Search results for: Uno Carlsson

Items from 1 to 20 out of 41 results

article

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

Jutta Speda, Bengt-Harald Jonsson, Uno Carlsson, Martin Karlsson

Biotechnology for Biofuels > 2017 > 10 > 1 > 1-17

Background Hitherto, the main goal of metaproteomic analyses has been to characterize the functional role of particular microorganisms in the microbial ecology of various microbial communities. Recently, it has been suggested that metaproteomics could be used for bioprospecting microbial communities to query for the most active enzymes to improve the selection process of industrially relevant enzymes...

article

Assessment of sample preparation methods for metaproteomics of extracellular proteins

Jutta Speda, Mikaela A. Johansson, Uno Carlsson, Martin Karlsson

Analytical Biochemistry > 2017 > 516 > C > 23-36

Enzyme discovery in individual strains of microorganisms is compromised by the limitations of pure culturing. In principle, metaproteomics allows for fractionation and study of different parts of the protein complement but has hitherto mainly been used to identify intracellular proteins. However, the extracellular environment is also expected to comprise a wealth of information regarding important...

chapter

Soil peroxidase-mediated chlorination of fulvic acid

Gunilla Asplund, Hans Borén, Uno Carlsson, Anders Grimvall

Lecture Notes in Earth Sciences > Humic Substances in the Aquatic and Terrestrial Environment > 475-483

Humic matter has recently been shown to contain considerable quantities of naturally produced organohalogens. The present study investigated the possibility of a non-specific, enzymatically mediated halogenation of organic matter in soil. The results showed that, in the presence of chloride and hydrogen peroxide, the enzyme chloroperoxidase (CPO) from the fungus Caldariomyces fumago catalyzes chlorination...

article

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

Satish Babu Moparthi, Daniel Sjölander, Laila Villebeck, Bengt-Harald Jonsson, more

Journal of Chemical Biology > 2014 > 7 > 1 > 1-15

The commonly accepted dogma of the bacterial GroE chaperonin system entails protein folding mediated by cycles of several ATP-dependent sequential steps where GroEL interacts with the folding client protein. In contrast, we herein report GroES-mediated dynamic remodeling (expansion and compression) of two different protein substrates during folding: the endogenous substrate MreB and carbonic anhydrase...

article

Effects on the conformation of FVIIa by sTF and Ca2+ binding: Studies of fluorescence resonance energy transfer and quenching

Karin Carlsson, Egon Persson, Mikael Lindgren, Uno Carlsson, more

Biochemical and Biophysical Research Communications > 2011 > 413 > 4 > 545-549

The apparent length of FVIIa in solution was estimated by a FRET analysis. Two fluorescent probes, fluorescein (Fl-FPR) and a rhodamine derivative (TMR), were covalently attached to FVIIa. The binding site of Fl-FPR was in the protease domain whereas TMR was positioned in the Gla domain, thus allowing a length measure over virtually the whole extension of the protein. From the FRET measurements, the...

article

Chaperone Activity of Cyp18 through Hydrophobic Condensation That Enables Rescue of Transient Misfolded Molten Globule Intermediates

Satish Babu Moparthi, Rikard Fristedt, Rajesh Mishra, Karin Almstedt, more

Biochemistry > 2010 > 49 > 6 > 1137 - 1145

article

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

Rikard Owenius, Anngelica Jarl, Bengt-Harald Jonsson, Uno Carlsson, more

Journal of Chemical Biology > 2010 > 3 > 3 > 127-139

The Hsp60-type chaperonin GroEL assists in the folding of the enzyme human carbonic anhydrase II (HCA II) and protects it from aggregation. This study was aimed to monitor conformational rearrangement of the substrate protein during the initial GroEL capture (in the absence of ATP) of the thermally unfolded HCA II molten-globule. Single- and double-cysteine mutants were specifically spin-labeled at...

article

Small-Molecule Suppression of Misfolding of Mutated Human Carbonic Anhydrase II Linked to Marble Brain Disease

Karin Almstedt, Therese Rafstedt, Claudiu T. Supuran, Uno Carlsson, more

Biochemistry > 2009 > 48 > 23 > 5358 - 5364

article

Thermodynamic Interrogation of a Folding Disease. Mutant Mapping of Position 107 in Human Carbonic Anhydrase II Linked to Marble Brain Disease

Karin Almstedt, Lars-Göran Mårtensson, Uno Carlsson, Per Hammarström

Biochemistry > 2008 > 47 > 5 > 1288 - 1298

article

Inhibitors of factor VIIa affect the interface between the protease domain and tissue factor

Karin Carlsson, Egon Persson, Uno Carlsson, Magdalena Svensson

Biochemical and Biophysical Research Communications > 2006 > 349 > 3 > 1111-1116

Blood coagulation is triggered by the formation of a complex between factor VIIa (FVIIa) and its cofactor, tissue factor (TF). The γ–carboxyglutamic acid-rich domain of FVIIa docks with the C-terminal domain of TF, the EGF1 domain of FVIIa contacts both domains of TF, and the EGF2 domain and protease domain (PD) form a continuous surface that sits on the N-terminal domain of TF. Our aim was to investigate...

article

Autocrine production of biologically active hepatocyte growth factor (HGF) by injured human skin

Fariba Nayeri, Junjang Xu, Avni Abdiu, Tayeb Nayeri, more

Journal of Dermatological Science > 2006 > 43 > 1 > 49-56

Hepatocyte growth factor (HGF) is a potent regenerative factor involved in wound healing. Previous studies have shown that mesenchymal cells produce HGF, stimulating epithelial cells in a paracrine fashion.To examine whether autocrine HGF production by keratinocytes can occur upon skin injury.A 31-year-old male patient sustained a burn affecting 80% of his total body surface area. Biopsies were taken...

article

Sequential coagulation factor VIIa domain binding to tissue factor

Maria Österlund, Egon Persson, Uno Carlsson, Per-Ola Freskgård, more

Biochemical and Biophysical Research Communications > 2005 > 337 > 4 > 1276-1282

Vessel wall tissue factor (TF) is exposed to blood upon vascular damage which enables association with factor VIIa (FVIIa). This leads to initiation of the blood coagulation cascade through localization and allosteric induction of FVIIa procoagulant activity. To examine the docking pathway of the FVIIa–TF complex, various residues in the extracellular part of TF (sTF) that are known to interact with...

article

Activity, Folding, Misfolding, and Aggregation in Vitro of the Naturally Occurring Human Tissue Factor Mutant R200W ^†

Jimmy Wiréhn, Karin Carlsson, Anna Herland, Egon Persson, more

Biochemistry > 2005 > 44 > 18 > 6755 - 6763

article

Protein Adsorption Orientation in the Light of Fluorescent Probes: Mapping of the Interaction between Site-Directly Labeled Human Carbonic Anhydrase II and Silica Nanoparticles

Martin Karlsson, Uno Carlsson

Biophysical Journal > 2005 > 88 > 5 > 3536-3544

Little is known about the direction and specificity of protein adsorption to solid surfaces, a knowledge that is of great importance in many biotechnological applications. To resolve the direction in which a protein with known structure and surface potentials binds to negatively charged silica nanoparticles, fluorescent probes were attached to different areas on the surface of the protein human carbonic...

article

Denaturant-Assisted Formation of a Stabilizing Disulfide Bridge from Engineered Cysteines in Nonideal Conformations ^†

Martin Karlsson, Lars-Göran Mårtensson, Carin Karlsson, Uno Carlsson

Biochemistry > 2005 > 44 > 9 > 3487 - 3493

article

Transition state analysis of the complex between coagulation factor VIIa and tissue factor: suggesting a sequential domain-binding pathway

Maria Österlund, Egon Persson, Magdalena Svensson, Uno Carlsson, more

Biochemical and Biophysical Research Communications > 2005 > 327 > 3 > 789-793

Injury of a blood vessel exposes membrane-bound tissue factor (TF) to blood, which allows binding of coagulation factor VIIa (FVIIa). This initiation of the coagulation cascade is dictated by a specific multi-domain interaction between FVIIa and TF. To examine the energies involved in the transition state of the FVIIa:TF complex, various residues in the extracellular part of TF (sTF) that are known...

article

Unfolding a Folding Disease: Folding, Misfolding and Aggregation of the Marble Brain Syndrome-associated Mutant H107Y of Human Carbonic Anhydrase II

Karin Almstedt, Martin Lundqvist, Jonas Carlsson, Martin Karlsson, more

Journal of Molecular Biology > 2004 > 342 > 2 > 619-633

Most loss-of-function diseases are caused by aberrant folding of important proteins. These proteins often misfold due to mutations. The disease marble brain syndrome (MBS), known also as carbonic anhydrase II deficiency syndrome (CADS), can manifest in carriers of point mutations in the human carbonic anhydrase II (HCA II) gene. One mutation associated with MBS entails the His107Tyr substitution....

article

Circumnavigating Misfolding Traps in the Energy Landscape through Protein Engineering: Suppression of Molten Globule and Aggregation in Carbonic Anhydrase ^†

Martin Karlsson, Lars-Göran Mårtensson, Patrik Olofsson, Uno Carlsson

Biochemistry > 2004 > 43 > 21 > 6803 - 6807

article

Reshaping the folding energy landscape by chloride salt: impact on molten-globule formation and aggregation behavior of carbonic anhydrase

Kristina Borén, Hannah Grankvist, Per Hammarström, Uno Carlsson

FEBS Letters > 2004 > 566 > 1-3 > 95-99

During chemical denaturation different intermediate states are populated or suppressed due to the nature of the denaturant used. Chemical denaturation by guanidine-HCl (GuHCl) of human carbonic anhydrase II (HCA II) leads to a three-state unfolding process (C _m _, _N _I =1.0 and C _m _, _I _U =1.9 M GuHCl) with formation of an equilibrium molten-globule intermediate...

article

The Cyclooxygenase-2 Inhibitor Celecoxib Is a Potent Inhibitor of Human Carbonic Anhydrase II

James F. Knudsen, Uno Carlsson, Per Hammarström, Gerald H. Sokol, more

Inflammation > 2004 > 28 > 5 > 285-290

Cyclooxygenase-2 (COX-2) is up-regulated in stromal and inflammatory cells. The inducible COX-2 isoform is expressed during inflammation, in some cancers, and in brain tissue after global and focal ischemia. Tissue acidosis is a dominant factor in inflammation, and contributes to pain and hyperalgesia. Recently, compelling epidemiological and clinical evidence has documented the COX-independent effects...

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Search results for: Uno Carlsson

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

Assessment of sample preparation methods for metaproteomics of extracellular proteins

Soil peroxidase-mediated chlorination of fulvic acid

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

Effects on the conformation of FVIIa by sTF and Ca2+ binding: Studies of fluorescence resonance energy transfer and quenching

Chaperone Activity of Cyp18 through Hydrophobic Condensation That Enables Rescue of Transient Misfolded Molten Globule Intermediates

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

Small-Molecule Suppression of Misfolding of Mutated Human Carbonic Anhydrase II Linked to Marble Brain Disease

Thermodynamic Interrogation of a Folding Disease. Mutant Mapping of Position 107 in Human Carbonic Anhydrase II Linked to Marble Brain Disease

Inhibitors of factor VIIa affect the interface between the protease domain and tissue factor

Autocrine production of biologically active hepatocyte growth factor (HGF) by injured human skin

Sequential coagulation factor VIIa domain binding to tissue factor

Activity, Folding, Misfolding, and Aggregation in Vitro of the Naturally Occurring Human Tissue Factor Mutant R200W ^†

Protein Adsorption Orientation in the Light of Fluorescent Probes: Mapping of the Interaction between Site-Directly Labeled Human Carbonic Anhydrase II and Silica Nanoparticles

Denaturant-Assisted Formation of a Stabilizing Disulfide Bridge from Engineered Cysteines in Nonideal Conformations ^†

Transition state analysis of the complex between coagulation factor VIIa and tissue factor: suggesting a sequential domain-binding pathway

Unfolding a Folding Disease: Folding, Misfolding and Aggregation of the Marble Brain Syndrome-associated Mutant H107Y of Human Carbonic Anhydrase II

Circumnavigating Misfolding Traps in the Energy Landscape through Protein Engineering: Suppression of Molten Globule and Aggregation in Carbonic Anhydrase ^†

Reshaping the folding energy landscape by chloride salt: impact on molten-globule formation and aggregation behavior of carbonic anhydrase

The Cyclooxygenase-2 Inhibitor Celecoxib Is a Potent Inhibitor of Human Carbonic Anhydrase II

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