Masarykova Univerzita

Masarykova Univerzita V Brne

Enantis S.r.o.

Jiri Damborsky

Zbynek Prokop

Jan Brezovsky

Kamil Paruch

Fedor Nikulenkov

Benoit Carbain

Stepan Havel

Lumir Krejci

Yuji Nagata

Veronika Stepankova

Radka Chaloupkova

Lukas Daniel

Alexandra Sisakova

Pavel Krejci

Dick Barend Janssen

Lukas Balek

Frantisek Oplustil

Andrea Jesenska

Petr Dvorak

Zaneta Konecna

Tana Koudelakova

Pavel Dvorak

David Bednar

Livia Eiselleova

Pavel Vanacek

Eva Sebestova

Michaela Bosakova

Eva Chovancova

Artur Wiktor Gora

Sarka Bidmanova

Axel Dürkop

Otto S Wolfbeis

The invention provides an isolated thermostable polypeptide possessing FGF2 activity and having at least 85% sequence identity to SEQ ID NO: 2 (FGF2 wt) or a functional fragment thereof, and comprising at least one amino acid substitution R31L and the use thereof in the cell biology research, regenerative medicine and related medical applications or cosmetics. Further it discloses a culture medium comprising subjected FGF2 suitable for culturing a human pluripotent stem cells involving both human embryonic stem cells and induced pluripotent stem cells.

Thermostable FGF2 polypeptide, use thereof

Compounds represented by the structural formula (1) R1, R2, R3, R4, R5, R6 are inhibitors of nucleases, and are useful in particular in a method of treatment and/or prevention of proliferative diseases, neurodegenerative diseases, and other genomic instability associated diseases.

Substituted aminothiazoles as inhibitors of nucleases

The invention provides compounds represented by the structural formula (1): wherein R, R, Rand Rare as defined in the claims. The compounds are inhibitors of nucleases, and are useful in particular in a method of treatment and/or prevention of proliferative diseases, neurodegenerative diseases, and other genomic instability associated diseases.

Pyrazolotriazines as inhibitors of nucleases

Thermostabilization of a protein where the protein contains access routes and wherein at least one amino acid in the bottleneck of the access route is mutated, includes identifying the amino acids of the bottleneck and the amino acids control exchange of the solvent between a buried protein core and surrounding environment and/or in the packing of the amino acids inside the access route. Modification of the amino acids are determined so that the packing of the amino acids inside the tunnel is improved and the access route prevents access of undesired solvent molecules to the protein core, while allowing passage of the compounds necessary at the protein core to enable the protein to perform its biological function.

Method of thermostabilization of a protein and/or stabilization towards organic solvents

The method of detoxification of yperite&#x2014;bis(2-chloroethyl)sulfide&#x2014;by the use of a haloalkane dehalogenases or their compositions, the method of preparation of dehalogenationating enzymes and of decontamination compositions which contains at least one wild type and/or modified haloalkane dehalogenase (EC 3.8.1.5) as an chemically active component. The preferred dehalogenases are LinB fromUT26, DhaA fromNCIMB 13064, DmbA from5033/66. Decontamination is utilizable for detoxification of yperite from the surfaces of instrumentality, constructional objects, human or animal skin and elements of environment by the treatment of yperite with the detoxification composition according the invention at +10&#xb0; C. to +70&#xb0; C., preferably at about +40&#xb0; C. and pH from 4 to 12.

Method of detoxification of yperite by using haloalkane dehalogenases

A method of production of optically active compounds, particularly halohydrocarbons, haloalcohols, alcohols, halopolyols and polyols using hydrolytic dehalogenation of racemic or prochiral halegenhydrocarbons by dehalohenation catalysed by haloalkane dehalogenases (the enzyme code number EC 3.8.1.5) where at least one wild type or modified haloalkane dehalogenase is applied to at least one racemic or prochiral chlorinated, brominated or iodinated compound at the temperature ranged between +10 and +70&#xb0; C. and pH value between 4.0 and 12.0, in aqueous system or in a monophasic organic solution or in a monophasic organic/aqueous solution or in organic/aqueous biphasic systems.

Method of production of optically active halohydrocarbons and alcohols using hydrolytic dehalogenation catalysed by haloalkane dehalogenases

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Brno, Czechia

Jiri Damborsky