M. Oliveberg

发表

Global structural motions from the strain of a single hydrogen bond

J. Danielsson, W. Awad, K. Saraboji, 2013, Proceedings of the National Academy of Sciences.

SOD1‐associated ALS: A promising system for elucidating the origin of protein‐misfolding disease

Anna Nordlund, M. Oliveberg, Anna Nordlund, 2008, HFSP journal.

Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: evidence for residual electrostatic interactions in the acid/thermally denatured state.

A. Fersht, S. Vuilleumier, M. Oliveberg, 1994, Biochemistry.

Perturbed pKA-values in the denatured states of proteins.

A. Fersht, B. Davis, M. Oliveberg, 1995, Journal of molecular biology.

pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds.

V L Arcus, A. Fersht, V. Arcus, 1995, Biochemistry.

Negative activation enthalpies in the kinetics of protein folding.

A. Fersht, M. Oliveberg, Y. Tan, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Changes of Protein Folding Pathways by Circular Permutation

Ellinor Haglund, M. Oliveberg, E. Haglund, 2008, Journal of Biological Chemistry.

Titration properties and thermodynamics of the transition state for folding: comparison of two-state and multi-state folding pathways.

A. Fersht, M. Oliveberg, Y. Tan, 1996, Journal of molecular biology.

Waltz, an exciting new move in amyloid prediction

M. Oliveberg, 2010, Nature Methods.

The experimental survey of protein-folding energy landscapes

P. Wolynes, M. Oliveberg, 2005, Quarterly Reviews of Biophysics.

Tryptophan-BODIPY: a versatile donor-acceptor pair for probing generic changes of intraprotein distances.

S. Kalinin, M. Oliveberg, L. Johansson, 2006, Physical chemistry chemical physics : PCCP.

The Cost of Long Catalytic Loops in Folding and Stability of the ALS-Associated Protein SOD1.

J. Danielsson, D. Logan, M. Oliveberg, 2018, Journal of the American Chemical Society.

Complete change of the protein folding transition state upon circular permutation

Jeanette Tångrot, M. Oliveberg, M. Lindberg, 2002, Nature Structural Biology.

Comparing protein behaviour in vitro and in vivo, what does the data really tell us?

J. Danielsson, M. Oliveberg, 2017, Current opinion in structural biology.

The pierced lasso topology leptin has a bolt on dynamic domain composed by the disordered loops I and III.

J. Onuchic, J. Noel, P. Jennings, 2020, Journal of molecular biology.

Physicochemical code for quinary protein interactions in Escherichia coli

N. Dokholyan, J. Danielsson, Lisa Lang, 2017, Proceedings of the National Academy of Sciences.

Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry

E. Marklund, C. Robinson, A. Laganowsky, 2021, JACS Au.

Structural insights into HetR−PatS interaction involved in cyanobacterial pattern formation

Qingfa Wu, M. Oliveberg, Zhiyong Zhang, 2015, Scientific Reports.

Internal electron transfer in cytochrome c oxidase: evidence for a rapid equilibrium between cytochrome a and the bimetallic site.

M. Oliveberg, B. Malmström, 1991, Biochemistry.

Indications that Amorphous Calcium Carbonates Occur in Pathological Mineralisation—A Urinary Stone from a Guinea Pig

M. Oliveberg, N. Hedin, D. Gebauer, 2018 .

Physicochemical classification of organisms

M. Oliveberg, Eloy Vallina Estrada, 2022, Proceedings of the National Academy of Sciences of the United States of America.

Cytotoxicity of Superoxide Dismutase 1 in Cultured Cells Is Linked to Zn2+ Chelation

J. Danielsson, Lisa Lang, L. Leinartaitė, 2012, PloS one.

ALS precursor finally shaken into fibrils

J. Schymkowitz, F. Rousseau, M. Oliveberg, 2008, Proceedings of the National Academy of Sciences.

Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry

E. Marklund, C. Robinson, A. Laganowsky, 2021, JACS Au.

Structural and kinetic analysis of protein-aggregate strains in vivo using binary epitope mapping

P. Andersen, J. Danielsson, Lisa Lang, 2015, Proceedings of the National Academy of Sciences.

On the osmotic pressure of cells

M. Oliveberg, H. Wennerström, 2022, QRB Discovery.

The effect of pH and temperature on the reaction of fully reduced and mixed-valence cytochrome c oxidase with dioxygen.

M. Oliveberg, P. Brzezinski, B. Malmström, 1989, Biochimica et biophysica acta.

Uptake and release of protons during the reaction between cytochrome c oxidase and molecular oxygen: a flow-flash investigation.

M. Oliveberg, T. Nilsson, S. Hallén, 1991, Biochemistry.

Reaction of dioxygen with cytochrome c oxidase reduced to different degrees: indications of a transient dioxygen complex with copper-B.

M. Oliveberg, B. Malmström, 1992, Biochemistry.

Rapid proton release during flash‐induced oxidation of cytochrome c oxidase

M. Oliveberg, T. Nilsson, S. Hallén, 1990 .

From snapshot to movie: phi analysis of protein folding transition states taken one step further.

M. Akke, M. Oliveberg, U. Mayor, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly.

D. Otzen, M. Oliveberg, O. Kristensen, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Formation of electrostatic interactions on the protein-folding pathway.

A. Fersht, M. Oliveberg, 1996, Biochemistry.

Amyotrophic Lateral Sclerosis-associated Copper/Zinc Superoxide Dismutase Mutations Preferentially Reduce the Repulsive Charge of the Proteins*

P. Andersen, S. Marklund, M. Oliveberg, 2007, Journal of Biological Chemistry.

Functional features cause misfolding of the ALS-provoking enzyme SOD1

J. Danielsson, K. Saraboji, L. Leinartaitė, 2009, Proceedings of the National Academy of Sciences.

Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models.

P. Andersen, S. Marklund, M. Oliveberg, 2006, Brain : a journal of neurology.

A biosensor-based framework to measure latent proteostasis capacity

M. Oliveberg, A. Dickson, S. Ebbinghaus, 2018, Nature Communications.

Conformational plasticity in folding of the split β-α-β protein S6: evidence for burst-phase disruption of the native state

Daniel E. Otzen, D. Otzen, M. Oliveberg, 2002 .

Solid-state NMR studies of metal-free SOD1 fibrillar structures

C. Luchinat, J. Danielsson, M. Oliveberg, 2014, JBIC Journal of Biological Inorganic Chemistry.

Structural changes in the transition state of protein folding: alternative interpretations of curved chevron plots.

M. Proctor, D. Otzen, M. Oliveberg, 1999, Biochemistry.

Thermodynamics of protein destabilization in live cells

J. Danielsson, D. Logan, M. Oliveberg, 2015, Proceedings of the National Academy of Sciences.

Salt-induced detour through compact regions of the protein folding landscape.

D. Otzen, M. Oliveberg, Daniel E. Otzen, 1999, Proceedings of the National Academy of Sciences of the United States of America.

SOD1 aggregation in ALS mice shows simplistic test tube behavior

J. Danielsson, S. Marklund, M. Oliveberg, 2015, Proceedings of the National Academy of Sciences.

Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons.

Sebastian Hansson, Derek T Logan, D. Logan, 2006, Journal of molecular biology.

Direct detection of neuropeptide dynorphin A binding to the second extracellular loop of the κ opioid receptor using a soluble protein scaffold

J. Danielsson, M. Kurnik, M. Oliveberg, 2014, The FEBS journal.

Cutting Off Functional Loops from Homodimeric Enzyme Superoxide Dismutase 1 (SOD1) Leaves Monomeric β-Barrels*

J. Danielsson, M. Kurnik, M. Oliveberg, 2011, The Journal of Biological Chemistry.

Protein folding: Defining a “standard” set of experimental conditions and a preliminary kinetic data set of two‐state proteins

Kevin W Plaxco, Ingo Ruczinski, Fabrizio Chiti, 2005, Protein science : a publication of the Protein Society.

Diffusive protein interactions in human versus bacterial cells

J. Danielsson, M. Oliveberg, X. Mu, 2020, Current research in structural biology.

Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks.

A. Fersht, J. Clarke, M. Oliveberg, 1997, Journal of molecular biology.

The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase.

S. Marklund, D. Logan, M. Oliveberg, 2007, Journal of molecular biology.

A biosensor-based framework to measure latent proteostasis capacity

M. Oliveberg, A. Dickson, S. Ebbinghaus, 2018, Nature Communications.

Light‐induced structural changes in cytochrome c oxidase

M. Oliveberg, P. Brzezinski, M Oliveberg, 1993, FEBS Letters.

Exposure of a cryptic Hsp70 binding site determines the cytotoxicity of the ALS-associated SOD1-mutant A4V.

Nikolaos N. Louros, W. Robberecht, Jacinte Beerten, 2019, Protein engineering, design & selection : PEDS.

Folding catalysis by transient coordination of Zn2+ to the Cu ligands of the ALS-associated enzyme Cu/Zn superoxide dismutase 1.

K. Saraboji, L. Leinartaitė, D. Logan, 2010, Journal of the American Chemical Society.

Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: Parallels to precursors in amyloid disease

M. Oliveberg, A. Nordlund, 2006, Proceedings of the National Academy of Sciences.

Polyanions Cause Protein Destabilization Similar to That in Live Cells

J. Danielsson, M. Oliveberg, S. Leeb, 2021, Biochemistry.

Connecting Longitudinal and Transverse Relaxation Rates in Live-Cell NMR

J. Danielsson, M. Oliveberg, Fan Yang, 2020, The journal of physical chemistry. B.

Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins

J. Danielsson, D. Logan, M. Oliveberg, 2020, Proceedings of the National Academy of Sciences.

Colloidal stability of the living cell

J. Danielsson, M. Oliveberg, H. Wennerström, 2020, Proceedings of the National Academy of Sciences.

Tricking a Protein To Swap Strands.

J. Danielsson, D. Logan, M. Oliveberg, 2016, Journal of the American Chemical Society.

Pruning the ALS-associated protein SOD1 for in-cell NMR.

M. Shirakawa, J. Danielsson, M. Oliveberg, 2013, Journal of the American Chemical Society.

Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium

J. Danielsson, M. Kurnik, M. Oliveberg, 2012, Proceedings of the National Academy of Sciences.

Folding without charges

J. Danielsson, M. Kurnik, M. Oliveberg, 2012, Proceedings of the National Academy of Sciences.

SOD1 Mutations Targeting Surface Hydrogen Bonds Promote Amyotrophic Lateral Sclerosis without Reducing Apo-state Stability*

P. Andersen, M. Oliveberg, G. Gröbner, 2010, The Journal of Biological Chemistry.

Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS models

P. Andersen, S. Marklund, M. Oliveberg, 2007, Proceedings of the National Academy of Sciences.

Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers.

A. Holmgren, M. Oliveberg, Mikael Oliveberg, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Folding intermediates of wild-type and mutants of barnase. I. Use of phi-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium.

A. Fersht, P. Dalby, M. Oliveberg, 1998, Journal of molecular biology.

Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization

M. Akke, Melanie H. Smith, E. Schulz, 2009, Proceedings of the National Academy of Sciences.

Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants.

Peter M Andersen, P. Andersen, M. Oliveberg, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state

L. Tibell, M. Oliveberg, M. Lindberg, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Malleability of protein folding pathways: a simple reason for complex behaviour.

M. Oliveberg, M. Lindberg, Mikael Oliveberg, 2007, Current opinion in structural biology.

Identification of the minimal protein-folding nucleus through loop-entropy perturbations.

Eugene I Shakhnovich, Ellinor Haglund, E. Shakhnovich, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Conformational plasticity in folding of the split beta-alpha-beta protein S6: evidence for burst-phase disruption of the native state.

D. Otzen, M. Oliveberg, Mikael Oliveberg, 2002, Journal of molecular biology.

Mutant SOD1 aggregates formed in vitro and in cultured cells are polymorphic and differ from those arising in the CNS

J. Danielsson, M. Oliveberg, P. Andersen, 2022, Journal of neurochemistry.

Formation of short-lived protein aggregates directly from the coil in two-state folding.

A. Fersht, M. Oliveberg, Y. Tan, 1999, Biochemistry.

Trimming Down a Protein Structure to Its Bare Foldons

Ellinor Haglund, Derek T Logan, J. Danielsson, 2011, The Journal of Biological Chemistry.

The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway

M. Oliveberg, E. Haglund, Tommy Öman, 2009, Proceedings of the National Academy of Sciences.

A simple way to measure protein refolding rates in water.

D. Otzen, M. Oliveberg, 2001, Journal of molecular biology.

Burst-phase expansion of native protein prior to global unfolding in SDS.

D. Otzen, M. Oliveberg, 2002, Journal of molecular biology.

Characterisation of the transition states for protein folding: towards a new level of mechanistic detail in protein engineering analysis.

M. Oliveberg, 2001, Current opinion in structural biology.

The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding.

A. Fersht, M. Oliveberg, Y. Tan, 1998, Journal of molecular biology.

High-energy channeling in protein folding.

M. Oliveberg, M Oliveberg, M. Silow, 1997, Biochemistry.

Folding of circular permutants with decreased contact order: general trend balanced by protein stability.

A. V. Finkelstein, D. Otzen, M. Oliveberg, 2001, Journal of molecular biology.

The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2.

A. Fersht, D. Otzen, M. Oliveberg, 1997, Journal of molecular biology.

Transient aggregates in protein folding are easily mistaken for folding intermediates.

M. Oliveberg, M. Silow, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Transient formation of nano‐crystalline structures during fibrillation of an Aβ‐like peptide

D. Otzen, M. Oliveberg, 2004, Protein science : a publication of the Protein Society.

Diffusive intracellular interactions: On the role of protein net charge and functional adaptation.

J. Danielsson, M. Oliveberg, H. Wennerström, 2023, Current opinion in structural biology.

Diffuse binding of Zn2+ to the denatured ensemble of Cu/Zn superoxide dismutase 1

M. Oliveberg, S. Szpryngiel, Lena Mäler, 2015, FEBS open bio.

Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins

P. Andersen, S. Marklund, M. Oliveberg, 2007 .

Chapter 11. In-cell NMR: Spectral Optimization and Population Adjustment by Rational Protein Engineering

J. Danielsson, M. Oliveberg, Fan Yang, 2019, New Developments in NMR.

Thermodynamics of transient conformations in the folding pathway of barnase: reorganization of the folding intermediate at low pH.

A. Fersht, M. Oliveberg, Mikael Oliveberg, 1996, Biochemistry.

Common motifs and topological effects in the protein folding transition state.

Eugene I Shakhnovich, Ellinor Haglund, E. Shakhnovich, 2006, Journal of molecular biology.

Simulation, experiment, and evolution: understanding nucleation in protein S6 folding.

E. Shakhnovich, I. Hubner, M. Oliveberg, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Correspondence between anomalous m‐ and Δ Cp‐values in protein folding

D. Otzen, M. Oliveberg, 2004 .

Solid-state NMR studies of metal-free SOD1 fibrillar structures

C. Luchinat, J. Danielsson, M. Oliveberg, 2014, JBIC Journal of Biological Inorganic Chemistry.

Cutting Off Functional Loops from Homodimeric Enzyme Superoxide Dismutase 1 (SOD1) Leaves Monomeric β-Barrels*

J. Danielsson, M. Kurnik, M. Oliveberg, 2011, Journal of Biological Chemistry.

Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization

M. Akke, Melanie H. Smith, E. Schulz, 2009, Proceedings of the National Academy of Sciences.

Pruning the ALS-associated protein SOD1 for in-cell NMR.

M. Shirakawa, J. Danielsson, M. Oliveberg, 2013, Journal of the American Chemical Society.

High concentrations of viscogens decrease the protein folding rate constant by prematurely collapsing the coil.

M. Oliveberg, M. Silow, 2003, Journal of molecular biology.

Adsorption of a small protein to a methyl-terminated hydrophobic surfaces: effect of protein-folding thermodynamics and kinetics

Daniel E. Otzen, Fredrik Höök, D. Otzen, 2003 .

Scanning malleable transition state ensembles: comparing theory and experiment for folding protein U1A.

Peter G Wolynes, Tongye Shen, P. Wolynes, 2005, Biochemistry.