Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Emadoldin Feyzi"'
Autor:
Anne-Marit Sponaas, Neda Nejati Moharrami, Emadoldin Feyzi, Therese Standal, Even Holth Rustad, Anders Waage, Anders Sundan
Publikováno v:
PLoS ONE, Vol 10, Iss 10, p e0139867 (2015)
In this study we set out to investigate whether anti PDL1 or PD-1 treatment targeting the immune system could be used against multiple myeloma. DCs are important in regulating T cell responses against tumors. We therefore determined PDL1 and PDL2 exp
Externí odkaz:
https://doaj.org/article/7cebf2e048444632861d9ca46d1a934c
Publikováno v:
Biomacromolecules. 16:3417-3424
Alginate is a promising polysaccharide for use in biomaterials as it is biologically inert. One way to functionalize alginate is by chemical sulfation to emulate sulfated glycosaminoglycans, which interact with a variety of proteins critical for tiss
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8256595c518722d027f84c84ab710b9a
https://doi.org/10.1021/acs.biomac.5b01125
https://doi.org/10.1021/acs.biomac.5b01125
Autor:
Anne M, Sponaas, Siv H, Moen, Nina B, Liabakk, Emadoldin, Feyzi, Toril, Holien, Solveig, Kvam, Lill Anny G, Grøseth, Berit, Størdal, Glenn, Buene, Terje, Espevik, Anders, Waage, Therese, Standal, Anders, Sundan
Publikováno v:
Immunity, Inflammation and Disease
Multiple myeloma is an incurable cancer with expansion of malignant plasma cells in the bone marrow. Previous studies have shown that monocytes and macrophages in the bone marrow milieu are important for tumor growth and may play a role in the drug r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3a4238ea64ca59dba5af6ee8445e00e0
https://pubmed.ncbi.nlm.nih.gov/26029369
https://pubmed.ncbi.nlm.nih.gov/26029369
Publikováno v:
Journal of Biological Chemistry. 272:5518-5524
Platelet-derived growth factors (PDGFs) are homo- or heterodimers of two related polypeptides, known as A and B chains. The A chain exists as two splice variants due to the alternative usage of exons 6 (PDGF-AL, longer) and 7 (PDGF-AS, shorter). Exon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63c1e0c9606dfea54f0c7b105f3ac4f6
https://doi.org/10.1074/jbc.272.9.5518
https://doi.org/10.1074/jbc.272.9.5518
Publikováno v:
Biochemical Journal. 309:465-472
Capsular polysaccharide from Escherichia coli K5, with the basic structure (GlcA beta 1-4GlcNAc alpha 1-4)n, was chemically modified through N-deacetylation, N-sulphation and O-sulphation [Casu, Grazioli, Razi, Guerrini, Naggi, Torri, Oreste, Tursi,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8b1c6a848da65a535ac60bdfe8b28ba
https://doi.org/10.1042/bj3090465
https://doi.org/10.1042/bj3090465
Autor:
Per Arne Aas, Nina B. Liabakk, Hans E. Krokan, Emadoldin Feyzi, Karin Margaretha Gilljam, Cathrine Broberg Vågbø, Rebekka Müller, Geir Slupphaug, Finn Drabløs, Mirta M. L. Sousa, Tara C. Catterall, Marit Otterlei
Publikováno v:
The Journal of Cell Biology
AlkB PCNA-interacting motif (APIM) is present in >200 proteins and may mediate PCNA binding during genotoxic stress.
Numerous proteins, many essential for the DNA replication machinery, interact with proliferating cell nuclear antigen (PCNA) thr
Numerous proteins, many essential for the DNA replication machinery, interact with proliferating cell nuclear antigen (PCNA) thr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5d60046b4a1a63bf2cb8c1157a7c887
https://pubmed.ncbi.nlm.nih.gov/19736315
https://pubmed.ncbi.nlm.nih.gov/19736315
Autor:
Nina-Beate Liabakk, Lars Hagen, Vivi Talstad, Geir Slupphaug, Bodil Kavli, Emadoldin Feyzi, Marit Otterlei, Ottar Sundheim, Marianne Pedersen Westbye, Mansour Akbari, Cathrine Broberg Vågbø, Per Arne Aas, Hans E. Krokan
Publikováno v:
The Journal of biological chemistry. 283(36)
The Escherichia coli AlkB protein and human homologs hABH2 and hABH3 are 2-oxoglutarate (2OG)/Fe(II)-dependent DNA/RNA demethylases that repair 1-methyladenine and 3-methylcytosine residues. Surprisingly, hABH1, which displays the strongest homology
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90cdb7dab72c241fff3ad6e3647c3ab5
https://pubmed.ncbi.nlm.nih.gov/18603530
https://pubmed.ncbi.nlm.nih.gov/18603530
Autor:
Marianne Pedersen Westbye, Geir Slupphaug, Cathrine Broberg Vågbø, Hans E. Krokan, Emadoldin Feyzi, Ottar Sundheim, Per Arne Aas, Marit Otterlei
Publikováno v:
Current pharmaceutical biotechnology. 8(6)
Elaborate repair pathways counteract the deleterious effects of DNA damage by mechanisms that are understood in reasonable detail. In contrast, repair of damaged RNA has not been widely explored. This may be because aberrant RNAs are generally assume
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfd7707cd7120c85417f6cb34870ff8d
https://pubmed.ncbi.nlm.nih.gov/18289040
https://pubmed.ncbi.nlm.nih.gov/18289040
Autor:
Emadoldin Feyzi, Cathrine B. Vaagbø, Per Arne Aas, Javier Peña-Diaz, Hans E. Krokan, Bodil Kavli, Marit Otterlei, Geir Slupphaug, Finn Drabløs, Marit S Bratlie
Publikováno v:
DNA repair. 3(11)
Alkylation lesions in DNA and RNA result from endogenous compounds, environmental agents and alkylating drugs. Simple methylating agents, e.g. methylnitrosourea, tobacco-specific nitrosamines and drugs like temozolomide or streptozotocin, form adduct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d40a7c019aa0d6bc97b0ee6d5542d193
https://pubmed.ncbi.nlm.nih.gov/15380096
https://pubmed.ncbi.nlm.nih.gov/15380096
Publikováno v:
The Journal of biological chemistry. 273(22)
Heparan sulfate interacts with growth factors, matrix components, effectors and modulators of enzymatic catalysis as well as with microbial proteins via sulfated oligosaccharide domains. Although a number of such domains have been characterized, litt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddb94eec72c72df5a211dd7ca97534e7
https://pubmed.ncbi.nlm.nih.gov/9593669
https://pubmed.ncbi.nlm.nih.gov/9593669