168fd583-f95b-4d01-8c46-11cbd709abe3).html
Zobrazit plný text záznamu
9
Human inter-α-inhibitor is a substrate for factor XIIIa and tissue transglutaminase
Autor: Ole N. Jensen, Ida B. Thøgersen, Camilla Lund Nikolajsen, Carsten Scavenius, Peter Højrup, Steffen Bak, Kristian W. Sanggaard, Jan J. Enghild, Zuzana Valnickova
Publikováno v: Sonne-Schmidt, C S, Sanggaard, K W, Nikolajsen, C L, Bak, S, Valnickova, Z, Thøgersen, I B, Jensen, O N, Højrup, P & Enghild, J J 2011, ' Human inter-α-inhibitor is a substrate for factor XIIIa and tissue transglutaminase ', BBA General Subjects, vol. 1814, no. 12, pp. 1624-30 . https://doi.org/10.1016/j.bbapap.2011.08.017
Sonne-Schmidt, C S, Sanggaard, K W, Nikolajsen, C L, Bak, S, Valnickova, Z, Thøgersen, I, Jensen, O N, Højrup, P & Enghild, J J 2011, ' Human inter-α-inhibitor is a substrate for factor XIIIa and tissue transglutaminase ', BBA General Subjects, vol. 1814, no. 12, pp. 1624-1630 . https://doi.org/10.1016/j.bbapap.2011.08.017
In this study, we show that inter-α-inhibitor is a substrate for both factor XIIIa and tissue transglutaminase. These enzymes catalyze the incorporation of dansylcadaverine and biotin-pentylamine, revealing that inter-α-inhibitor contains reactive
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7725819c747b20188e4b32a0715701c
https://pure.au.dk/portal/da/publications/human-interinhibitor-is-a-substrate-for-factor-xiiia-and-tissue-transglutaminase(486e1eb4-900f-4f1d-8949-8cfee71a61ca).html
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje