Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Alexander Kotzsch"'
Autor:
Alexander Kotzsch, Philip Gröger, Damian Pawolski, Paul H. H. Bomans, Nico A. J. M. Sommerdijk, Michael Schlierf, Nils Kröger
Publikováno v:
BMC Biology, Vol 15, Iss 1, Pp 1-16 (2017)
Abstract Background Biological mineral formation (biomineralization) proceeds in specialized compartments often bounded by a lipid bilayer membrane. Currently, the role of membranes in biomineralization is hardly understood. Results Investigating bio
Externí odkaz:
https://doaj.org/article/d31f0ad9051c4675948680ceb9a76a09
Publikováno v:
PLoS ONE, Vol 5, Iss 9, p e744 (2010)
BACKGROUND: Members of the TGF-β superfamily are characterized by a highly promiscuous ligand-receptor interaction as is readily apparent from the numeral discrepancy of only seven type I and five type II receptors available for more than 40 ligands
Externí odkaz:
https://doaj.org/article/3631c65af937427b94eff47b4e9c1c23
Autor:
Nicole Poulsen, Damian Pawolski, Nils Kröger, Alexander Milentyev, Anna Shevchenko, Alexander Kotzsch, Andrej Shevchenko, André Scheffel
Publikováno v:
Journal of Biological Chemistry. 291:4982-4997
The nano- and micropatterned biosilica cell walls of diatoms are remarkable examples of biological morphogenesis and possess highly interesting material properties. Only recently has it been demonstrated that biosilica-associated organic structures w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cd75ef990ead04579aabf9cb04499df
https://doi.org/10.1074/jbc.m115.706440
https://doi.org/10.1074/jbc.m115.706440
Autor:
Nils Kröger, Damian Pawolski, Michael Schlierf, Alexander Kotzsch, Nico A. J. M. Sommerdijk, Philip Gröger, Phh Paul Bomans
Publikováno v:
BMC Biology
BMC Biology, 15(1):65, 1-16. BioMed Central
BMC Biology, Vol 15, Iss 1, Pp 1-16 (2017)
BMC Biology, 15(1):65, 1-16. BioMed Central
BMC Biology, Vol 15, Iss 1, Pp 1-16 (2017)
Background Biological mineral formation (biomineralization) proceeds in specialized compartments often bounded by a lipid bilayer membrane. Currently, the role of membranes in biomineralization is hardly understood. Results Investigating biomineraliz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b945f2a79f644b3a3f19d4d5560e398a
https://doi.org/10.1186/s12915-017-0400-8
https://doi.org/10.1186/s12915-017-0400-8
Autor:
Jens Berthelsen, Simon Thye Andersen, Kanchan Devkota, Tine Skovgaard, Alexander Kotzsch, Uwe Buus
Publikováno v:
Analytical Biochemistry. 452:34-42
ADAM12 belongs to the A disintegrin and metalloprotease (ADAM) family of secreted sheddases activating extracellular growth factors such as epidermal growth factor receptor (EGFR) ligands and tumor necrosis factor-alpha (TNF-α). ADAM proteases, most
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bda259fa2ad5ba3c3ecb7badd23dee1
https://doi.org/10.1016/j.ab.2014.02.008
https://doi.org/10.1016/j.ab.2014.02.008
Autor:
Marie Kveiborg, Julie B. Noer, Jens Berthelsen, Pauliina Kronqvist, Marie Christine Klitgaard, Reidar Albrechtsen, Alexander Kotzsch, Carl P. Blobel, Ulla M. Wewer, Camilla Fröhlich, Camilla Nehammer
Publikováno v:
Biochemical Journal. 452:97-109
ADAM (a disintegrin and metalloproteinase) 12 is a metalloprotease implicated in cancer progression. ADAM12 can activate membrane-anchored proteins, such as sonic hedgehog, Delta-like 1 and certain epidermal growth factor receptor ligands, through a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd6cad5552e52730cc4bbc05af58c4c2
https://doi.org/10.1042/bj20121558
https://doi.org/10.1042/bj20121558
Publikováno v:
Protein Expression and Purification. 77:104-111
Soluble expression of proteins in a relevant form for functional and structural investigations still often remains a challenge. Although many biochemical factors are known to affect solubility, a thorough investigation of yield-limiting factors is no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a437a6739d458f9abc1301f249ab9d6
https://doi.org/10.1016/j.pep.2010.11.016
https://doi.org/10.1016/j.pep.2010.11.016
Autor:
Michael Sundström, Alexander Kotzsch, J. Weigelt, Erik Vernet, Susanne Gräslund, Martin Hammarström, Jens Berthelsen
Publikováno v:
Protein Science. 20:597-609
Escherichia coli represents a robust, inexpensive expression host for the production of recombinant proteins. However, one major limitation is that certain protein classes do not express well in a biologically relevant form using standard expression
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e14328e969fe81fdc29aef07469f7862
https://doi.org/10.1002/pro.593
https://doi.org/10.1002/pro.593
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:779-783
The ligand-receptor complex of GDF5 bound to its type I and type II receptors BRIB and ActRIIB was produced and crystallized. Crystals of the GDF5-BRIB complex could only be obtained if a ternary complex comprising GDF5, BRIB and the extracellular do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::213ad8f7ad8a3f669fdfb9184d4a1bda
https://doi.org/10.1107/s1744309109024142
https://doi.org/10.1107/s1744309109024142
Publikováno v:
Molecular Pharmacology. 76:275-289
We have shown previously that Leu447 and Gln448 in the transmembrane helix (TMH) 10 of rat organic cation transporter rOCT1 are critical for inhibition of cation uptake by corticosterone. Here, we tested whether the affinity of corticosterone is diff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22acf1bef68acfcb3e3b58c417ed0f67
https://doi.org/10.1124/mol.109.054783
https://doi.org/10.1124/mol.109.054783