Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Dirk Roeser"'
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e81926 (2013)
The amyloid precursor protein (APP) and its processing by the α-, β- and γ-secretases is widely believed to play a central role during the development of Alzheimer´s disease. The three-dimensional structure of the entire protein, its physiologic
Externí odkaz:
https://doaj.org/article/db98e990c52943a7b53f1f35bda64cd5
Autor:
Miriam Böhm, Kornelia Hardes, Charlotte A. Bäuml, Dirk Roeser, Manuel E. Than, Torsten Steinmetzer, Diana Imhof, Arijit Biswas, Yvonne Schaub
Publikováno v:
Journal of Medicinal Chemistry. 57:10355-10365
The inhibition of the final step in blood coagulation, the factor XIIIa (FXIIIa) catalyzed cross-linking of fibrin monomers, is currently still a challenge in medicinal chemistry. We report synthesis, recombinant expression, disulfide connectivity, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b5307f8426e19e3c2a8aa987aee689b
https://doi.org/10.1021/jm501058g
https://doi.org/10.1021/jm501058g
Publikováno v:
Journal of Structural Biology. 187(1):30-37
The amyloid precursor protein (APP) and its cellular processing are believed to be centrally involved in the etiology of Alzheimer’s disease (AD). In addition, many physiological functions have been described for APP, including a role in cell–cel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::919416b1e4db096c1d1b80718bf38ef9
Autor:
Yvonne Schaub, Diana Imhof, Wibke E. Diederich, Torsten Steinmetzer, Kornelia Hardes, Manuel E. Than, Nina Klee, Patrick Maeder, Ina Coburger, Dirk Roeser
Publikováno v:
MicrobiologyOpen, 5(4): 637-646
MicrobiologyOpen
MicrobiologyOpen
GxGD‐type intramembrane cleaving proteases (I‐CLiPs) form a family of proteolytic enzymes that feature an aspartate‐based catalytic mechanism. Yet, they structurally and functionally largely differ from the classical pepsin‐like aspartic prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1100b48ac5947e04fd78a97147ba5987
https://repository.publisso.de/resource/frl:6402526
https://repository.publisso.de/resource/frl:6402526
Publikováno v:
Journal of Molecular Biology. 409:189-201
Death receptors belong to the tumor necrosis factor receptor (TNFR) super family and are intimately involved in the signal transduction during apoptosis, stress response and cellular survival. Here we present the crystal structure of recombinantly ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57013a2c31aa8b3691b7685e038e88dc
https://doi.org/10.1016/j.jmb.2011.03.048
https://doi.org/10.1016/j.jmb.2011.03.048
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 63:621-627
The catalytic residue in sulfatases is a unique formylglycine that is post-translationally generated by oxidation of a cysteine or serine precursor. Molecular oxygen oxidizes the cysteine precursor in eukaryotic sulfatases, a reaction that is catalys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9d56f1fb64da9c184c9baae98dbcd22
https://doi.org/10.1107/s0907444907009961
https://doi.org/10.1107/s0907444907009961
Autor:
Andrea Preusser-Kunze, Kathrin Gasow, Thomas Dierks, Bernhard Schmidt, Dirk Roeser, Kurt von Figura, Julia G. Wittmann, Markus G. Rudolph
Publikováno v:
Proceedings of the National Academy of Sciences. 103:81-86
The formylglycine (FGly)-generating enzyme (FGE) uses molecular oxygen to oxidize a conserved cysteine residue in all eukaryotic sulfatases to the catalytically active FGly. Sulfatases degrade and remodel sulfate esters, and inactivity of FGE results
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36829f005204dc2c542efeabfeb85f1f
https://doi.org/10.1073/pnas.0507592102
https://doi.org/10.1073/pnas.0507592102
Autor:
Michael Schaefer, Linda Schauenburg, Daniela Kaden, Manuel E. Than, Gerhard Multhaup, Dirk Roeser, Christian Barucker, Magnus C. Mayer, Philipp Voigt, Mark A. Hancock
Publikováno v:
The Journal of biological chemistry. 289(27)
The amyloid precursor protein (APP) and the APP-like proteins 1 and 2 (APLP1 and APLP2) are a family of multidomain transmembrane proteins possessing homo- and heterotypic contact sites in their ectodomains. We previously reported that divalent metal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c992d6c5764a12cda52432fc36a1c2e
https://pubmed.ncbi.nlm.nih.gov/24855651
https://pubmed.ncbi.nlm.nih.gov/24855651
Autor:
Peter Hortschansky, Karl-Heinz Gührs, Manuel E. Than, Ina Coburger, Dirk Roeser, Sven O. Dahms
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 12, p e81926 (2013)
PLoS ONE, Vol 8, Iss 12, p e81926 (2013)
The amyloid precursor protein (APP) and its processing by the α-, β- and γ-secretases is widely believed to play a central role during the development of Alzheimer´s disease. The three-dimensional structure of the entire protein, its physiologic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec873063758e60da05a24346e5fb2473
http://europepmc.org/articles/PMC3852973
http://europepmc.org/articles/PMC3852973
Autor:
Sven O. Dahms, Magnus C. Mayer, Gerd Multhaup, Ina Könnig, Manuel E. Than, Dirk Roeser, Karl-Heinz Gührs, Daniela Kaden
Publikováno v:
Journal of molecular biology. 416(3)
The amyloid precursor protein (APP) and its neurotoxic cleavage product Aβ are key players in the development of Alzheimer's disease and appear essential for neuronal development and cell homeostasis in mammals. Proteolytic processing of APP is infl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a90c05095c7c0cb5851b67ab45f1a1db
https://pubmed.ncbi.nlm.nih.gov/22245578
https://pubmed.ncbi.nlm.nih.gov/22245578