The present invention provides a multifunctional multispecific multimeric biomolecule polymer which is formed by obtaining a biomolecule, to which a ubiquitin C-terminal tag is bound, by recombinantly expressing the biomolecule from a host cell, and polyubiquitinating, in vitro, the biomolecule along with a substrate, and proteins E1 (activation enzyme), E2 (conjugation enzyme) and E3 (ligase) which are involved in ubiquitination, and thus having the biomolecule bind to a polyubiquitin scaffold which is formed by covalently bonding two or more ubiquitins. The biomolecule of the present invention may be one or more selected from the group consisting of a protein, peptide, polypeptide, antibody, antibody fragment, DNA and RNA, and, for example, by using heterologous proteins, modularized functionality may be imparted to the multifunctional multispecific biomolecule polymer. In addition, according to the present invention, the multifunctional multispecific multimeric biomolecule polymer is provided in a form that is bound to a molecule capable of increasing the in vivo duration, and thus may be used for producing drugs requiring the increased in vivo duration of efficacy.

Provided herein are methods for diagnosing and treating Alzheimer's disease in a subject comprising determining the expression level of three, four or five members of a panel of proteins in a biological sample obtained from the subject.

The present invention relates to epitopes containing homocitrulline (Heit) that can be used as targets for cancer immunotherapy. The homocitrullinated T cell epitope has (i) a predicted binding score to MIC class II or class I of <30 using the online IEDB prediction program (http://www.iedb.org/) and (ii) at least 5 consecutive amino acids that form a spiral conformational structure. These modified peptides can be used as vaccines or as targets for T cell receptor (TCR) and adoptive T cell transfer therapies.

Described herein are fusion proteins including methanol dehydrogenase (MeDH) and at least one other polypeptide such as 3-hexulose-6-phosphate dehydrogenase (HPS) or 6-phospho-3-hexuloisomerase (PHI), such as DHAS synthase or fructose-6-Phosphate aldolase or such as DHA synthase or DHA kinase. In a localized manner, the fusion protein can promote the conversion of methanol to formaldehyde and then to a ketose phosphate such as hexulose 6-phosphate or then to DHA and G3P. When expressed in cells, the fusion proteins can promote methanol uptake and rapid conversion to the ketose phosphate or to the DHA and D3P, which in turn can be used in a pathway for the production of a desired bioproduct. Beneficially, the rapid conversion to the ketose phosphate or to the DHA and G3P can avoid the undesirable accumulation of formaldehyde in the cell. Also described are engineered cells expressing the fusion protein, optionally include one or more additional metabolic pathway transgene(s), methanol metabolic pathway genes, target product pathway genes, cell culture compositions including the cells, methods for promoting production of the target product or intermediate thereof from the cells, compositions including the target product or intermediate, and products made from the target product or intermediate.

The present invention provides a method for efficiently producing L-homophenylalanine and a strain producing L-homophenylalanine. In the present invention, a new route for the synthesis of L-homophenylalanine by a cascade enzymatic method using cheap benzaldehyde and pyruvic acid as raw materials is designed. By constructing the pathway-related enzymes into the same E. coli strain, a recombinant E. coli is obtained, with which L-homophenylalanine is catalytically produced through reaction in a 5 L reactor, with a yield of 100.9 g/L, a conversion rate of 94%, and ee>99%. Compared with the existing main methods for producing L-HPA, the production cost of L-homophenylalanine is greatly reduced. Thus, the present invention has good application prospects.