Zobrazeno 1 - 10
of 133
pro vyhledávání: '"Flemming M. Poulsen"'
Autor:
Morten F Gjerstorff, Heike I Rösner, Christina B Pedersen, Katrine B V Greve, Steffen Schmidt, Katherine L Wilson, Jan Mollenhauer, Hüseyin Besir, Flemming M Poulsen, Niels Erik Møllegaard, Henrik J Ditzel
Publikováno v:
PLoS ONE, Vol 7, Iss 9, p e45819 (2012)
GAGE proteins are highly similar, primate-specific molecules with unique primary structure and undefined cellular roles. They are restricted to cells of the germ line in adult healthy individuals, but are broadly expressed in a wide range of cancers.
Externí odkaz:
https://doaj.org/article/caa21b9d79494282bf95567b6de2f1c9
Autor:
Flemming M. Poulsen, Ulrik Gether, Simon Erlendsson, Kenneth L. Madsen, Kaare Teilum, Pétur O. Heidarsson, Mette Rathje
Publikováno v:
Journal of Biological Chemistry. 289:25327-25340
PDZ domain proteins control multiple cellular functions by governing assembly of protein complexes. It remains unknown why individual PDZ domains can bind the extreme C terminus of very diverse binding partners and maintain selectivity. By employing
Publikováno v:
Journal of Proteome Research
Protein digestion is an integral part of the "shotgun" proteomics approach and commonly requires overnight incubation prior to mass spectrometry analysis. Quadruplicate "shotgun" proteomic analysis of whole yeast lysate demonstrated that Guanidine-Hy
Autor:
Guido Tiana, Birthe B. Kragelund, Carlo Camilloni, Immanuel Valpapuram, Ciro Cecconi, Alberto Imparato, Pétur O. Heidarsson, Flemming M. Poulsen
Publikováno v:
Heidarsson, P O, Valpapuram, I, Camilloni, C, Imparato, A, Tiana, G, Poulsen, F M, Kragelund, B B & Cecconi, C 2012, ' A highly compliant protein native state with a spontaneous-like mechanical unfolding pathway ', Journal of American Chemical Society, vol. 134, no. 41, pp. 17068-17075 . https://doi.org/10.1021/ja305862m
Journal of the American Chemical Society
134 (2012): 17068–17075. doi:10.1021/ja305862m
info:cnr-pdr/source/autori:Heidarsson P.O.[ 2 ] ; Valpapuram I.[1]; Camilloni C.[ 4 ]; Imparato A.[ 5 ]; Tiana G.[ 3 ]; Poulsen F.M.[ 2 ] ; Kragelund B.B.[ 2 ]; Cecconi C.[ 1 ]/titolo:A highly compliant protein native state with a spontaneous-like mechanical unfolding pathway/doi:10.1021%2Fja305862m/rivista:Journal of the American Chemical Society (Print)/anno:2012/pagina_da:17068/pagina_a:17075/intervallo_pagine:17068–17075/volume:134
Journal of the American Chemical Society
134 (2012): 17068–17075. doi:10.1021/ja305862m
info:cnr-pdr/source/autori:Heidarsson P.O.[ 2 ] ; Valpapuram I.[1]; Camilloni C.[ 4 ]; Imparato A.[ 5 ]; Tiana G.[ 3 ]; Poulsen F.M.[ 2 ] ; Kragelund B.B.[ 2 ]; Cecconi C.[ 1 ]/titolo:A highly compliant protein native state with a spontaneous-like mechanical unfolding pathway/doi:10.1021%2Fja305862m/rivista:Journal of the American Chemical Society (Print)/anno:2012/pagina_da:17068/pagina_a:17075/intervallo_pagine:17068–17075/volume:134
The mechanical properties of proteins and their force-induced structural changes play key roles in many biological processes. Previous studies have shown that natively folded proteins are brittle under tension, unfolding after small mechanical deform
Autor:
Janne Nielsen, Ole R. Clausen, Lene Kohler, Michelle D. Gjørlund, Claus Christensen, Flemming M. Poulsen, Lanjun Zhang, Kristian Rohde, Vladimir Berezin, Elisabeth Bock, Kirsten Borup Bojesen, Shizhong Li, Steen Nielbo
Publikováno v:
Journal of Biological Chemistry; Vol 287
Nectins belong to a family of immunoglobulin (Ig)-like cell-adhesion molecules comprising four members, nectin-1 through nectin-4. Nectins are involved in formation of the mechanical adhesive puncta adherentia junctions of synapses. Nectins share the
Publikováno v:
Biophysical Journal. 102(7):1627-1635
The nuclear coactivator binding domain of CREB binding protein folds into remarkably different structures in complex with different ligands. To understand the mechanism of the structural adaptability in the nuclear coactivator binding domain (NCBD),
Autor:
Ida J. Bjerrum-Bohr, Birthe B. Kragelund, Gitte A. Jensen, Flemming M. Poulsen, Olaf Pongs, Bryan E. Finn, Pétur O. Heidarsson
Publikováno v:
Journal of Molecular Biology. 417:51-64
Neuronal calcium sensor 1 (NCS-1) and orthologs are expressed in all organisms from yeast to humans. In the latter, NCS-1 plays an important role in neurotransmitter release and interacts with a plethora of binding partners mostly through a large sol
Autor:
Magnus Kjaergaard, Flemming M. Poulsen
Publikováno v:
Progress in Nuclear Magnetic Resonance Spectroscopy. 60:42-51
Autor:
Magnus Kjaergaard, Flemming M. Poulsen
Publikováno v:
Journal of Biomolecular NMR. 50:157-165
Random coil chemical shifts are necessary for secondary chemical shift analysis, which is the main NMR method for identification of secondary structure in proteins. One of the largest challenges in the determination of random coil chemical shifts is
Publikováno v:
Journal of Biomolecular NMR. 49:139-149
Secondary chemical shift analysis is the main NMR method for detection of transiently formed secondary structure in intrinsically disordered proteins. The quality of the secondary chemical shifts is dependent on an appropriate choice of random coil c