B. Jonsson

发表

A mutant form of the ribosomal protein L1 reveals conformational flexibility

A. Liljas, N. Nevskaya, M. Garber, 1997, FEBS letters.

Protein adsorption onto silica nanoparticles: conformational changes depend on the particles' curvature and the protein stability.

Bengt-Harald Jonsson, Martin Lundqvist, B. Jonsson, 2004, Langmuir : the ACS journal of surfaces and colloids.

Applying theories of microbial metabolism for induction of targeted enzyme activity in a methanogenic microbial community at a metabolic steady state

B. Jonsson, M. Johansson, Jutta Speda, 2016, Applied Microbiology and Biotechnology.

Metaproteomics-guided selection of targeted enzymes for bioprospecting of mixed microbial communities

B. Jonsson, Jutta Speda, M. Karlsson, 2017, Biotechnology for Biofuels.

GroEL-induced topological dislocation of a substrate protein β-sheet core: a solution EPR spin–spin distance study

R. Owenius, B. Jonsson, P. Hammarström, 2010, Journal of chemical biology.

Unfolding a folding disease: folding, misfolding and aggregation of the marble brain syndrome-associated mutant H107Y of human carbonic anhydrase II.

B. Persson, J. Carlsson, B. Jonsson, 2004, Journal of molecular biology.

A 13C nuclear-magnetic-resonance study of CO2-HCO3-exchange catalyzed by human carbonic anhydrase C at chemical equilibrium.

B. Jonsson, S. Lindskog, B H Jonsson, 1979, European journal of biochemistry.

Participation of buffer in the catalytic mechanism of carbonic anhydrase

B. Jonsson, S. Lindskog, H. Steiner, 1976, FEBS letters.

Ribosomal protein L22 from Thermus thermophilus: sequencing overexpression and crystallisation

A. Liljas, M. Garber, S. Al-Karadaghi, 1995, FEBS letters.

Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan‐indole‐HN sites

B. Jonsson, P. Jonasson, I. Sethson, 1999, FEBS letters.

Purification and properties of the mercuric-ion-binding protein MerP.

B. Jonsson, L. Sahlman, 1992, European journal of biochemistry.

The equilibrium unfolding of MerP characterized by multivariate analysis of 2D NMR data.

A. Berglund, B. Jonsson, I. Sethson, 2005, Journal of magnetic resonance.

Crystallographic analysis of Thr‐200 → His human carbonic anhydrase II and its complex with the substrate, HCO 3−

A. Liljas, B. Jonsson, S. Lindskog, 1993, Proteins.

A 13C nuclear magnetic resonance study of CO2/HCO-3 exchange catalyzed by human carbonic anhydrase I.

B. Jonsson, S. Lindskog, I. Simonsson, 1982, European journal of biochemistry.

Structural and functional differences between carbonic anhydrase isoenzymes I and II as studied by site-directed mutagenesis.

B. Jonsson, P. Jonasson, S. Lindskog, 1991, European journal of biochemistry.

Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling

U. Edlund, T. Holak, B. Jonsson, 1996, Journal of Biomolecular NMR.

Isomerase and chaperone activity of prolyl isomerase in the folding of carbonic anhydrase.

B. Jonsson, P. Freskgård, U. Carlsson, 1992, Science.

Analysis of Explosives by GC‐UV

B. Jonsson, J. Dahlén, J. Andrasko, 2017, Journal of forensic sciences.

Thermal induction of an alternatively folded state in human IgG-Fc.

B. Jonsson, K. Enander, A. Brorsson, 2011, Biochemistry.

Contribution of individual tryptophan residues to the fluorescence spectrum of native and denatured forms of human carbonic anhydrase II.

B. Jonsson, P. Freskgård, P. Jonasson, 1995, Biochemistry.

Mapping the folding intermediate of human carbonic anhydrase II. Probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues.

B. Jonsson, P. Freskgård, M. Lindgren, 1995, Biochemistry.

Perspectives on the Classical Enzyme Carbonic Anhydrase and the Search for Inhibitors.

A. Liljas, B. Jonsson, 2020, Biophysical journal.

Polypeptide Conjugate Binders that Discriminate between Two Isoforms of Human Carbonic Anhydrase in Human Blood

J. Carlsson, B. Jonsson, L. Baltzer, 2011, Chembiochem : a European journal of chemical biology.

Cis‐trans isomerization is rate‐determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase

B. Jonsson, P. Freskgård, P. Jonasson, 1992, FEBS letters.

Paramagnetic and fluorescent probes attached to "buried" sulfhydryl groups in human carbonic anhydrases. Application to inhibitor binding, denaturation and refolding.

B. Jonsson, S. Lindskog, U. Carlsson, 1975, European journal of biochemistry.

High-resolution 2D 1H-15N NMR characterization of persistent structural alterations of proteins induced by interactions with silica nanoparticles.

B. Jonsson, M. Lundqvist, I. Sethson, 2005, Langmuir : the ACS journal of surfaces and colloids.

Some properties of site-specific mutants of human carbonic anhydrase II having active-site residues characterizing carbonic anhydrase III.

B. Jonsson, S. Lindskog, X. Ren, 1991, European journal of biochemistry.

Proton transfer in the catalytic mechanism of carbonic anhydrase. Effects of placing histidine residues at various positions in the active site of human isoenzyme II.

B. Jonsson, S. Lindskog, Z. Liang, 1993, Biochimica et biophysica acta.

Kinetics and Mechanism of Carbonic Anhydrase Isoenzymes a

L. Tibell, B. Jonsson, S. Lindskog, 1984, Annals of the New York Academy of Sciences.

Importance of the conserved active-site residues Tyr7, Glu106 and Thr199 for the catalytic function of human carbonic anhydrase II.

B. Jonsson, S. Lindskog, G. Behravan, 1993, European journal of biochemistry.

Proteolytic cleavage reveals interaction patterns between silica nanoparticles and two variants of human carbonic anhydrase.

B. Jonsson, M. Lundqvist, M. Karlsson, 2005, Langmuir : the ACS journal of surfaces and colloids.

Adsorption of Human Carbonic Anhydrase II Variants to Silica Nanoparticles Occur Stepwise: Binding Is Followed by Successive Conformational Changes to a Molten-Globule-like State

B. Jonsson, M. Karlsson, U. Carlsson, 2000 .

Induction of structure and function in a designed peptide upon adsorption on a silica nanoparticle.

B. Jonsson, M. Lundqvist, P. Nygren, 2006, Angewandte Chemie.

Catalytic and inhibitor-binding properties of some active-site mutants of human carbonic anhydrase I.

B. Jonsson, S. Lindskog, C. Engstrand, 1995, European journal of biochemistry.

Two point mutations convert a catalytically inactive carbonic anhydrase‐related protein (CARP) to an active enzyme

B. Jonsson, S. Lindskog, B. Sjöblom, 1996, FEBS letters.

The ALS-associated mutation G93A in human copper-zinc superoxide dismutase selectively destabilizes the remote metal binding region.

L. Tibell, B. Jonsson, M. Lundqvist, 2009, Biochemistry.

Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli

A. Liljas, H. Berglund, T. Härd, 1997, FEBS letters.

A comparison of the kinetic properties of native bovine muscle carbonic anhydrase and an activated derivative with modified thiol groups.

B. Jonsson, S. Lindskog, E. Millqvist, 1988, Biochimica et biophysica acta.

Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II.

B. Jonsson, P. Freskgård, P. Jonasson, 1994, Biochemistry.

Electron spin echo decay as a probe of aminoxyl environment in spin-labeled mutants of human carbonic anhydrase II†

B. Jonsson, M. Lindgren, S. Eaton, 1997 .

Probing Local Mobility by Electron Paramagnetic Resonance

B. Jonsson, P. Jonasson, Per-Ola, 2005 .

Probing local mobility in carbonic anhydrase EPR of spin-labelled SH groups introduced by site-directed mutagenesis

B. Jonsson, P. Freskgård, M. Lindgren, 1993 .

Fine tuning of the catalytic properties of human carbonic anhydrase II. Effects of varying active-site residue 200.

B. Jonsson, S. Lindskog, G. Behravan, 1991, European journal of biochemistry.

Histidine 64 is not required for high CO2 hydration activity of human carbonic anhydrase II

B. Jonsson, S. Lindskog, J. Sandström, 1988, FEBS letters.

Proton nuclear magnetic resonance studies of histidines in horse carbonic anhydrase I.

B. Jonsson, S. Lindskog, C. Forsman, 1983, Biochimica et biophysica acta.

Phenol, a competitive inhibitor of CO2 hydration catalyzed by carbonic anhydrase.

B. Jonsson, S. Lindskog, I. Simonsson, 1982, Biochemical and biophysical research communications.

PINT: a software for integration of peak volumes and extraction of relaxation rates

M. Carlsson, Patrik Lundström, B. Jonsson, 2013, Journal of Biomolecular NMR.

Applying theories of microbial metabolism for induction of targeted enzyme activity in a methanogenic microbial community at a metabolic steady state

B. Jonsson, Jutta Speda, M. Karlsson, 2016, Applied Microbiology and Biotechnology.

Studies of luminescent conjugated polythiophene derivatives: enhanced spectral discrimination of protein conformational states.

K. Nilsson, O. Inganäs, B. Jonsson, 2007, Bioconjugate chemistry.

Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigation of the thiocyanate adduct of the cobalt (II)-substituted human carbonic anhydrase II.

I. Bertini, C. Luchinat, R. Pierattelli, 1994, Journal of magnetic resonance. Series B.

Activity, life time and effect of hydrolytic enzymes for enhanced biogas production from sludge anaerobic digestion.

B. Jonsson, M. Karlsson, Anna Odnell, 2016, Water research.

Folding of β-sheet proteins

B. Jonsson, U. Carlsson, 1995 .

Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis.

B. Jonsson, P. Freskgård, U. Carlsson, 1993, Biochemistry.

Expression and localization of α- and β-carbonic anhydrase in Helicobacter pylori

B. Jonsson, S. Lindskog, T. Borén, 2002 .

Pyrene excimer fluorescence as a proximity probe for investigation of residual structure in the unfolded state of human carbonic anhydrase II

B. Jonsson, B. Kalman, P. Hammarström, 1997, FEBS letters.

Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetazolamide.

B. Jonsson, S. Lindskog, Shenghua Huang, 1998, Journal of molecular biology.

Organization of an efficient carbonic anhydrase: implications for the mechanism based on structure-function studies of a T199P/C206S mutant.

Bengt-Harald Jonsson, B. Jonsson, B. Sjöblom, 2002, Biochemistry.

Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant.

D. Silverman, B. Jonsson, C. Tu, 1989, Biochemistry.

The complete sequence, expression in Escherichia coli, purification and some properties of carbonic anhydrase from Neisseria gonorrhoeae.

B. Jonsson, S. Lindskog, B. Elleby, 1997, European journal of biochemistry.

Fine tuning of the catalytic properties of carbonic anhydrase. Studies of a Thr200----His variant of human isoenzyme II.

B. Jonsson, S. Lindskog, G. Behravan, 1990, European journal of biochemistry.

Folding and stability of the N-terminus of human carbonic anhydrase II.

B. Jonsson, U. Carlsson, L. Mårtensson, 1995, Biochemistry.

Role of an evolutionarily invariant serine for the stability of human carbonic anhydrase II.

B. Jonsson, M. Andersson, U. Carlsson, 1992, Biochimica et biophysica acta.

Production of active human carbonic anhydrase II in E. coli.

A. Osterman, B. Jonsson, C. Forsman, 1988, Acta chemica Scandinavica. Series B: Organic chemistry and biochemistry.

The catalytic mechanism of human carbonic anhydrase C: Inhibition of CO2 hydration and ester hydrolysis by HCO− 3

B. Jonsson, S. Lindskog, H. Steiner, 1976, FEBS letters.

A ribosomal protein from Thermus thermophilus is homologous to a general shock protein.

A. Liljas, M. Garber, B. Jonsson, 1996, Biochimie.

PINT: a software for integration of peak volumes and extraction of relaxation rates

Mats Carlsson, Bengt-Harald Jonsson, Patrik Lundström, 2013, Journal of Biomolecular NMR.

Remarkably slow folding of a small protein

B. Jonsson, B H Jonsson, G Aronsson, 1997, FEBS letters.

Retention of misfolded mutant transthyretin by the chaperone BiP/GRP78 mitigates amyloidogenesis.

J. Kelly, B. Jonsson, B. Ghafouri, 2006, Journal of molecular biology.

The Quaternary Structure of DNA Polymerase ε from Saccharomyces cerevisiae *

B. Jonsson, E. Johansson, Olga Chilkova, 2003, The Journal of Biological Chemistry.

Characterization of a folding intermediate of human carbonic anhydrase II: probing local mobility by electron paramagnetic resonance.

B. Jonsson, P. Freskgård, M. Lindgren, 1995, Biophysical journal.

Carbonic Anhydrase: Structure, Kinetics, and Mechanism

Bengt-Harald Jonsson, B. Jonsson, S. Lindskog, 1983 .

The catalytic mechanism of carbonic anhydrase. Hydrogen-isotope effects on the kinetic parameters of the human C isoenzyme.

B. Jonsson, S. Lindskog, H. Steiner, 1975, European journal of biochemistry.

Folding and stability of human carbonic anhydrase II.

B. Jonsson, U. Carlsson, 2000, EXS.

Inhibition and catalysis of carbonic anhydrase. Recent crystallographic analyses.

A. Liljas, K. Håkansson, B. Jonsson, 1994, European journal of biochemistry.

Inhibition and catalysis of carbonic anhydrase

Anders Liljas, Bengt-Harald Jonsson, K. Håkansson, 1994 .

Local destabilization of the metal-binding region in human copper-zinc superoxide dismutase by remote mutations is a possible determinant for progression of ALS.

Patrik Lundström, L. Tibell, J. Hennig, 2015, Biochemistry.

Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components

J. Wenger, R. Vincentelli, B. Jonsson, 2016, Scientific Reports.

Transient conformational remodeling of folding proteins by GroES—individually and in concert with GroEL

B. Jonsson, S. Moparthi, P. Hammarström, 2013, Journal of chemical biology.

GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroEL.

B. Jonsson, P. Freskgård, U. Carlsson, 1995, Biochimica et biophysica acta.

Fundamental design principles that guide induction of helix upon formation of stable peptide-nanoparticle complexes.

B. Jonsson, M. Lundqvist, P. Nygren, 2008, Nano letters.

GuHCl and NaCl-dependent hydrogen exchange in MerP reveals a well-defined core with an unusual exchange pattern.

B. Jonsson, M. Lundqvist, I. Sethson, 2006, Journal of molecular biology.

N‐terminal domain, residues 1–91, of ribosomal protein TL5 from Thermus thermophilus binds specifically and strongly to the region of 5S rRNA containing loop E

A. Serganov, A. Liljas, M. Garber, 1999, FEBS letters.

Adsorption to silica nanoparticles of human carbonic anhydrase II and truncated forms induce a molten‐globule‐like structure

B. Jonsson, P. Freskgård, P. Billsten, 1997, FEBS letters.

Structural Mapping of an Aggregation Nucleation Site in a Molten Globule Intermediate*

B. Jonsson, P. Freskgård, P. Hammarström, 1999, The Journal of Biological Chemistry.

Determination of the structural role of the N-terminal domain of human extracellular superoxide dismutase by use of protein fusions.

L. Tibell, B. Jonsson, E. Skärfstad, 1996, Biochimica et biophysica acta.

Combined Enzyme and Substrate Design: Grafting of a Cooperative Two‐Histidine Catalytic Motif into a Protein Targeted at the Scissile Bond in a Designed Ester Substrate

G. Höst, B. Jonsson, L. Baltzer, 2007, Chembiochem : a European journal of chemical biology.

Detection of a high affinity binding site in recombinant Aleuria aurantia lectin

L. Tibell, B. Jonsson, J. Olausson, 2008, Glycoconjugate Journal.

Production and characterization of a monomeric form and a single-site form of Aleuria aurantia lectin.

L. Tibell, B. Jonsson, J. Olausson, 2011, Glycobiology.

Tertiary structure formation at specific tryptophan side chains in the refolding of human carbonic anhydrase II.

B. Jonsson, P. Jonasson, U. Carlsson, 1997, Biochemistry.

Transient interaction with nanoparticles "freezes" a protein in an ensemble of metastable near-native conformations.

Bengt-Harald Jonsson, Martin Lundqvist, B. Jonsson, 2005, Biochemistry.

Formation of local native-like tertiary structures in the slow refolding reaction of human carbonic anhydrase II as monitored by circular dichroism on tryptophan mutants.

B. Jonsson, P. Freskgård, U. Carlsson, 1997, Biochemistry.

Folding around the C‐terminus of human carbonic anhydrase II Kinetic characterization by use of a chemically reactive SH‐group introduced by protein engineering

B. Jonsson, P. Freskgård, L. Mårtensson, 1991, FEBS letters.

Hydration of denatured and molten globule proteins

Bengt-Harald Jonsson, B. Halle, B. Jonsson, 1999, Nature Structural Biology.

Expression and localization of alpha- and beta-carbonic anhydrase in Helicobacter pylori.

B. Jonsson, S. Lindskog, T. Borén, 2002, Biochimica et biophysica acta.

Converting human carbonic anhydrase II into a benzoate ester hydrolase through rational redesign.

G. Höst, B. Jonsson, 2008, Biochimica et biophysica acta.

The binding of human carbonic anhydrase II by functionalized folded polypeptide receptors.

B. Jonsson, K. Enander, L. Baltzer, 2005, Chemistry & biology.

The "two-state folder" MerP forms partially unfolded structures that show temperature dependent hydrogen exchange.

B. Jonsson, I. Sethson, A. Brorsson, 2004, Journal of molecular biology.

Domain-specific chaperone-induced expansion is required for beta-actin folding: a comparison of beta-actin conformations upon interactions with GroEL and tail-less complex polypeptide 1 ring complex (TRiC).

B. Jonsson, M. Lindgren, S. Moparthi, 2007, Biochemistry.

Conformational rearrangements of tail-less complex polypeptide 1 (TCP-1) ring complex (TRiC)-bound actin.

B. Jonsson, M. Lindgren, P. Hammarström, 2007, Biochemistry.

Crystallographic analysis of Thr‐200 → His human carbonic anhydrase II and its complex with the substrate, HCO 3−

A. Liljas, B. Jonsson, S. Lindskog, 1993, Proteins.

The catalytic mechanism of carbonic anhydrase.

B. Jonsson, S. Lindskog, J. Coleman, 1973, Proceedings of the National Academy of Sciences of the United States of America.

Lack of correspondence between the room‐temperature phosphorescence decay‐components and Trp residues in a series of Trp→Cys or Trp→Phemutants of human carbonic anhydrase II

B. Jonsson, D. Steel, U. Carlsson, 1994, FEBS letters.

Hydrogen exchange in a large 29 kD protein and characterization of molten globule aggregation by NMR.

B. Jonsson, I. Sethson, Annika Kjellsson, 2003, Biochemistry.

Folding of beta-sheet proteins.

B. Jonsson, U. Carlsson, 1995, Current opinion in structural biology.