QTL for ethanol withdrawal on Chr12 at D12Ncvs38 (14.25 Mbp , Build 37)
Description:
ethanol withdrawal spans 0.00 - 39.25 Mbp (NCBI Build 37) on Chr12. This interval was obtained by using an interval width of 25 Mbp around the peak marker (Build 37, MGI, http://informatics.jax.org).
The chemical processes, enzymatic activities, and pathways of living things and related temporal, dimensional, qualitative, and quantitative concepts.
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The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
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The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.
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Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
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Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
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chr14q32
Genes in cytogenetic band chr14q32
c1 - Positional genesets for each human chromosome and cytogenetic band.
Molecular Signatures Database (MSigDB) Geneset. This geneset was imported from one of the MSigDB collections.
gene2msig v. 0.1.0
Last updated 2015.08.31
The PROTEIN SUBUNITS of the multimeric IMMUNOGLOBULIN proteins, such as IGA; IGD; IGE; IGG; and IGM. Included are the heavy and light chains which contain the specific ANTIGEN binding domains, as well as the accessory proteins that are part of the the secreted forms of IGM and IGA; (SECRETORY IGA).
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Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
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Univalent antigen-binding fragments composed of one entire IMMUNOGLOBULIN LIGHT CHAIN and the amino terminal end of one of the IMMUNOGLOBULIN HEAVY CHAINS from the hinge region, linked to each other by disulfide bonds. Fab contains the IMMUNOGLOBULIN VARIABLE REGIONS, which are part of the antigen-binding site, and the first IMMUNOGLOBULIN CONSTANT REGIONS. This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN.
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Multi-subunit proteins which function in IMMUNITY. They are produced by B LYMPHOCYTES from the IMMUNOGLOBULIN GENES. They are comprised of two heavy (IMMUNOGLOBULIN HEAVY CHAINS) and two light chains (IMMUNOGLOBULIN LIGHT CHAINS) with additional ancillary polypeptide chains depending on their isoforms. The variety of isoforms include monomeric or polymeric forms, and transmembrane forms (B-CELL ANTIGEN RECEPTORS) or secreted forms (ANTIBODIES). They are divided by the amino acid sequence of their heavy chains into five classes (IMMUNOGLOBULIN A; IMMUNOGLOBULIN D; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M) and various subclasses.
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Partial immunoglobulin molecules resulting from selective cleavage by proteolytic enzymes or generated through PROTEIN ENGINEERING techniques.
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That region of the immunoglobulin molecule that varies in its amino acid sequence and composition, and comprises the binding site for a specific antigen. It is located at the N-terminus of the Fab fragment of the immunoglobulin. It includes hypervariable regions (COMPLEMENTARITY DETERMINING REGIONS) and framework regions.
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Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.
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This set describes genes whose transcription is upregulated in the whole blood of severe COVID-19 patients versus healthy donors. Genes listed in table S2 were entered using ENSEMBL Gene identifiers. Values are the reported log2 fold-change.
Authors:
Anna C Aschenbrenner, Maria Mouktaroudi, Benjamin Krämer, Marie Oestreich, Nikolaos Antonakos, Melanie Nuesch-Germano, Konstantina Gkizeli, Lorenzo Bonaguro, Nico Reusch, Kevin Baßler, Maria Saridaki, Rainer Knoll, Tal Pecht, Theodore S Kapellos, Sarandia Doulou, Charlotte Kröger, Miriam Herbert, Lisa Holsten, Arik Horne, Ioanna D Gemünd, Nikoletta Rovina, Shobhit Agrawal, Kilian Dahm, Martina van Uelft, Anna Drews, Lena Lenkeit, Niklas Bruse, Jelle Gerretsen, Jannik Gierlich, Matthias Becker, Kristian Händler, Michael Kraut, Heidi Theis, Simachew Mengiste, Elena De Domenico, Jonas Schulte-Schrepping, Lea Seep, Jan Raabe, Christoph Hoffmeister, Michael ToVinh, Verena Keitel, Gereon Rieke, Valentina Talevi, Dirk Skowasch, N Ahmad Aziz, Peter Pickkers, Frank L van de Veerdonk, Mihai G Netea, Joachim L Schultze, Matthijs Kox, Monique M B Breteler, Jacob Nattermann, Antonia Koutsoukou, Evangelos J Giamarellos-Bourboulis, Thomas Ulas,
The processes, properties and biological objects that are involved in maintaining, expressing, and transmitting from one organism to another, genetically encoded traits.
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The biological objects that contain genetic information and that are involved in transmitting genetically encoded traits from one organism to another.
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Average rotarod training latency Chr# 12 rs13481614 (102385663) with right flanking marker rs33846822 (30605487) and left marker rs29187760 (115166913). This was mapped in 300 + (b6x129)F2 mice.
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