Výsledky vyhledávání - "Mette Dahl Andersen"

Structural characterization of both the non-proteolytic and proteolytic activation pathways of coagulation Factor XIII studied by hydrogen–deuterium exchange mass spectrometry

Autor: Mette Dahl Andersen, Johan H. Faber

Publikováno v: International Journal of Mass Spectrometry. 302:139-148

Activated Factor XIII is a 83 kDa transglutaminase crucial in the final steps of blood coagulation. FXIII can be activated both via a proteolytic pathway and a non-proteolytic pathway. Activation in plasma takes place by a thrombin catalyzed cleavage

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::134a23b1852760f0226d561861a2eaf5
https://doi.org/10.1016/j.ijms.2010.09.010

Zobrazit plný text záznamu

Reversible Activation of Cellular Factor XIII by Calcium

Autor: Gunhild Klarskov Kristiansen, Mette Dahl Andersen

Publikováno v: Journal of Biological Chemistry. 286:9833-9839

Factor XIII (FXIII) is a pro-transglutaminase found in the plasma as well as intracellularly in platelets and macrophages. Plasma FXIII is activated by thrombin cleavage (FXIIIa*) and acts in the final stages of blood coagulation cascade. In contrast

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97259158d8c40ba601d8ee08d9876ddd
https://doi.org/10.1074/jbc.m110.174128

Zobrazit plný text záznamu

Coagulation factor XIII variants with altered thrombin activation rates

Autor: Inger Lautrup-Larsen, Marianne Kjalke, Mette Dahl Andersen, Ole Hvilsted Olsen, Henning R. Stennicke, Peter B. Becker, Asser Sloth Andersen, Susanne Bang

Publikováno v: bchm. 390:1279-1283

Coagulation factor XIII (FXIII) is activated by thrombin and catalyses crosslinking between fibrin monomers thereby providing mechanical strength to the fibrin network. V34L is a common FXIII-A polymorphism found in the activation peptide. FXIII-A V3

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5eccf8e656cd890ea4c42a31f91cee8
https://doi.org/10.1515/bc.2009.142

Zobrazit plný text záznamu

Pro-interleukin (IL)-1β Shares a Core Region of Stability as Compared with Mature IL-1β While Maintaining a Distinctly Different Configurational Landscape

Autor: Sheng Li, Patricia A. Jennings, Kendra L. Hailey, Melinda Roy, Virgil L. Woods, Mette Dahl Andersen

Publikováno v: Journal of Biological Chemistry. 284:26137-26148

Interleukin-1β (IL-1β) is a master cytokine involved in initiating the innate immune response in vertebrates (Dinarello, C. A. (1994) FASEB J. 8, 1314–1325). It is first synthesized as an inactive 269-residue precursor (pro-interleukin-1β or pro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::aa15489ed562c4643d546a5fb5e91fb7
https://doi.org/10.1074/jbc.m109.027375

Zobrazit plný text záznamu

Probing the Conformational and Functional Consequences of Disulfide Bond Engineering in Growth Hormone by Hydrogen-Deuterium Exchange Mass Spectrometry Coupled to Electron Transfer Dissociation

Autor: Signe T. Seger, Johan H. Faber, Charlotte Wiberg, Jens Breinholt, Christine B. Schjødt, Kasper D. Rand, Mette Dahl Andersen

Publikováno v: Analytical chemistry. 87(12)

Human growth hormone (hGH), and its receptor interaction, is essential for cell growth. To stabilize a flexible loop between helices 3 and 4, while retaining affinity for the hGH receptor, we have engineered a new hGH variant (Q84C/Y143C). Here, we e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6fce70847ff195e5649c617222ad565
https://pubmed.ncbi.nlm.nih.gov/25978680

Zobrazit plný text záznamu

Cytochromes P-450 from Cassava (Manihot esculentaCrantz) Catalyzing the First Steps in the Biosynthesis of the Cyanogenic Glucosides Linamarin and Lotaustralin

Autor: Mette Dahl Andersen, Birger Lindberg Møller, Ib Svendsen, Peter Kamp Busk

Publikováno v: Journal of Biological Chemistry. 275:1966-1975

The first committed steps in the biosynthesis of the two cyanogenic glucosides linamarin and lotaustralin in cassava are the conversion of l-valine andl-isoleucine, respectively, to the corresponding oximes. Two full-length cDNA clones that encode cy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fd08e2f13729fefa5b6eb0a2c483d77f
https://doi.org/10.1074/jbc.275.3.1966

Zobrazit plný text záznamu

Heterologous expression and characterization of wild-type and mutant forms of a 26 kDa endochitinase from barley (Hordeum vulgare L.)

Autor: Jon D. Robertus, Robert Leah, Karen Skriver, Arne L. Jensen, Mette Dahl Andersen

Publikováno v: Biochemical Journal. 322:815-822

To investigate structure–function relationships in plant chitinases, we have developed a heterologous expression system for the 26 kDa endochitinase from Hordeum vulgare L. (barley). Escherichia coli cells harbouring the gene in a T7 RNA polymerase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9fba4067bd64f8a5632f50cecfcdc82
https://doi.org/10.1042/bj3220815

Zobrazit plný text záznamu

Prolonged half-life and preserved enzymatic properties of factor IX selectively PEGylated on native N-glycans in the activation peptide

Publikováno v: Blood. 118(8)

Current management of hemophilia B entails multiple weekly infusions of factor IX (FIX) to prevent bleeding episodes. In an attempt to make a longer acting recombinant FIX (rFIX), we have explored a new releasable protraction concept using the native

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbaabc81a11f6399a0797747f6229409
https://pubmed.ncbi.nlm.nih.gov/21700771

Zobrazit plný text záznamu

Crystal structure of a prolactin receptor antagonist bound to the extracellular domain of the prolactin receptor

Autor: Kent Bondensgaard, Leif Nørskov-Lauritsen, Peter Becker, Kasper D. Rand, L. Anders Svensson, Jens Breinholt, Morten Jonas Maltesen, Mette Dahl Andersen, Leif Christensen

Publikováno v: The Journal of biological chemistry. 283(27)

The crystal structure of the complex between an N-terminally truncated G129R human prolactin (PRL) variant and the extracellular domain of the human prolactin receptor (PRLR) was determined at 2.5A resolution by x-ray crystallography. This structure

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc2730b724aaf25284719e6715fbcb7f
https://pubmed.ncbi.nlm.nih.gov/18467331

Zobrazit plný text záznamu

The origins of enhanced activity in factor VIIa analogs and the interplay between key allosteric sites revealed by hydrogen exchange mass spectrometry

Autor: Henning R. Stennicke, Ole N. Jensen, Egon Persson, Mette Dahl Andersen, Thomas J. D. Jørgensen, Henrik Østergaard, Kasper D. Rand, Ole Hvilsted Olsen

Publikováno v: Rand, K D, Andersen, M D, Olsen, O H, Jørgensen, T J D, Ostergaard, H, Jensen, O N, Stennicke, H R & Persson, E 2008, ' The origins of enhanced activity in factor VIIa analogs and the interplay between key allosteric sites revealed by hydrogen exchange mass spectrometry ', Journal of Biological Chemistry, vol. 283, no. 19, pp. 13378-13387 . https://doi.org/10.1074/jbc.M709716200

Factor VIIa (FVIIa) circulates in the blood in a zymogen-like state. Only upon association with membrane-bound tissue factor (TF) at the site of vascular injury does FVIIa become active and able to initiate blood coagulation. Here we used hydrogen ex

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a339e70ed3cd0901d02b8cf636d018fe
https://pubmed.ncbi.nlm.nih.gov/18343822

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání