MeSH term | MeSH ID | Detail |
---|---|---|
Body Weight | D001835 | 333 associated lipids |
Kidney Neoplasms | D007680 | 29 associated lipids |
Spinocerebellar Ataxias | D020754 | 4 associated lipids |
Dl-serine is a lipid of Fatty Acyls (FA) class. Dl-serine is associated with abnormalities such as Spastic syndrome, Machado-Joseph Disease, Huntington Disease, Infection and Gram positive septicemia. The involved functions are known as Lipid Binding, Proteolysis, Protein Processing, Post-Translational, Cytokinesis and Phosphorylation. Dl-serine often locates in Anatomic Site, Membrane, Cytoplasmic Domain, Extracellular and Blood. The associated genes with Dl-serine are polyserine, lipovitellin, Polypeptides, CSNK2A1 wt Allele and Spider Proteins. The related experimental models are Mouse Model.
To understand associated biological information of Dl-serine, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.
Dl-serine is suspected in Huntington Disease, Infection, Spastic syndrome, Machado-Joseph Disease, Gram positive septicemia and other diseases in descending order of the highest number of associated sentences.
Disease | Cross reference | Weighted score | Related literature |
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We collected disease MeSH terms mapped to the references associated with Dl-serine
MeSH term | MeSH ID | Detail |
---|---|---|
Body Weight | D001835 | 333 associated lipids |
Kidney Neoplasms | D007680 | 29 associated lipids |
Spinocerebellar Ataxias | D020754 | 4 associated lipids |
There are no associated biomedical information in the current reference collection.
Associated locations are in red color. Not associated locations are in black.
Location | Cross reference | Weighted score | Related literatures |
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Function | Cross reference | Weighted score | Related literatures |
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There are no associated biomedical information in the current reference collection.
Gene | Cross reference | Weighted score | Related literatures |
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Mouse Model are used in the study 'Polyalanine and polyserine frameshift products in Huntington's disease.' (Davies JE and Rubinsztein DC, 2006).
Model | Cross reference | Weighted score | Related literatures |
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Authors | Title | Published | Journal | PubMed Link |
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Esposito A et al. | First stereocontrolled synthesis of (S)-cleonin and related cyclopropyl-substituted amino acids. | 2001 | Org. Lett. | pmid:11594812 |
Kimura T et al. | Effect of serine residue on the effectiveness of cationic polypeptide-based gene delivery. | 2000 | Nucleic Acids Symp. Ser. | pmid:12903387 |
Schöttelndreier H et al. | Beta1-integrins mediate Ca2+-signalling and T cell spreading via divergent pathways. | 1999 | Cell. Signal. | pmid:10433522 |
Hasper A et al. | Modification of the N-terminal polyserine cluster alters stability of the plasma membrane H(+)-ATPase from Saccharomyces cerevisiae. | 1999 | Biochim. Biophys. Acta | pmid:10446304 |
Aoki Y et al. | Anti-proliferative effects of unmodified antisense oligodeoxynucleotides targeted against c-raf mRNA: use of poly (lysine/serine) copolymers or cationic lipopolyamines. | 1998 | Clin. Exp. Pharmacol. Physiol. | pmid:9750959 |
Gonsalves KE et al. | Synthesis and surface characterization of functionalized polylactide copolymer microparticles. | 1998 | Biomaterials | pmid:9794526 |
Bates PA and DeLuca NA | The polyserine tract of herpes simplex virus ICP4 is required for normal viral gene expression and growth in murine trigeminal ganglia. | 1998 | J. Virol. | pmid:9696805 |
Doruker P and Bahar I | Role of water on unfolding kinetics of helical peptides studied by molecular dynamics simulations. | 1997 | Biophys. J. | pmid:9168021 |
Evans JS et al. | Prediction of polyelectrolyte polypeptide structures using Monte Carlo conformational search methods with implicit solvation modeling. | 1995 | Protein Sci. | pmid:8535238 |
Picking WD et al. | Fluorescence characterization of the environment encountered by nascent polyalanine and polyserine as they exit Escherichia coli ribosomes during translation. | 1992 | Biochemistry | pmid:1540593 |