K. Nordling

发表

Self-assembly of spider silk proteins is controlled by a pH-sensitive relay

Anna Rising, Jan Johansson, M. Hedhammar, 2010, Nature.

Kinetic characterization of the substrate reaction between a complex of antithrombin with a synthetic reactive-bond loop tetradecapeptide and four target proteinases of the inhibitor.

S. Olson, K. Nordling, I. Björk, 1992, The Journal of biological chemistry.

Immunologic evidence for insertion of the reactive-bond loop of antithrombin into the A beta-sheet of the inhibitor during trapping of target proteinases.

S. Olson, K. Nordling, I. Björk, 1993, Biochemistry.

Identification of an epitope in antithrombin appearing on insertion of the reactive-bond loop into the A beta-sheet.

K. Nordling, I. Björk, 1996, Biochemistry.

A Novel Anti-angiogenic Form of Antithrombin with Retained Proteinase Binding Ability and Heparin Affinity*

L. Claesson‐Welsh, K. Nordling, I. Björk, 2001, The Journal of Biological Chemistry.

The Brichos domain of prosurfactant protein C can hold and fold a transmembrane segment

Jan Johansson, J. Johansson, K. Nordling, 2009, Protein science : a publication of the Protein Society.

The Active Site Of Antithrombin. Release Of The Same Proteolytically Cleaved Form Of The Inhibitor From Complexes With Factor IXa, Factor Xa And Thrombin

H. Jörnvall, K. Nordling, I. Björk, 1982, Thrombosis and Haemostasis.

Extension and structural variability of the antithrombin-binding sequence in heparin.

K. Nordling, I. Björk, U. Lindahl, 1984, The Journal of biological chemistry.

Inactivation of pulmonary surfactant by silicone oil in vitro and in ventilated immature rabbits

J. Johansson, K. Nordling, B. Robertson, 2009, Critical care medicine.

Surfactant protein C in canine pulmonary fibrosis.

J. Johansson, J. Häggström, K. Nordling, 2009, Journal of veterinary internal medicine.

Permanent activation of antithrombin by covalent attachment of heparin oligosaccharides

O. Larm, K. Nordling, I. Björk, 1982, FEBS letters.

Immunological evidence for a proteolytic cleavage at the active site of antithrombin in the mechanism of inhibition of coagulation serine proteases.

K. Nordling, I. Björk, P. Wallgren, 1981, European journal of biochemistry.

Evidence by chemical modification for the involvement of one or more tryptophanyl residues of bovine antithrombin in the binding of high-affinity heparin.

K. Nordling, I. Björk, 1979, European journal of biochemistry.

High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

J. Johansson, N. Kronqvist, K. Nordling, 2020, Scientific Reports.

Total serum immunoglobulin E levels in a case–control study in asthmatic/allergic patients, their family members, and healthy subjects from India

B. Ghosh, K. Nordling, C. Gupta, 2006, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

C‐terminal, endoplasmic reticulum‐lumenal domain of prosurfactant protein C – structural features and membrane interactions

J. Johansson, M. Gustafsson, K. Nordling, 2008, The FEBS journal.

A differential effect of low-affinity heparin on the inhibition of thrombin and factor Xa by antithrombin.

K. Nordling, I. Björk, B. Nordenman, 1980, Thrombosis research.

A novel strategy to generate biologically active neo-glycosaminoglycan conjugates.

K. Nordling, I. Björk, U. Lindahl, 1999, Glycobiology.

A new technique, requiring small amounts of cells, for the parallel study of chemiluminescence and phagocytosis via different receptors in the same cell population.

K. Nordling, I. Björk, C. Sandgren, 1991, Journal of immunological methods.

Carbonic Anhydrase Generates CO2 and H+ That Drive Spider Silk Formation Via Opposite Effects on the Terminal Domains

J. Johansson, H. Jörnvall, M. Chesler, 2014, PLoS biology.

Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy.

J. Johansson, Qing Meng, K. Nordling, 2017, Angewandte Chemie.

Biomimicry of artificial spider silk spinning assessed by NMR

J. Johansson, Qing Meng, K. Nordling, 2017 .

Efficient protein production inspired by how spiders make silk

C. Robinson, J. Johansson, H. Jörnvall, 2017, Nature Communications.

Isolation and phagocytic properties of neutrophils and other phagocytes from nonmastitic bovine milk.

K. Nordling, I. Björk, C. Sandgren, 1991, Journal of dairy science.

Peptide-binding specificity of the prosurfactant protein C Brichos domain analyzed by electrospray ionization mass spectrometry.

J. Johansson, H. Jörnvall, T. Bergman, 2009, Rapid communications in mass spectrometry : RCM.

Structural properties of recombinant nonrepetitive and repetitive parts of major ampullate spidroin 1 from Euprosthenops australis: implications for fiber formation.

Anna Rising, Jan Johansson, M. Hedhammar, 2008, Biochemistry.

Denaturation behavior of antithrombin in guanidinium chloride. Irreversibility of unfolding caused by aggregation.

Å. Danielsson, K. Nordling, S. Miller, 1985, Biochemistry.

Tissue Response to Subcutaneously Implanted Recombinant Spider Silk: An in Vivo Study

M. Hedhammar, J. Johansson, K. Nordling, 2009, Materials.

High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C

J. Åqvist, J. Johansson, H. Jörnvall, 2012, Proceedings of the National Academy of Sciences.

Diversified Structural Basis of a Conserved Molecular Mechanism for pH‐Dependent Dimerization in Spider Silk N‐Terminal Domains

J. Johansson, H. Jörnvall, Qing Meng, 2015, ChemBioChem.

Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation

Jerker Widengren, Qing Meng, Hans Jörnvall, 2014, Nature Communications.

A pH-dependent dimer lock in spider silk protein.

Tomas Bergman, Juan Astorga-Wells, Hans Jörnvall, 2010, Journal of molecular biology.

High intracellular stability of the spidroin N‐terminal domain in spite of abundant amyloidogenic segments revealed by in‐cell hydrogen/deuterium exchange mass spectrometry

J. Johansson, H. Jörnvall, D. Lane, 2019, The FEBS journal.

pH-dependent dimerization of spider silk N-terminal domain requires relocation of a wedged tryptophan side chain.

Hans Jörnvall, Kristaps Jaudzems, Michael Landreh, 2012, Journal of molecular biology.

Sterilized recombinant spider silk fibers of low pyrogenicity.

Jan Johansson, M. Hedhammar, J. Johansson, 2010, Biomacromolecules.

Systemic AA amyloidosis in the red fox (Vulpes vulpes)

L. Tjernberg, J. Johansson, C. Palmberg, 2017, Protein science : a publication of the Protein Society.

The Brichos Domain-containing C-terminal Part of Pro-surfactant Protein C Binds to an Unfolded Poly-Val Transmembrane Segment*

J. Johansson, K. Nordling, T. Weaver, 2006, Journal of Biological Chemistry.

Mutations linked to interstitial lung disease can abrogate anti-amyloid function of prosurfactant protein C.

J. Johansson, M. Gustafsson, K. Nordling, 2008, The Biochemical journal.

High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

J. Johansson, N. Kronqvist, K. Nordling, 2020, Scientific Reports.

Anti-amyloid activity of the C-terminal domain of proSP-C against amyloid beta-peptide and medin.

J. Johansson, M. Gustafsson, K. Nordling, 2009, Biochemistry.

A three center study on the diagnostic accuracy of 99mTc-MIBI scintimammography.

G De Vincentis, R. Danieli, O. Schillaci, 1997, Anticancer research.

Diversified Structural Basis of a Conserved Molecular Mechanism for pH‐Dependent Dimerization in Spider Silk N‐Terminal Domains

J. Johansson, H. Jörnvall, Qing Meng, 2015, Chembiochem : a European journal of chemical biology.

Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation

J. Johansson, H. Jörnvall, D. Otzen, 2014, Nature Communications.

Inactivation of papain by antithrombin due to autolytic digestion: a model of serpin inactivation of cysteine proteinases.

U. Hellman, S. Olson, K. Nordling, 1998, The Biochemical journal.