Disclosed are bacterial toxins and uses thereof as specific proteases for Ras sarcoma oncoproteins (Ras proteins). The bacterial toxins may be modified for use as pharmaceutical agents for treating Ras-dependent diseases and disorders including cell proliferation diseases and disorders such as cancer.

Compositions, methods, and kits are provided for assaying calpain-5 activity and inhibition. In particular, novel peptide substrates are provided for detecting calpain-5, measuring calpain-5 activity, and screening for inhibitors of calpain-5 to identify potential therapeutic agents for treating retinal diseases and other diseases associated with calpain-5 hyperactivity. Additionally, novel inhibitors of calpain-5 are also provided.

Covalently cross-linked pilus polymers displayed on the cell surface of Gram-positive bacteria are assembled by class C sortase enzymes. These pilus-specific transpeptidases located on the bacterial membrane catalyze a two-step protein ligation reaction—first, cleaving the LPXTG motif of one pilin protomer to form an acyl-enzyme intermediate, and second, joining the terminal threonine to the nucleophilic lysine residue residing within the pilin motif of another pilin protomer. Informed by the high-resolution crystal structures of corynebacterial pilus-specific sortase (SrtA) and by developing structural variants of the sortase enzyme whose catalytic pocket has been unmasked by activating mutations, we have developed new reagents capable of forming isopeptide bonds in vitro. The reagents disclosed herein can catalyze ligation of isolated SpaA domains in vitro provide a facile and versatile new platform for protein engineering and bio-conjugation that has major implications for biotechnology.

The object of the present invention is a method for the production of block polymers comprising a firstand a second block comprising the method steps: A) providing a first block having a nucleophilic peptide sequence for afirst transpeptidase enzyme, B) providing a second block having a peptide recognition sequence for the first transpeptidase enzyme, C) linking the first block to the second block by means of the first transpeptidase enzyme, wherein the first and second blocks are independently selected from nanoparticles, non-peptide polymers, and recombinant proteins. Such a production method makes it possible to build block polymers from identical or different blocks in a particularly simple and controlled manner.

Provided is an enzymatic process that hydrolyzes spinach plant material to form a salt-enhancing ingredient, the formed salt-enhancing ingredient, food products comprising said salt-enhancing ingredient and a method of enhancing the salty taste of food products.

The invention provides protease genes which are regulated in a specific manner during curing of tobacco plants material and which affect the flavour of cured tobacco.

Provided in the present disclosure is a fused protein. The fused protein comprises a plurality of target protein sequences, which are connected in series, wherein every two adjacent target protein sequences are connected by means of a linker sequence, the linker sequence is suitable for being cut into a plurality of free target proteins by means of protease, the multiple target protein sequences are not cleaved by the protease, and neither the C-terminus nor the N-terminus of the free target proteins contains additional residues.

The present disclosure provides, in part, compositions and methods for transient removal of neutralizing antibodies directed to AAV vectors. Such compositions and methods expand the patient cohort eligible for gene therapy and also for redosing/re-administration of AAV in patients previously treated with AAV vectors.

The present invention relates to the use of a cysteine endoprotease or a malt extract to prevent or reduce the cloudiness of a cereal-based beverage, fermented or not.

Disclosed herein are compositions and in vitro and in vivo methods for reprogramming lymphatic tissue to induce the lymphatic tissue to form a lymphovenous anastomosis with an adjacent vessel of the venous system.