The invention is intended to identify glutathione-S-transferase that exhibits the activities to metabolize and detoxify an isoxazoline derivative, such as pyroxasulfone. The invention provides a method for cultivating a transgenic plant into which a nucleic acid encoding a protein (a or b) below has been introduced in the presence of isoxazoline derivatives: (a) a protein comprising the amino acid sequence as shown in SEQ ID NO: 2; or (b) a protein comprising an amino acid sequence having 80% or higher identity to the amino acid sequence as shown in SEQ ID NO: 2 and having the activity of glutathione-S-transferase.

This invention provides compounds, compositions and methods for modulating the expression of target genes using RNA interference. RNAi structures and molecules of this invention can be used for modulating or silencing the expression of genes, with high levels of RNAi activity and reduced off target actions. Advantageous structures include siRNAs targeted to any gene having one or more 2-deoxy nucleotides located in the seed region. The RNA interference molecules can be used in methods for preventing or treating diseases.

The present invention relates to a method for screening protein-protein interaction inhibitors using a nanopore, a method for analyzing protein structures, a method for analyzing protein-protein interactions, and a kit therefor.

The present invention generally relates to systems and methods for treating certain oxidative stress conditions. In one aspect, compositions and methods of the invention can be used to treat a subject having an oxidative stress condition, for example, a subject having pulmonary fibrosis. In some embodiments, an inhibitor of ERp57 (for example, thiomuscimol) and/or an inhibitor of GSTP (for example, TLK-199) may be used to treat the subject. Also provided in certain aspects of the present invention are kits for such therapies, methods for promoting such therapies, and the like.

Disclosed is a recombinant protein composed by the fusion of Glutathione S-transferase (GST), or an esa-histidine peptide (poly-His), or Maltose Binding Protein (MBP), to the Carboxyl-terminus end of the human KHNYN protein, containing residues 597-678 or a region including at least the amino acidic region 630-678. Also disclosed is a second recombinant protein where the Carboxyl-terminus end of the human KHNYN protein, containing residues 627-678 is genetically fused in a tandem construct to the Carboxyl-terminus end of KHNYN including residues 597-678. The tandem construct is N-terminally tagged with Glutathione S-transferase (GST), or an esa-histidine peptide (poly-His), or Maltose Binding Protein (MBP). The potential use of these Neddylation sensors also called Neddylation probes to isolate mono-, poly-neddylated targets as well as substrates modified by the addition of ubiquitin-NEDD8 mixed chains is considered.

Provided is a cell culture vessel characterized in that a surface to be in contact with cells is coated with a laminin fragment having integrin 61 binding activity or a modified form thereof in a dry state, the laminin fragment being derived from at least one kind selected from laminin 511 and laminin 521, the cell culture vessel being any of the following:
(1) a cell culture vessel of which a surface to be in contact with cells is coated only with a laminin fragment having integrin 61 binding activity or a modified form thereof in a dry state;
(2) a cell culture vessel of which a surface to be in contact with cells is coated with a laminin fragment having integrin 61 binding activity or a modified form thereof in combination with a laminin fragment having no integrin 61 binding activity in a dry state; and
(3) a cell culture vessel of which a surface to be in contact with cells is coated with a laminin fragment having integrin 61 binding activity or a modified form thereof in combination with a protein that is neither a laminin nor a laminin fragment, in a dry state.

Fusion proteins containing active agonist or antagonist fragments of parathyroid hormone (PTH) and parathyroid hormone related peptide (PTHrP) coupled to a collagen-binding domain are presented. The fusion proteins can be used to promote bone growth, to promote hair growth, to prevent cancer metastasis to bone, to promote immune reconstitution with a bone marrow stem cell transplant, to promote mobilization of bone marrow stem cells for collection for autologous stem cell transplant, and to treat renal osteodystrophy. Pharmaceutical agents comprising a collagen-binding polypeptide segment linked to a non-peptidyl PTH/PTHrP receptor agonist or antagonist are also presented.

The present invention relates to novel polypeptides comprising an ice-binding capability resulting in an ice crystal formation and/or growth reducing or inhibiting activity. The present invention also relates to an edible product and to a solid support comprising the novel polypeptide. Furthermore, the present invention also relates to a method for producing the novel polypeptide and to different uses of the novel polypeptide.

This disclosure relates to particles comprising recombinant proteins, pharmaceutical composition comprising the particles, and therapeutic uses related thereto. In certain embodiments, the particles are made by the process of producing recombinant proteins and conjugating the recombinant proteins to form nanoparticles with a linking reagent comprising disulfide bonds. Typically the recombinant protein has a polypeptide of viral, fungal, or bacterial origin such as secreted effector proteins AvrA and YopJ. In certain embodiments, the disclosure relates to treating or preventing autoimmune diseases, cancer, or inflammatory diseases, or conditions such as inflammatory bowel disease (IBD).

Enzymes for depolymerizing lignin. The enzymes include dehydrogenases, -etherases, and glutathione lyases. The dehydrogenases can comprise one or more or LigD, LigO, LigN, and LigL. The -etherases can comprise one or more of LigE, LigF, LigP, and BaeA. The glutathione lyases can comprise any one or more of LigG and a number of non-stereospecific, optionally recombinant glutathione lyases derived from Sphingobium sp. SYK-6, Novosphingobium aromaticivorans, Escherichia coli, Streptococcus sanguinis, Phanerochaete chrysosporium, and other microorganisms. The enzymes can be combined in compositions and/or used in methods of processing lignin or other aromatic compounds in vitro.