Výsledky vyhledávání - "Enghild, J. J."

Adjuvant-free in vivo targeting. Antigen delivery by alpha 2-macroglobulin enhances antibody formation

Autor: Chu, C T, Oury, T D, Enghild, J J, Pizzo, S V

Publikováno v: Chu, C T, Oury, T D, Enghild, J J & Pizzo, S V 1994, ' Adjuvant-free in vivo targeting. Antigen delivery by alpha 2-macroglobulin enhances antibody formation ', Journal of Immunology, vol. 152, no. 4, pp. 1538-45 .

The proteinase "inhibitor" alpha 2-macroglobulin (alpha 2M) is able to entrap and form covalent linkages with diverse proteins during a transient proteinase-activated state. These complexes are rapidly endocytosed after binding to receptors present o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e01be31ea9453a8d454c4b4ff0237d2e
https://doi.org/10.4049/jimmunol.152.4.1538

Zobrazit plný text záznamu

The folding of human aEC-sod and iEC-sod is an intracellular event

Autor: Steen Vang Petersen, Kristensen, T., Petersen, J. S., Ramsgaard, L., Oury, T. D., Crapo, J. D., Niels Chr. Nielsen, Enghild, J. J.

Publikováno v: Petersen, S V, Kristensen, T, Petersen, J S, Ramsgaard, L, Oury, T D, Crapo, J D, Nielsen, N C & Enghild, J J 2008, ' The folding of human aEC-sod and iEC-sod is an intracellular event ', Journal of Biological Chemistry .
Aarhus University

Udgivelsesdato: Apr. 2.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::d02d095ad11f7d44bb279be2b8a6c004
https://pure.au.dk/portal/da/publications/the-folding-of-human-aecsod-and-iecsod-is-an-intracellular-event(c0e9d400-0538-11dd-b919-000ea68e967b).html

Zobrazit plný text záznamu

Histologic distribution and biochemical properties of alpha 1-microglobulin in human placenta

Autor: Berggård, T, Enghild, J J, Badve, S, Salafia, C M, Lögdberg, L, Akerström, B

Publikováno v: Berggård, T, Enghild, J J, Badve, S, Salafia, C M, Lögdberg, L & Akerström, B 1999, ' Histologic distribution and biochemical properties of alpha 1-microglobulin in human placenta ', American Journal of Reproductive Immunology, vol. 41, no. 1, pp. 52-60 .

Udgivelsesdato: 1999-Jan PROBLEM: The embryo is protected from immunologic rejection by the mother, possibly accomplished by immunosuppressive molecules located in the placenta. We investigated the distribution and biochemical properties in placenta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pure_au_____::adec395ae17e7dc391232d948b5b07e4
https://pure.au.dk/portal/da/publications/histologic-distribution-and-biochemical-properties-of-alpha-1microglobulin-in-human-placenta(57adfd40-8657-11dd-a5a8-000ea68e967b).html

Zobrazit plný text záznamu

Alpha1-microglobulin chromophores are located to three lysine residues semiburied in the lipocalin pocket and associated with a novel lipophilic compound

Autor: Berggård, T, Cohen, A, Persson, P, Lindqvist, A, Cedervall, T, Silow, M, Thøgersen, I B, Jönsson, J A, Enghild, J J, Akerström, B

Publikováno v: Berggård, T, Cohen, A, Persson, P, Lindqvist, A, Cedervall, T, Silow, M, Thøgersen, I B, Jönsson, J A, Enghild, J J & Akerström, B 1999, ' Alpha1-microglobulin chromophores are located to three lysine residues semiburied in the lipocalin pocket and associated with a novel lipophilic compound ', Protein Science, vol. 8, no. 12, pp. 2611-20 .

Udgivelsesdato: 1999-Dec Alpha1-microglobulin (alpha1m) is an electrophoretically heterogeneous plasma protein. It belongs to the lipocalin superfamily, a group of proteins with a three-dimensional (3D) structure that forms an internal hydrophobic li

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pure_au_____::349d8cb3dfae0bc9710e030cc65a63bb
https://pure.au.dk/portal/da/publications/alpha1microglobulin-chromophores-are-located-to-three-lysine-residues-semiburied-in-the-lipocalin-pocket-and-associated-with-a-novel-lipophilic-compound(f2759170-840f-11dd-a5a8-000ea68e967b).html

Zobrazit plný text záznamu

Organization of the inter-alpha-inhibitor heavy chains on the chondroitin sulfate originating from Ser(10) of bikunin: posttranslational modification of IalphaI-derived bikunin

Autor: Enghild, J J, Thøgersen, I B, Cheng, F, Fransson, L A, Roepstorff, P, Rahbek-Nielsen, H

Publikováno v: Enghild, J J, Thøgersen, I B, Cheng, F, Fransson, L A, Roepstorff, P & Rahbek-Nielsen, H 1999, ' Organization of the inter-alpha-inhibitor heavy chains on the chondroitin sulfate originating from Ser(10) of bikunin: posttranslational modification of IalphaI-derived bikunin ', Biochemistry, vol. 38, no. 36, pp. 11804-13 .

Udgivelsesdato: 1999-Sep-7 Inter-alpha-inhibitor-derived bikunin was purified and the molecular mass was determined to be approximately 8.7 kDa higher than the prediction based on the protein sequence, suggesting extensive posttranslational modificat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pure_au_____::3b113a9afc4effa62f6d4707a52a03c0
https://pure.au.dk/portal/da/publications/organization-of-the-interalphainhibitor-heavy-chains-on-the-chondroitin-sulfate-originating-from-ser10-of-bikunin-posttranslational-modification-of-ialphaiderived-bikunin(920f5ce0-8657-11dd-a5a8-000ea68e967b).html

Zobrazit plný text záznamu

Angiostatin binds ATP synthase on the surface of human endothelial cells

Autor: Moser, T L, Stack, M S, Asplin, I, Enghild, J J, Højrup, P, Everitt, L, Hubchak, S, Schnaper, H W, Pizzo, S V

Publikováno v: Moser, T L, Stack, M S, Asplin, I, Enghild, J J, Højrup, P, Everitt, L, Hubchak, S, Schnaper, H W & Pizzo, S V 1999, ' Angiostatin binds ATP synthase on the surface of human endothelial cells ', Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 6, pp. 2811-6 .

Udgivelsesdato: 1999-Mar-16 Angiostatin, a proteolytic fragment of plasminogen, is a potent antagonist of angiogenesis and an inhibitor of endothelial cell migration and proliferation. To determine whether the mechanism by which angiostatin inhibits

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pure_au_____::31c4c1af0bd1606ce5b27f6b154100ca
https://pure.au.dk/portal/da/publications/angiostatin-binds-atp-synthase-on-the-surface-of-human-endothelial-cells(50cfdf20-8657-11dd-a5a8-000ea68e967b).html

Zobrazit plný text záznamu

The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis

Autor: Enghild, J J, Thøgersen, Ida, Oury, T D, Valnickova, Z, Hojrup, P, Crapo, J D

Publikováno v: Enghild, J J, Thøgersen, I, Oury, T D, Valnickova, Z, Hojrup, P & Crapo, J D 1999, ' The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis ', Journal of Biological Chemistry, vol. 274, no. 21, pp. 14818-22 .

Udgivelsesdato: 1999-May-21 Extracellular superoxide dismutase (EC-SOD) is the only known extracellular enzyme designed to scavenge the superoxide anion. The purified enzyme exists in two forms when visualized by reduced SDS-polyacrylamide gel electr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pure_au_____::e779af65325a005cf84eaeea0845b6be
https://pure.au.dk/portal/da/publications/the-heparinbinding-domain-of-extracellular-superoxide-dismutase-is-proteolytically-processed-intracellularly-during-biosynthesis(837591e0-8657-11dd-a5a8-000ea68e967b).html

Zobrazit plný text záznamu

Accumulation of beta ig-h3 gene product in corneas with granular dystrophy

Autor: Klintworth, G K, Valnickova, Z, Enghild, J J

Publikováno v: Klintworth, G K, Valnickova, Z & Enghild, J J 1998, ' Accumulation of beta ig-h3 gene product in corneas with granular dystrophy ', American Journal of Pathology, vol. 152, no. 3, pp. 743-8 .

Udgivelsesdato: 1998-Mar We isolated and identified the major protein present in corneas with granular dystrophy (GCD). We compared Coomassie-blue-stained protein bands obtained on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::86f615ac45c6c5300a2e8a24f68b1ab4
https://europepmc.org/articles/PMC1858399/

Zobrazit plný text záznamu

Human procarboxypeptidase U, or thrombin-activable fibrinolysis inhibitor, is a substrate for transglutaminases. Evidence for transglutaminase-catalyzed cross-linking to fibrin

Autor: Valnickova, Z, Enghild, J J

Publikováno v: Valnickova, Z & Enghild, J J 1998, ' Human procarboxypeptidase U, or thrombin-activable fibrinolysis inhibitor, is a substrate for transglutaminases. Evidence for transglutaminase-catalyzed cross-linking to fibrin ', Journal of Biological Chemistry, vol. 273, no. 42, pp. 27220-4 .

Udgivelsesdato: 1998-Oct-16 Procarboxypeptidase U (EC 3.4.17.20) (pro-CpU), also known as plasma procarboxypeptidase B and thrombin-activable fibrinolysis inhibitor, is a human plasma protein that has been implicated in the regulation of fibrinolysis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pure_au_____::82c1c4fa4b5167c6bcfe725a172d9a2b
https://pure.au.dk/portal/da/publications/human-procarboxypeptidase-u-or-thrombinactivable-fibrinolysis-inhibitor-is-a-substrate-for-transglutaminases-evidence-for-transglutaminasecatalyzed-crosslinking-to-fibrin(0b4f3fd0-8658-11dd-a5a8-000ea68e967b).html

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání