Publications

Allostery Frustrates the Experimentalist.
Gianni, S., Jemth, P. (2023). Journal of Molecular Biology, . vol. 435 DOI
Evaluation of affinity-purification coupled to mass spectrometry approaches for capture of short linear motif-based interactions.
Kassa, E., Jamshidi, S., Mihalič, F., Simonetti, L., Kliche, J. et al. (2023). Analytical Biochemistry, . vol. 663 DOI
Proteome-scale mapping of binding sites in the unstructured regions of the human proteome.
Benz, C., Ali, M., Krystkowiak, I., Simonetti, L., Sayadi, A. et al. (2022). Molecular Systems Biology, . vol. 18 DOI
Disordered Regions Flanking the Binding Interface Modulate Affinity between CBP and NCOA.
Karlsson, E., Schnatwinkel, J., Paissoni, C., Andersson, E., Herrmann, C. et al. (2022). Journal of Molecular Biology, . vol. 434 DOI
The dynamic properties of a nuclear coactivator binding domain are evolutionarily conserved.
Karlsson, E., Sorgenfrei, F., Andersson, E., Dogan, J., Jemth, P. et al. (2022). Communications Biology, . vol. 5 DOI
Determinants of affinity, specificity, and phase separation in a supramodule from Post-synaptic density protein 95.
Laursen, L., Inturi, R., Ostergaard, S., Jemth, P. (2022). iScience, . vol. 25 DOI
A Syntenin Inhibitor Blocks Endosomal Entry of SARS-CoV-2 and a Panel of RNA Viruses.
Lindqvist, R., Benz, C., Sereikaite, V., Maassen, L., Laursen, L. et al. (2022). Viruses, . vol. 14 DOI
Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets.
Mihalic, F., Benz, C., Kassa, E., Lindqvist, R., Simonetti, L. et al. (2022). Nature Structural & Molecular Biology
Monoclonal antibodies binding data for SARS-CoV-2 proteins.
Mishra, N., Teyra, J., Boytz, R., Miersch, S., Merritt, T. et al. (2022). Data in Brief, . vol. 43 DOI
Development of Monoclonal Antibodies to Detect for SARS-CoV-2 Proteins.
Mishra, N., Teyra, J., Boytz, R., Miersch, S., Merritt, T. et al. (2022). Journal of Molecular Biology, . vol. 434 DOI
Fuzziness and Frustration in the Energy Landscape of Protein Folding, Function, and Assembly.
Gianni, S., Freiberger, M., Jemth, P., Ferreiro, D., Wolynes, P. et al. (2021). Accounts of Chemical Research, . vol. 54, ss. 1251-1259 DOI
CRISPR/Cas9-based inactivation of human papillomavirus oncogenes E6 or E7 induces senescence in cervical cancer cells.
Inturi, R., Jemth, P. (2021). Virology, . vol. 562, ss. 92-102 DOI
Molecular Details of a Coupled Binding and Folding Reaction between the Amyloid Precursor Protein and a Folded Domain.
Jensen, T., Bartling, C., Karlsson, O., Åberg, E., Haugaard-Kedström, L. et al. (2021). ACS Chemical Biology, . vol. 16, ss. 1191-1200 DOI
Large scale discovery of coronavirus-host factor protein interaction motifs reveals SARS-CoV-2 specific mechanisms and vulnerabilities.
Kruse, T., Benz, C., Garvanska, D., Lindqvist, R., Mihalic, F. et al. (2021). Nature Communications, vol. 12 DOI
Dissecting Inter-domain Cooperativity in the Folding of a Multi Domain Protein.
Laursen, L., Gianni, S., Jemth, P. (2021). Journal of Molecular Biology, . vol. 433 DOI
Divergent evolution of a protein-protein interaction revealed through ancestral sequence reconstruction and resurrection.
Laursen, L., Čalyševa, J., Gibson, T., Jemth, P. (2021). Molecular biology and evolution, vol. 38, ss. 152-167 DOI
Double Mutant Cycles as a Tool to Address Folding, Binding, and Allostery.
Pagano, L., Toto, A., Malagrino, F., Visconti, L., Jemth, P. et al. (2021). International Journal of Molecular Sciences, . vol. 22 DOI
An Early Association between the α-Helix of the TEAD Binding Domain of YAP and TEAD Drives the Formation of the YAP:TEAD Complex.
Bokhovchuk, F., Mesrouze, Y., Meyerhofer, M., Zimmermann, C., Fontana, P. et al. (2020). Biochemistry, vol. 59, ss. 1804-1812 DOI
Structure and Characterization of Phosphoglucomutase 5 from Atlantic and Baltic Herring: An Inactive Enzyme with Intact Substrate Binding.
Gustafsson, R., Eckhard, U., Ye, W., Enbody, E., Pettersson, M. et al. (2020). Biomolecules, vol. 10 DOI
High affinity between CREBBP/p300 and NCOA evolved in vertebrates.
Karlsson, E., Lindberg, A., Andersson, E., Jemth, P. (2020). Protein Science, . vol. 29, ss. 1687-1691 DOI
Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins.
Karlsson, E., Paissoni, C., Erkelens, A., Tehranizadeh, Z., Sorgenfrei, F. et al. (2020). Journal of Biological Chemistry, . vol. 295, ss. 17698-17712 DOI
Functional interplay between protein domains in a supramodular structure involving the postsynaptic density protein PSD-95.
Laursen, L., Karlsson, E., Gianni, S., Jemth, P. (2020). Journal of Biological Chemistry, . vol. 295, ss. 1992-2000 DOI
Supertertiary protein structure affects an allosteric network.
Laursen, L., Kliche, J., Gianni, S., Jemth, P. (2020). Proceedings of the National Academy of Sciences of the United States of America, vol. 117, ss. 24294-24304 DOI
Templated folding of intrinsically disordered proteins.
Toto, A., Malagrino, F., Visconti, L., Troilo, F., Pagano, L. et al. (2020). Journal of Biological Chemistry, vol. 295, ss. 6586-6593 DOI
Affinity versus specificity in coupled binding and folding reactions.
Gianni, S., Jemth, P. (2019). Protein Engineering Design & Selection, vol. 32, ss. 355-357 DOI
Editorial overview: Folding and binding.
Ivarsson, Y., Jemth, P. (2019). Current opinion in structural biology, . vol. 54, ss. 139-140 DOI
Affinity and specificity of motif-based protein-protein interactions.
Ivarsson, Y., Jemth, P. (2019). Current opinion in structural biology, . vol. 54, ss. 26-33 DOI
A structurally heterogeneous transition state underlies coupled binding and folding of disordered proteins.
Karlsson, E., Andersson, E., Dogan, J., Gianni, S., Jemth, P. et al. (2019). Journal of Biological Chemistry, vol. 294, ss. 1230-1239 DOI
Coupled Binding and Helix Formation Monitored by Synchrotron-Radiation Circular Dichroism.
Karlsson, E., Andersson, E., Jones, N., Hoffmann, S., Jemth, P. et al. (2019). Biophysical Journal, . vol. 117, ss. 729-742 DOI
Seeking allosteric networks in PDZ domains.
Gautier, C., Laursen, L., Jemth, P., Gianni, S. (2018). Protein Engineering Design & Selection, vol. 31, ss. 367-373 DOI
Structure and dynamics conspire in the evolution of affinity between intrinsically disordered proteins.
Jemth, P., Karlsson, E., Vogeli, B., Guzovsky, B., Andersson, E. et al. (2018). Science Advances, . vol. 4 DOI
Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations.
Sereikaite, V., Jensen, T., Bartling, C., Jemth, P., Pless, S. et al. (2018). ChemBioChem (Print), . vol. 19, ss. 2136-2145 DOI
Binding Kinetics of the Intrinsically Disordered p53 Family Transactivation Domains and MDM2.
Åberg, E., Karlsson, O., Andersson, E., Jemth, P. (2018). Journal of Physical Chemistry B, vol. 122, ss. 6899-6905 DOI
Addressing the role of the alpha-helical extension in the folding of the third PDZ domain from PSD-95.
Gautier, C., Visconti, L., Jemth, P., Gianni, S. (2017). Scientific Reports, . vol. 7 DOI
How Fast Is Protein-Ligand Association?.
Gianni, S., Jemth, P. (2017). TIBS -Trends in Biochemical Sciences. Regular ed., vol. 42, ss. 847-849 DOI
Emergence and evolution of an interaction between intrinsically disordered proteins.
Hultqvist, G., Åberg, E., Camilloni, C., Sundell, G., Andersson, E. et al. (2017). eLIFE, vol. 6 DOI
The evolution of Sex-linked barring alleles in chickens involves both regulatory and coding changes in CDKN2A.
Thalmann, D., Ring, H., Sundström, E., Cao, X., Larsson, M. et al. (2017). PLOS Genetics, . vol. 13 DOI
Understanding the role of phosphorylation in the binding mechanism of a PDZ domain.
Toto, A., Mattei, A., Jemth, P., Gianni, S. (2017). Protein Engineering Design & Selection, . vol. 30, ss. 1-5 DOI
Evolution of the p53-MDM2 pathway.
Åberg, E., Saccoccia, F., Grabherr, M., Ore, W., Jemth, P. et al. (2017). BMC Evolutionary Biology, . vol. 17 DOI
Activation Barrier-Limited Folding and Conformational Sampling of a Dynamic Protein Domain.
Dogan, J., Toto, A., Andersson, E., Gianni, S., Jemth, P. (2016). Biochemistry, vol. 55, ss. 5289-5295 DOI
Coupled binding and folding of intrinsically disordered proteins: what can we learn from kinetics?.
Gianni, S., Dogan, J., Jemth, P. (2016). Current opinion in structural biology, vol. 36, ss. 18-24 DOI
Protein folding: Vexing debates on a fundamental problem.
Gianni, S., Jemth, P. (2016). Biophysical Chemistry, vol. 212, ss. 17-21 DOI
Improved affinity at the cost of decreased specificity: a recurring theme in PDZ-peptide interactions..
Karlsson, O., Sundell, G., Andersson, E., Ivarsson, Y., Jemth, P. (2016). Scientific Reports, vol. 6 DOI
Ligand binding to the PDZ domains of postsynaptic density protein 95.
Toto, A., Pedersen, S., Karlsson, O., Moran, G., Andersson, E. et al. (2016). Protein Engineering Design & Selection, vol. 29, ss. 169-175 DOI
Binding Rate Constants Reveal Distinct Features of Disordered Protein Domains.
Dogan, J., Jonasson, J., Andersson, E., Jemth, P. (2015). Biochemistry, vol. 54, ss. 4741-4750 DOI
Rigidified Clicked Dimeric Ligands for Studying the Dynamics of the PDZ1-2 Supramodule of PSD-95.
Eildal, J., Bach, A., Dogan, J., Ye, F., Zhang, M. et al. (2015). ChemBioChem (Print), vol. 16, ss. 64-69 DOI
Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus.
Karlsson, O., Ramirez, J., Öberg, D., Malmqvist, T., Engström, Å. et al. (2015). Scientific Reports, vol. 5 DOI
Deconvoluting Protein (Un)folding Structural Ensembles Using X-Ray Scattering, Nuclear Magnetic Resonance Spectroscopy and Molecular Dynamics Simulation.
Nasedkin, A., Marcellini, M., Religa, T., Freund, S., Menzel, A. et al. (2015). PLOS ONE, vol. 10 DOI
Targeting Protein-Protein Interactions with Trimeric Ligands: High Affinity Inhibitors of the MAGUK Protein Family.
Nissen, K., Haugaard-Kedstrom, L., Wilbek, T., Nielsen, L., Åberg, E. et al. (2015). PLOS ONE, vol. 10 DOI
The binding mechanisms of intrinsically disordered proteins.
Dogan, J., Gianni, S., Jemth, P. (2014). Physical Chemistry, Chemical Physics - PCCP, vol. 16, ss. 6323-6331 DOI
Only kinetics can prove conformational selection.
Dogan, J., Jemth, P. (2014). Biophysical Journal, vol. 107, ss. 1997-1998 DOI
Nonequilibrium Capture Rates Induce Protein Accumulation and Enhanced Adsorption to Solid-State Nanopores.
Freedman, K., Haq, S., Fletcher, M., Foley, J., Jemth, P. et al. (2014). ACS Nano, vol. 8, ss. 12238-12249 DOI
Deciphering the mechanisms of binding induced folding at nearly atomic resolution: The Φ value analysis applied to IDPs.
Gianni, S., Dogan, J., Jemth, P. (2014). Intrinsically Disordered Proteins, vol. 2, ss. e28624- DOI Download fulltext
Distinguishing induced fit from conformational selection.
Gianni, S., Dogan, J., Jemth, P. (2014). Biophysical Chemistry, vol. 189, ss. 33-39 DOI
Conserved nucleation sites reinforce the significance of phi analysis in proteinfolding studies.
Gianni, S., Jemth, P. (2014). IUBMB Life - A Journal of the International Union of Biochemistry and Molecular Biology, vol. 66, ss. 449-452 DOI
Helical Propensity in an Intrinsically Disordered Protein Accelerates Ligand Binding.
Iesmantavicius, V., Dogan, J., Jemth, P., Teilum, K., Kjaergaard, M. (2014). Angewandte Chemie International Edition, vol. 53, ss. 1548-1551 DOI
A Frustrated Binding Interface for Intrinsically Disordered Proteins.
Jemth, P., Mu, X., Engström, Å., Dogan, J. (2014). Journal of Biological Chemistry, vol. 289, ss. 5528-5533 DOI
Thermodynamic Aspects of cAMP Dependent Protein Kinase Catalytic Subunit Allostery.
Kivi, R., Jemth, P., Jaerv, J. (2014). The Protein Journal, vol. 33, ss. 386-393 DOI
The Role of Backbone Hydrogen Bonds in the Transition State for Protein Folding of a PDZ Domain.
Pedersen, S., Hultqvist, G., Stromgaard, K., Jemth, P. (2014). PLOS ONE, vol. 9, ss. e95619- DOI
Probing backbone hydrogen bonding in PDZ/ligand interactions by protein amide-to-ester mutations.
Pedersen, S., Pedersen, S., Anker, L., Hultqvist, G., Kristensen, A. et al. (2014). Nature Communications, vol. 5, ss. 3215- DOI
The transition state structure for coupled binding and folding of disordered protein domains.
Dogan, J., Mu, X., Engström, Å., Jemth, P. (2013). Scientific Reports, vol. 3, ss. 2076- DOI
Probing the Role of Backbone Hydrogen Bonds in Protein-Peptide Interactions by Amide-to-Ester Mutations.
Eildal, J., Hultqvist, G., Balle, T., Stuhr-Hansen, N., Padrah, S. et al. (2013). Journal of the American Chemical Society, vol. 135, ss. 12998-13007 DOI
Single molecule unfolding and stretching of protein domains inside a solid-state nanopore by electric field.
Freedman, K., Haq, S., Edel, J., Jemth, P., Kim, M. (2013). Scientific Reports, vol. 3, ss. 1638- DOI
Energetic pathway sampling in a protein interaction domain.
Hultqvist, G., Haq, R., Punekar, A., Chi, C., Engström, Å. et al. (2013). Structure, vol. 21, ss. 1193-1202 DOI
Single-Molecule Studies of Intrinsically Disordered Proteins Using Solid-State Nanopores.
Japrung, D., Dogan, J., Freedman, K., Nadzeyka, A., Bauerdick, S. et al. (2013). Analytical Chemistry, vol. 85, ss. 2449-2456 DOI
Kinetics of Acrylodan-Labelled cAMP-Dependent Protein Kinase Catalytic Subunit Denaturation.
Kivi, R., Loog, M., Jemth, P., Jaerv, J. (2013). The Protein Journal, vol. 32, ss. 519-525 DOI
A high-affinity, dimeric inhibitor of PSD-95 bivalently interacts with PDZ1-2 and protects against ischemic brain damage.
Bach, A., Clausen, B., Moller, M., Vestergaard, B., Chi, C. et al. (2012). Proceedings of the National Academy of Sciences of the United States of America, vol. 109, ss. 3317-3322 DOI
Ligand binding by PDZ domains.
Chi, C., Bach, A., Stromgaard, K., Gianni, S., Jemth, P. (2012). Biofactors, vol. 38, ss. 338-348 DOI
Interactions outside the boundaries of the canonical binding groove of a pdz domain influence ligand binding.
Chi, C., Haq, S., Rinaldo, S., Dogan, J., Cutruzzolà, F. et al. (2012). Biochemistry, vol. 51, ss. 8971-8979 DOI
Fast Association and Slow Transitions in the Interaction between Two Intrinsically Disordered Protein Domains.
Dogan, J., Schmidt, T., Mu, X., Engström, Å., Jemth, P. (2012). Journal of Biological Chemistry, vol. 287, ss. 34316-34324 DOI
Characterization of the endopeptidase activity of tripeptidyl-peptidase II.
Eklund, S., Dogan, J., Jemth, P., Kalbacher, H., Tomkinson, B. (2012). Biochemical and Biophysical Research Communications - BBRC, vol. 424, ss. 503-507 DOI
Folding pathways of proteins with increasing degree of sequence identities but different structure and function.
Giri, R., Morrone, A., Travaglini-Allocatelli, C., Jemth, P., Brunori, M. et al. (2012). Proceedings of the National Academy of Sciences of the United States of America, vol. 109, ss. 17772-17776 DOI
Side-Chain Interactions Form Late and Cooperatively in the Binding Reaction between Disordered Peptides and PDZ Domains.
Haq, S., Chi, C., Bach, A., Dogan, J., Engström, Å. et al. (2012). Journal of the American Chemical Society, vol. 134, ss. 599-605 DOI
An expanded view of the protein folding landscape of PDZ domains.
Hultqvist, G., Pedersen, S., Strømgaard, K., Chi, C., Gianni, S. et al. (2012). Biochemical and Biophysical Research Communications - BBRC, vol. 421, ss. 550-553 DOI
Tolerance of Protein Folding to a Circular Permutation in a PDZ Domain.
Hultqvist, G., Punekar, A., Morrone, A., Chi, C., Engström, Å. et al. (2012). PLOS ONE, vol. 7, ss. e50055- DOI
The Transition State of Coupled Folding and Binding for a Flexible beta-Finger.
Karlsson, O., Chi, C., Engström, Å., Jemth, P. (2012). Journal of Molecular Biology, vol. 417, ss. 253-261 DOI
Biophysical Characterization of the Complex between Human Papillomavirus E6 Protein and Synapse-associated Protein 97.
Chi, C., Bach, A., Engström, Å., Stromgaard, K., Lundström, P. et al. (2011). Journal of Biological Chemistry, vol. 286, ss. 3597-3606 DOI
Chemical, Thermal, and Electric Field Induced Unfolding of Single Protein Molecules Studied Using Nanopores.
Freedman, K., Jürgens, M., Prabhu, A., Ahn, C., Jemth, P. et al. (2011). Analytical Chemistry, vol. 83, ss. 5137-5144 DOI
Sequence-specific Long Range networks in PSD-95/Discs Large/ZO-1 (PDZ) Domains Tune Their Binding Selectivity.
Gianni, S., Haq, S., Montemiglio, L., Jürgens, M., Engström, Å. et al. (2011). Journal of Biological Chemistry, vol. 286, ss. 27167-27175 DOI
Deciphering the kinetic binding mechanism of dimeric ligands, using a potent plasma-stable dimeric inhibitor of postsynaptic density protein-95 as an example.
Chi, C., Bach, A., Gottschalk, M., Kristensen, S., Strømgaard, K. et al. (2010). Journal of Biological Chemistry, vol. 285, ss. 28252-28260 DOI
Structural and functional characterization of CcmG from Pseudomonas aeruginosa, a key component of the bacterial cytochrome c maturation apparatus.
Di Matteo, A., Calosci, N., Gianni, S., Jemth, P., Brunori, M. et al. (2010). Proteins, vol. 78, ss. 2213-2221 DOI
The plastic energy landscape of protein folding: a triangular folding mechanism with an equilibrium intermediate for a small protein domain.
Haq, S., Jürgens, M., Chi N, C., Koh, C., Elfström, L. et al. (2010). Journal of Biological Chemistry, vol. 285, ss. 18051-18059 DOI
Design and synthesis of highly potent and plasma-stable dimeric inhibitors of the PSD-95-NMDA receptor interaction.
Bach, A., Chi, C., Pang, G., Olsen, L., Kristensen, A. et al. (2009). Angewandte Chemie International Edition, . vol. 48, ss. 9685-9689 DOI
A sequential binding mechanism in a PDZ domain.
Chi N, C., Bach, A., Engström, Å., Wang, H., Strømgaard, K. et al. (2009). Biochemistry, vol. 48, ss. 7089-7097 DOI
Distinguishing between smooth and rough free energy barriers in protein folding.
Gianni, S., Brunori, M., Jemth, P., Oliveberg, M., Zhang, M. (2009). Biochemistry, vol. 48, ss. 11825-11830 DOI
Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate.
Savino, C., Montemiglio, L., Sciara, G., Miele, A., Kendrew, S. et al. (2009). Journal of Biological Chemistry, vol. 284, ss. 29170-29179 DOI
Folding and stability of globular proteins and implications for function.
Travaglini-Allocatelli, C., Ivarsson, Y., Jemth, P., Gianni, S. (2009). Current opinion in structural biology, vol. 19, ss. 3-7 DOI
Modified peptides as potent inhibitors of the postsynaptic density-95/N-methyl-D-aspartate receptor interaction..
Bach, A., Chi, C., Olsen, T., Pedersen, S., Røder, M. et al. (2008). Journal of Medicinal Chemistry, vol. 51, ss. 6450-9 DOI
Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins.
Calosci, N., Chi, C., Richter, B., Camilloni, C., Engström, Å. et al. (2008). Proceedings of the National Academy of Sciences of the United States of America, . vol. 105, ss. 19241-19246 DOI
Reassessing a sparse energetic network within a single protein domain.
Chi, C., Elfström, L., Shi, Y., Snäll, T., Engström, Å. et al. (2008). Proceedings of the National Academy of Sciences of the United States of America, vol. 105, ss. 4679-4684 DOI
Demonstration by burst-phase analysis of a robust folding intermediate in the FF domain.
Jemth, P., Johnson, C., Gianni, S., Fersht, A. (2008). Protein Engineering Design & Selection, vol. 21, ss. 207-214 DOI
A conserved folding mechanism for PDZ domains.
Chi, C., Gianni, S., Calosci, N., Travaglini-Allocatelli, C., Engström, Å. et al. (2007). FEBS Letters, vol. 581, ss. 1109-1113 DOI
A PDZ domain recapitulates a unifying mechanism for protein folding.
Gianni, S., Geierhaas, C., Calosci, N., Jemth, P., Vuister, G. et al. (2007). Proceedings of the National Academy of Sciences of the United States of America, vol. 104, ss. 128-133 DOI
Identification and characterization of protein folding intermediates.
Gianni, S., Ivarsson, Y., Jemth, P., Brunori, M., Travaglini-Allocatelli, C. (2007). Biophysical Chemistry, vol. 128, ss. 105-113 DOI
An on-pathway intermediate in the folding of a PDZ domain.
Ivarsson, Y., Travaglini-Allocatelli, C., Jemth, P., Malatesta, F., Brunori, M. et al. (2007). Journal of Biological Chemistry, vol. 282, ss. 8568-8572 DOI
PDZ domains: folding and binding.
Jemth, P., Gianni, S. (2007). Biochemistry, vol. 46, ss. 8701-8708 DOI
Two conserved residues govern the salt and pH dependencies of the binding reaction of a PDZ domain.
Chi, C., Engström, Å., Gianni, S., Larsson, M., Jemth, P. (2006). Journal of Biological Chemistry, vol. 281, ss. 36811-36818 DOI
Demonstration of long-range interactions in a PDZ domain by NMR, kinetics, and protein engineering.
Gianni, S., Walma, T., Arcovito, A., Calosci, N., Bellelli, A. et al. (2006). Structure, vol. 14, ss. 1801-1809 DOI
Renal cell carcinoma risk in type 2 von Hippel-Lindau disease correlates with defects in pVHL stability and HIF-1 alpha interactions.
Knauth, K., Bex, C., Jemth, P., Buchberger, A. (2006). Oncogene, vol. 25, ss. 370-377 DOI
The kinetics of PDZ domain-ligand interactions and implications for the binding mechanism.
Gianni, S., Engström, Å., Larsson, M., Calosci, N., Malatesta, F. et al. (2005). Journal of Biological Chemistry, vol. 280, ss. 34805-34812 DOI
The structure of the major transition state for folding of an FF domain from experiment and simulation..
Jemth, P., Day, R., Gianni, S., Khan, F., Allen, M. et al. (2005). J Mol Biol, vol. 350, ss. 363-78
Fibroblast growth factors share binding sites in heparan sulphate..
Kreuger, J., Jemth, P., Sanders-Lindberg, E., Eliahu, L., Ron, D. et al. (2005). Biochem J, vol. 389, ss. 145-50
Simulation and experiment conspire to reveal cryptic intermediates and a slide from the nucleation-condensation to framework mechanism of folding..
White, G., Gianni, S., Grossmann, J., Jemth, P., Fersht, A. et al. (2005). J Mol Biol, vol. 350, ss. 757-75
Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation..
Jemth, P., Gianni, S., Day, R., Li, B., Johnson, C. et al. (2004). Proc Natl Acad Sci U S A, vol. 101, ss. 6450-5
Processing of macromolecular heparin by heparanase.
Gong, F., Jemth, P., Escobar Galvis, M., Vlodavsky, I., Horner, A. et al. (2003). Journal of Biological Chemistry, vol. 278, ss. 35152-35158 DOI
Oligosaccharide library-based assessment of heparan sulfate6-O-sulfotransferase substrate specificity..
Jemth, P., Smeds, E., Do, A., Habuchi, H., Kimata, K. et al. (2003). J Biol Chem, vol. 278, ss. 24371-
Oligosaccharide Library-based Assessment of Heparan Sulfate 6-O-Sulfotransferase Substrate Specificity.
Jemth, P., Smeds, E., Do, A., Habuchi, H., Kimata, K. et al. (2003). Journal of Biological Chemistry, vol. 278, ss. 24371-24376
Nitrocellulose filter binding to assess binding of glycosaminoglycans to proteins.
Kreuger, J., Lindahl, U., Jemth, P. (2003). I Yuan C. Lee, Reiko T. Lee (red.) Recognition of carbohydrates in biological systems, Part B, . ss. 327-339 DOI
An ensemble of Theta class glutathione transferases with novel catalytic properties generated by stochastic recombination of fragments of two mammalian enzymes.
Broo, K., Larsson, A., Jemth, P., Mannervik, B. (2002). Journal of Molecular Biology, vol. 318, ss. 59-70
Biosynthetic oligosaccharide libraries for identification of protein-binding heparan sulfate motifs: exploring the structural diversity by screening for fibroblast growth factor (FGF)1 and FGF2 binding..
Jemth, P., Kreuger, J., Kusche-Gullberg, M., Sturiale, L., Giménez-Gallego, G. et al. (2002). Journal of Biological Chemistry, vol. 277, ss. 30567-30573 DOI
A semisyntetic glutathione peroxidase with high catalytic efficiency: Selenoglutathione transferase.
Ren, X., Jemth, P., Board, P., Luo, G., Mannervik, B. et al. (2002). Chemical Biology, vol. 9, ss. 789-794
Role of the glutamyl alpha-carboxylate of the substrate glutathione in the catalytic mechanism of human glutathione transferase A1-1.
Gustafsson, A., Pettersson, P., Grehn, L., Jemth, P., Mannervik, B. (2001). Biochemistry, vol. 40, ss. 15835-15845 DOI
The active-site residue Tyr-175 in human glyoxalase II contributes to binding of glutathione derivatives.
Ridderstrom, M., Jemth, P., Cameron, A., Mannervik, B. (2000). BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, vol. 1481, ss. 344-348
Conformational change and non-canonical interactions in the complex between human papillomavirus E6 protein and Synapse-Associated Protein 97.
Chi, C., Bach, A., Engström, Å., Strømgaard, K., Lundström, P. et al.
Analysis of AtZDP substrate specificity.
Valsecchi, I., Wernersson, J., Jemth, P., Allinson, S., Martin, N. et al.