Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Christopher A G Söderberg"'
Autor:
Jaeyeong Choi, Marie Wahlgren, Vilhelm Ek, Ulla Elofsson, Jonas Fransson, Lars Nilsson, Ann Terry, Christopher A G Söderberg
Publikováno v:
PLoS ONE, Vol 15, Iss 11, p e0242605 (2020)
Protein-based drugs often require targeted drug delivery for optimal therapy. A successful strategy to increase the circulation time of the protein in the blood is to link the therapeutic protein with an albumin-binding domain. In this work, we chara
Externí odkaz:
https://doaj.org/article/a1937eb382f24beea50a687c2acd3d1f
Autor:
Christopher A G Söderberg, Wietske Lambert, Sven Kjellström, Alena Wiegandt, Ragna Peterson Wulff, Cecilia Månsson, Gudrun Rutsdottir, Cecilia Emanuelsson
Publikováno v:
PLoS ONE, Vol 7, Iss 6, p e38927 (2012)
Lysine-specific chemical crosslinking in combination with mass spectrometry is emerging as a tool for the structural characterization of protein complexes and protein-protein interactions. After tryptic digestion of crosslinked proteins there are tho
Externí odkaz:
https://doaj.org/article/42df66698a444a6b81c119185324f8d0
Autor:
Ann E. Terry, Christopher A. G. Söderberg, Marie Wahlgren, Ulla Elofsson, Jaeyeong Choi, Lennart Nilsson, Vilhelm Ek, Jonas Fransson
Publikováno v:
PLoS ONE, Vol 15, Iss 11, p e0242605 (2020)
PLoS ONE
PLOS ONE 15(11), e0242605-(2020). doi:10.1371/journal.pone.0242605
PLoS ONE
PLOS ONE 15(11), e0242605-(2020). doi:10.1371/journal.pone.0242605
PLOS ONE 15(11), e0242605 - (2020). doi:10.1371/journal.pone.0242605
Protein-based drugs often require targeted drug delivery for optimal therapy. A successful strategy to increase the circulation time of the protein in the blood is to link the
Protein-based drugs often require targeted drug delivery for optimal therapy. A successful strategy to increase the circulation time of the protein in the blood is to link the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68d143a92df0de59b94ffd0e3d473d5d
https://doaj.org/article/a1937eb382f24beea50a687c2acd3d1f
https://doaj.org/article/a1937eb382f24beea50a687c2acd3d1f
Autor:
Christopher A. G. Söderberg, Morten Rasmussen, Cecilia Månsson, Peter Højrup, Sreekanth Rajan, Johan Härmark, Cecilia Emanuelsson, Gudrun Rutsdottir, Hans Hebert, Katja Bernfur, Salam Al-Karadaghi
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-15 (2018)
Scientific Reports
Söderberg, C A G, Månsson, C, Bernfur, K, Rutsdottir, G, Härmark, J, Rajan, S, Al-Karadaghi, S, Rasmussen, M, Höjrup, P, Hebert, H & Emanuelsson, C 2018, ' Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface ', Scientific Reports, vol. 8, 5199 . https://doi.org/10.1038/s41598-018-23035-9
Scientific Reports
Söderberg, C A G, Månsson, C, Bernfur, K, Rutsdottir, G, Härmark, J, Rajan, S, Al-Karadaghi, S, Rasmussen, M, Höjrup, P, Hebert, H & Emanuelsson, C 2018, ' Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface ', Scientific Reports, vol. 8, 5199 . https://doi.org/10.1038/s41598-018-23035-9
The remarkably efficient suppression of amyloid fibril formation by the DNAJB6 chaperone is dependent on a set of conserved S/T-residues and an oligomeric structure, features unusual among DNAJ chaperones. We explored the structure of DNAJB6 using a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85fa11983f6d5107db865657faacc02f
http://link.springer.com/article/10.1038/s41598-018-23035-9
http://link.springer.com/article/10.1038/s41598-018-23035-9
Autor:
Christian Grundahl Frankær, Christopher A. G. Söderberg, Günther H.J. Peters, Ana Labrador, Pernille Sønderby, Jens T. Bukrinski, Tomás S. Plivelic, Pernille Harris
Publikováno v:
Sønderby, P, Söderberg, C, Frankær, C G, Peters, G H J, Bukrinski, J T, Labrador, A, Plivelic, T S & Harris, P 2020, ' Concentrated protein solutions investigated using acoustic levitation and small-angle X-ray scattering ', Journal of Synchrotron Radiation, vol. 27, no. 2, pp. 396-404 . https://doi.org/10.1107/s1600577519016977
An acoustically levitated droplet has been used to collect synchrotron SAXS data on human serum albumin protein solutions up to a protein concentration of 400 mg ml−1. A careful selection of experiments allows for fast data collection of a large am
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b7cc70d192264fd4026630db19c2d68
https://pubmed.ncbi.nlm.nih.gov/32153278
https://pubmed.ncbi.nlm.nih.gov/32153278
Autor:
Grazia Isaya, Wasantha Ranatunga, Belinda K. Galeano, Salam Al-Karadaghi, Oleksandr Gakh, Douglas Y. Smith, Christopher A. G. Söderberg, James R. Thompson
Publikováno v:
Journal of Biological Chemistry. 291:10378-10398
The biosynthesis of Fe-S clusters is a vital process involving the delivery of elemental iron and sulfur to scaffold proteins via molecular interactions that are still poorly defined. We reconstituted a stable, functional complex consisting of the ir
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::699597b77acb7637ccc81b9b25585094
https://doi.org/10.1074/jbc.m115.712414
https://doi.org/10.1074/jbc.m115.712414
Autor:
Morten Rasmussen, Peter Højrup, Katja Bernfur, Gudrun Rutsdottir, Christopher A. G. Söderberg, Cecilia Emanuelsson
Publikováno v:
Rutsdottir, G, I Rasmussen, M, Hojrup, P, Bernfur, K, Emanuelsson, C & Söderberg, C A G 2018, ' Chaperone-client interactions between Hsp21 and client proteins monitored in solution by small angle X-ray scattering and captured by crosslinking mass spectrometry ', Proteins, vol. 86, no. 1, pp. 110-123 . https://doi.org/10.1002/prot.25413
The small heat shock protein (sHsp) chaperones are important for stress survival, yet the molecular details of how they interact with client proteins are not understood. All sHsps share a folded middle domain to which is appended flexible N- and C-te
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ce04c52c1f9594bcf9c8f4d1b4b4256
https://portal.findresearcher.sdu.dk/da/publications/5b171911-901e-46fe-99e1-fdbbdfdfa5c7
https://portal.findresearcher.sdu.dk/da/publications/5b171911-901e-46fe-99e1-fdbbdfdfa5c7
Autor:
Christopher A. G. Söderberg, Roland Locmelis, Neha Chaurasia, Michael N. Hall, Patrik Storm, Stefan Jansson, Yogesh Mishra, Wolfgang P. Schröder, Lal Chand Rai, Kwangho Nam, Uwe Sauer
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
Peroxiredoxins (Prxs) are vital regulators of intracellular reactive oxygen species levels in all living organisms. Their activity depends on one or two catalytically active cysteine residues, the peroxidatic Cys (C-P) and, if present, the resolving
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6e28203b02c9395f430e2aeba03df62
https://doi.org/10.1038/s41598-017-17044-3
https://doi.org/10.1038/s41598-017-17044-3
Autor:
Grazia Isaya, Christopher A. G. Söderberg, Katja Bernfur, Salam Al-Karadaghi, Mostafa Fekry, Peter Højrup, Mathias Wiemann, Cecilia Emanuelsson, Olex Gakh, Morten Rasmussen, Eva-Christina Ahlgren
Publikováno v:
PLoS ONE, Vol 12, Iss 12, p e0188937 (2017)
PLoS ONE
Ahlgren, E C, Fekry, M, Wiemann, M, Söderberg, C A, Bernfur, K, Gakh, O, Rasmussen, M, Højrup, P, Emanuelsson, C, Isaya, G & Al-Karadaghi, S 2017, ' Iron-induced oligomerization of human FXN 81-210 and bacterial CyaY frataxin and the effect of iron chelators ', PLOS ONE, vol. 12, no. 12, e0188937 . https://doi.org/10.1371/journal.pone.0188937
PLoS ONE
Ahlgren, E C, Fekry, M, Wiemann, M, Söderberg, C A, Bernfur, K, Gakh, O, Rasmussen, M, Højrup, P, Emanuelsson, C, Isaya, G & Al-Karadaghi, S 2017, ' Iron-induced oligomerization of human FXN 81-210 and bacterial CyaY frataxin and the effect of iron chelators ', PLOS ONE, vol. 12, no. 12, e0188937 . https://doi.org/10.1371/journal.pone.0188937
Patients suffering from the progressive neurodegenerative disease Friedreich’s ataxia have reduced expression levels of the protein frataxin. Three major isoforms of human frataxin have been identified, FXN42-210, FXN56-210 and FXN81-210, of which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fab1be055569c2df5983d894c6495308
http://europepmc.org/articles/PMC5714350?pdf=render
http://europepmc.org/articles/PMC5714350?pdf=render
Autor:
Marek Tchórzewski, Oleksandr Gakh, Eva-Christina Ahlgren, Mostafa Fekry, Grazia Isaya, Christopher A. G. Söderberg, Wessen Alshokry, Przemysław Grela, Salam Al-Karadaghi
Publikováno v:
PLoS ONE, Vol 12, Iss 9, p e0184961 (2017)
'PloS One ', vol: 12, pages: e0184961-1-e0184961-22 (2017)
PLoS ONE
PLoS one 12(9), e0184961-(2017). doi:10.1371/journal.pone.0184961
'PloS One ', vol: 12, pages: e0184961-1-e0184961-22 (2017)
PLoS ONE
PLoS one 12(9), e0184961-(2017). doi:10.1371/journal.pone.0184961
Frataxin is a highly conserved protein found in both prokaryotes and eukaryotes. It is involved in several central functions in cells, which include iron delivery to biochemical processes, such as heme synthesis, assembly of iron-sulfur clusters (ISC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c79f650ae54172cde08053b917c2596c
http://europepmc.org/articles/PMC5607177?pdf=render
http://europepmc.org/articles/PMC5607177?pdf=render