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» Authors » Christopher A G Soderberg

Christopher A G Soderberg

Explore the profile of Christopher A G Soderberg including associated specialties, affiliations and a list of published articles. Areas
Snapshot
Articles 15
Citations 148
Followers 0
Related Specialties
Biochemistry
Science
Molecular Biology
Top 10 Co-Authors
Salam Al-Karadaghi
Gudrun Rutsdottir
Cecilia Emanuelsson
Sreekanth Rajan
Oleksandr Gakh
Grazia Isaya
Peter Hojrup
Michael Hall
Cecilia Mansson
Roland Locmelis
Published In
Sci Rep
J Biol Chem
PLoS One
Methods Enzymol
J Biol Inorg Chem
Affiliations
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Recent Articles
1.
Characterization of binding between model protein GA-Z and human serum albumin using asymmetrical flow field-flow fractionation and small angle X-ray scattering
Choi J, Wahlgren M, Ek V, Elofsson U, Fransson J, Nilsson L, et al.
PLoS One . 2020 Nov; 15(11):e0242605. PMID: 33232370
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...
2.
Author Correction: Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120
Mishra Y, Hall M, Locmelis R, Nam K, Soderberg C, Storm P, et al.
Sci Rep . 2018 Jun; 8(1):8658. PMID: 29855503
A correction to this article has been published and is linked from the HTML and PDF versions of this paper. The error has been fixed in the paper.
3.
Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface
Soderberg C, Mansson C, Bernfur K, Rutsdottir G, Harmark J, Rajan S, et al.
Sci Rep . 2018 Mar; 8(1):5199. PMID: 29581438
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...
4.
Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7210
Mishra Y, Hall M, Locmelis R, Nam K, Soderberg C, Storm P, et al.
Sci Rep . 2017 Dec; 7(1):17151. PMID: 29215017
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)...
5.
Chaperone-client interactions between Hsp21 and client proteins monitored in solution by small angle X-ray scattering and captured by crosslinking mass spectrometry
Rutsdottir G, Rasmussen M, Hojrup P, Bernfur K, Emanuelsson C, Soderberg C
Proteins . 2017 Oct; 86(1):110-123. PMID: 29082555
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...
6.
Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity
Rutsdottir G, Harmark J, Weide Y, Hebert H, Rasmussen M, Wernersson S, et al.
J Biol Chem . 2017 Mar; 292(19):8103-8121. PMID: 28325834
Small heat-shock proteins (sHsps) prevent aggregation of thermosensitive client proteins in a first line of defense against cellular stress. The mechanisms by which they perform this function have been hard...
7.
Architecture of the Yeast Mitochondrial Iron-Sulfur Cluster Assembly Machinery: THE SUB-COMPLEX FORMED BY THE IRON DONOR, Yfh1 PROTEIN, AND THE SCAFFOLD, Isu1 PROTEIN
Ranatunga W, Gakh O, Galeano B, Smith 4th D, Soderberg C, Al-Karadaghi S, et al.
J Biol Chem . 2016 Mar; 291(19):10378-98. PMID: 26941001
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...
8.
The molecular basis of iron-induced oligomerization of frataxin and the role of the ferroxidation reaction in oligomerization
Soderberg C, Rajan S, Shkumatov A, Gakh O, Schaefer S, Ahlgren E, et al.
J Biol Chem . 2013 Jan; 288(12):8156-8167. PMID: 23344952
The role of the mitochondrial protein frataxin in iron storage and detoxification, iron delivery to iron-sulfur cluster biosynthesis, heme biosynthesis, and aconitase repair has been extensively studied during the last...
9.
Detection of crosslinks within and between proteins by LC-MALDI-TOFTOF and the software FINDX to reduce the MSMS-data to acquire for validation
Soderberg C, Lambert W, Kjellstrom S, Wiegandt A, Wulff R, Mansson C, et al.
PLoS One . 2012 Jun; 7(6):e38927. PMID: 22723907
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...
10.
Oligomerization propensity and flexibility of yeast frataxin studied by X-ray crystallography and small-angle X-ray scattering
Soderberg C, Shkumatov A, Rajan S, Gakh O, Svergun D, Isaya G, et al.
J Mol Biol . 2011 Nov; 414(5):783-97. PMID: 22051511
Frataxin is a mitochondrial protein with a central role in iron homeostasis. Defects in frataxin function lead to Friedreich's ataxia, a progressive neurodegenerative disease with childhood onset. The function of...