Refined solution structure of the human TSG-6 Link module
The link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding.
The Link Module from Human Tsg-6 Inhibits Neutrophil Migration in a Hyaluronan- and Inter-Alpha -Inhibitor-Independent Manner
Hyaluronan Binding Properties of a Cd44 Chimera Containing the Link Module of Tsg-6
Mapping the Hyaluronan-Binding Site on the Link Module from Human Tumor Necrosis Factor-Stimulated Gene-6 by Site-Directed Mutagenesis
Localization and Characterization of the Hyaluronan-Binding Site on the Link Module from Human Tsg-6
Method for Quantitative Refolding of the Link Module from Human Tsg-6
Overexpression, Purification, and Refolding of Link Module from Human Tsg-6 in Escherichia Coli: Effect of Temperature, Media, and Mutagenesis on Lysine Misincorporation at Arginine Aga Codons
Solution Structure of the Link Module: A Hyaluronan-Binding Domain Involved in Extracellular Matrix Stability and Cell Migration
A Novel Secretory Tumour Necrosis Factor-Inducible Protein (Tsg-6) is a Member of the Family of Hyaluronate Binding Proteins, Closely Related to the Adhesion Receptor Cd44
TUMOR NECROSIS FACTOR-INDUCIBLE PROTEIN TSG-6
HUMAN TSG-6, HYALURONATE-BINDING PROTEIN, TNF-STIMULATED GENE 6 PROTEIN
GVYHREARSGKYKLTYAEAKAVCEFEGGHLATYKQLEAARKIGFHVCAAGWMAKGRVGYPIVKPGPNCGFGKTGIIDYGI RLNRSERWDAYCYNPHAK
NMR STUDY OF THE LINK MODULE FROM TSG-6 MINIMIZED AVERAGE STRUCTURE
SOLUTION STRUCTURE OF THE HUMAN TSG-6 LINK MODULE IN THE PRESENCE OF A HYALURONAN OCTASACCHARIDE
SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.
POSSIBLE ROLE IN CELL-MATRIX INTERACTIONS DURING INFLAMMATION
STRUCTURE DETERMINED BY NMR SPECTROSCOPY ON UNIFORMLY 15N- AND 13C,15N-LABELLED LINK_TSG6
REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,SIMONSON,WARREN
Home built incorporating Oxford Instruments magnet
HYALURONAN-BINDING DOMAIN, CARBOHYDRATE-BINDING DOMAIN, LINK MODULE, CELL ADHESION, GLYCOPROTEIN