Characterization of binding between model protein GA-Z and human serum albumin using asymmetrical flow field-flow fractionation and small angle X-ray scattering.

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

Characterization of binding between model protein GA-Z and human serum albumin using asymmetrical flow field-flow fractionation and small angle X-ray scattering

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 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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68d143a92df0de59b94ffd0e3d473d5d
https://doaj.org/article/a1937eb382f24beea50a687c2acd3d1f

Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface

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

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

Architecture of the Yeast Mitochondrial Iron-Sulfur Cluster Assembly Machinery

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

Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120

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)

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