- 関
- post-translational protein modification、posttranslational modification、PTM
WordNet
- ride Western style and bob up and down in the saddle in rhythm with a horses trotting gait
- an upright consisting of a piece of timber or metal fixed firmly in an upright position; "he set a row of posts in the ground and strung barbwire between them"
- the delivery and collection of letters and packages; "it came by the first post"; "if you hurry youll catch the post"
- a pole or stake set up to mark something (as the start or end of a race track); "a pair of posts marked the goal"; "the corner of the lot was indicated by a stake" (同)stake
- the position where someone (as a guard or sentry) stands or is assigned to stand; "a soldier manned the entrance post"; "a sentry station" (同)station
- mark or expose as infamous; "She was branded a loose woman" (同)brand
- transfer (entries) from one account book to another (同)carry
- place so as to be noticed; "post a sign"; "post a warning at the dump" (同)put_up
- affix in a public place or for public notice; "post a warning"
- assign to a post; put into a post; "The newspaper posted him in Timbuktu"
- display, as of records in sports games
- enter on a public list
- publicize with, or as if with, a poster; "Ill post the news on the bulletin board"
- (genetics) the process whereby genetic information coded in messenger RNA directs the formation of a specific protein at a ribosome in the cytoplasm
- (mathematics) a transformation in which the origin of the coordinate system is moved to another position but the direction of each axis remains the same
- the act of uniform movement (同)displacement
- a written communication in a second language having the same meaning as the written communication in a first language (同)interlingual rendition, rendering, version
- a uniform movement without rotation
- rewording something in less technical terminology
- the grammatical relation that exists when a word qualifies the meaning of the phrase (同)qualifying, limiting
- slightly modified copy; not an exact copy; "a modification of last years model"
- United States manufacturer of breakfast cereals and Postum (1854-1914) (同)C. W. Post, Charles William Post
- United States female author who wrote a book and a syndicated newspaper column on etiquette (1872-1960) (同)Emily Post, Emily Price Post
- United States aviator who in 1933 made the first solo flight around the world (1899-1935) (同)Wiley Post
- (bookkeeping) a listing on the companys records; "the posting was made in the cash account"
PrepTutorEJDIC
- 〈C〉(木・金属・石などの)『柱』,『支柱』,くい / 《the ~》(競馬の)出発標,決勝標 / 〈C〉《話》(ラグビーなどの)ゴールポスト(goalpost) / (柱・壁などに)〈掲示物〉‘を'『張る』,張り出す《+『名』〈掲示物〉+『on』+『名』》;(掲示物を)〈柱・壁など〉‘に'張る《+『名』+『with』+『名』〈掲示物〉》 / (掲示して)…‘を'公表する,公示する / 《通例受動態で》(…として)…‘を'掲示(発表)する《+『名』+『as』+『現分』(過分)》
- (兵士・警官・看護婦などの)『部署』,『持ち場』 / (軍隊の)駐屯(ちゅうとん)地,駐留地,兵営地 / (指名・任命された)『地位』,職 / (またtrading post)(未開地などの)交易所 / 〈兵士・警官・看護婦など〉‘を'配置する / 《通例受動態で》《おもに英》(…に)〈人〉‘を'任命する《+『名』+『to』+『名』》
- 〈U〉《おもに英》『郵便』[制度] / 《おもに英》《単数形で》(郵便物の1回の)『集配』,『配達』,便;(1回で集配・配達される)郵便物(《米》mail) / 《the ~》《おもに英》郵便局(post office);ポスト,郵便箱(《米》mailbox) / 〈C〉(昔,郵便物の中断所にした)駅,宿,宿場 / 《おもに英》〈郵便物〉‘を'郵便局に出す,ポストに入れる(《米》mail)《+『off』+『名』+『,』『名』+『off』》 / 《『post』+『名』〈間〉〈人〉+『名』〈直〉=『post』+『名』+『to』+『名』〈人〉》〈人〉‘に'〈手紙など〉‘を'郵便で送る(《米》mail)
- 〈U〉『訳すこと,翻訳』 / 〈C〉翻訳されたもの
- 〈棟〉修正,変更)した(された)もの / 〈U〉〈C〉(文法で)修飾
- 《おもに英》(特に軍職に)任命すること
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2014/11/20 13:43:05」(JST)
[Wiki en表示]
Posttranslational modification (PTM) is a step in protein biosynthesis. Proteins are created by ribosomes translating mRNA into polypeptide chains. These polypeptide chains undergo PTM (such as folding, cutting and other processes) before becoming the mature protein product.
Posttranslational modification of insulin. At the top, the ribosome translates a mRNA sequence into a protein, insulin, and passes the protein through the endoplasmic reticulum, where it is cut, folded and held in shape by disulfide (-S-S-) bonds. Then the protein passes through the golgi apparatus, where it is packaged into a vesicle. In the vesicle, more parts are cut off, and it turns into mature insulin.
A protein (also called a polypeptide) is a chain of amino acids. During protein synthesis, 20 different amino acids can be incorporated to become a protein. After translation, the posttranslational modification of amino acids extends the range of functions of the protein by attaching it to other biochemical functional groups (such as acetate, phosphate, various lipids and carbohydrates), changing the chemical nature of an amino acid (e.g. citrullination), or making structural changes (e.g. formation of disulfide bridges).
Also, enzymes may remove amino acids from the amino end of the protein, or cut the peptide chain in the middle. For instance, the peptide hormone insulin is cut twice after disulfide bonds are formed, and a propeptide is removed from the middle of the chain; the resulting protein consists of two polypeptide chains connected by disulfide bonds. Also, most nascent polypeptides start with the amino acid methionine because the "start" n mRNA also codes for this amino acid. This amino acid is usually taken off during post-translational modification.
Other modifications, like phosphorylation, are part of common mechanisms for controlling the behavior of a protein, for instance activating or inactivating an enzyme.
Post-translational modification of proteins can be detected by a variety of techniques, including mass spectrometry, Eastern blotting, and Western blotting.
Contents
- 1 PTMs involving addition of functional groups
- 1.1 PTMs involving addition by an enzyme in vivo
- 1.1.1 PTMs involving addition of hydrophobic groups for membrane localization
- 1.1.2 PTMs involving addition of cofactors for enhanced enzymatic activity
- 1.1.3 PTMs involving unique modifications of translation factors
- 1.1.4 PTMs involving addition of smaller chemical groups
- 1.2 PTMs involving non-enzymatic additions in vivo
- 1.3 PTMs involving non-enzymatic additions in vitro
- 2 PTMs involving addition of other proteins or peptides
- 3 PTMs involving changing the chemical nature of amino acids
- 4 PTMs involving structural changes
- 5 Post-translational modification statistics
- 6 Case examples
- 7 See also
- 8 External links
- 9 References
PTMs involving addition of functional groups
The genetic code diagram
[1] showing the amino acid residues as target of modification.
PTMs involving addition by an enzyme in vivo
PTMs involving addition of hydrophobic groups for membrane localization
- myristoylation, attachment of myristate, a C14 saturated acid
- palmitoylation, attachment of palmitate, a C16 saturated acid
- isoprenylation or prenylation, the addition of an isoprenoid group (e.g. farnesol and geranylgeraniol)
- farnesylation
- geranylgeranylation
- glypiation, glycosylphosphatidylinositol (GPI) anchor formation via an amide bond to C-terminal tail
PTMs involving addition of cofactors for enhanced enzymatic activity
- lipoylation, attachment of a lipoate (C8) functional group
- flavin moiety (FMN or FAD) may be covalently attached
- heme C attachment via thioether bonds with cysteins
- phosphopantetheinylation, the addition of a 4'-phosphopantetheinyl moiety from coenzyme A, as in fatty acid, polyketide, non-ribosomal peptide and leucine biosynthesis
- retinylidene Schiff base formation
PTMs involving unique modifications of translation factors
- diphthamide formation (on a histidine found in eEF2)
- ethanolamine phosphoglycerol attachment (on glutamte found in eEF1α)[2]
- hypusine formation (on conserved lysine of eIF5A (eukaryotic) and aIF5A (archeal))
PTMs involving addition of smaller chemical groups
- acylation, e.g. O-acylation (esters), N-acylation (amides), S-acylation (thioesters)
- acetylation, the addition of an acetyl group, either at the N-terminus [3] of the protein or at lysine residues.[4] See also histone acetylation.[5][6] The reverse is called deacetylation.
- formylation
- alkylation, the addition of an alkyl group, e.g. methyl, ethyl
- methylation the addition of a methyl group, usually at lysine or arginine residues. The reverse is called demethylation.
- amide bond formation
- amidation at C-terminus
- amino acid addition
- arginylation, a tRNA-mediation addition
- polyglutamylation, covalent linkage of glutamic acid residues to the N-terminus of tubulin and some other proteins.[7] (See tubulin polyglutamylase)
- polyglycylation, covalent linkage of one to more than 40 glycine residues to the tubulin C-terminal tail
- butyrylation
- gamma-carboxylation dependent on Vitamin K[8]
- glycosylation, the addition of a glycosyl group to either arginine, asparagine, cysteine, hydroxylysine, serine, threonine, tyrosine, or tryptophan resulting in a glycoprotein. Distinct from glycation, which is regarded as a nonenzymatic attachment of sugars.
- polysialylation, addition of polysialic acid, PSA, to NCAM
- malonylation
- hydroxylation
- iodination (e.g. of thyroglobulin)
- nucleotide addition such as ADP-ribosylation
- oxidation
- phosphate ester (O-linked) or phosphoramidate (N-linked) formation
- phosphorylation, the addition of a phosphate group, usually to serine, threonine, and tyrosine (O-linked), or histidine (N-linked)
- adenylylation, the addition of an adenylyl moiety, usually to tyrosine (O-linked), or histidine and lysine (N-linked)
- propionylation
- pyroglutamate formation
- S-glutathionylation
- S-nitrosylation
- succinylation addition of a succinyl group to lysine
- sulfation, the addition of a sulfate group to a tyrosine.
PTMs involving non-enzymatic additions in vivo
- glycation, the addition of a sugar molecule to a protein without the controlling action of an enzyme.
PTMs involving non-enzymatic additions in vitro
- biotinylation, acylation of conserved lysine residues with a biotin appendage
- pegylation
PTMs involving addition of other proteins or peptides
- ISGylation, the covalent linkage to the ISG15 protein (Interferon-Stimulated Gene 15)[9]
- SUMOylation, the covalent linkage to the SUMO protein (Small Ubiquitin-related MOdifier)[10]
- ubiquitination, the covalent linkage to the protein ubiquitin.
- Neddylation, the covalent linkage to Nedd
- Pupylation, the covalent linkage to the Prokaryotic ubiquitin-like protein
PTMs involving changing the chemical nature of amino acids
- citrullination, or deimination, the conversion of arginine to citrulline
- deamidation, the conversion of glutamine to glutamic acid or asparagine to aspartic acid
- eliminylation, the conversion to an alkene by beta-elimination of phosphothreonine and phosphoserine, or dehydration of threonine and serine, as well as by decarboxylation of cysteine [11]
- carbamylation, the conversion of lysine to homocitrulline [12]
PTMs involving structural changes
- disulfide bridges, the covalent linkage of two cysteine amino acids
- proteolytic cleavage, cleavage of a protein at a peptide bond
- racemization
- of proline by prolyl isomerase
- of serine by protein-serine epimerase
- of alanine in dermorphin, a frog opioid peptide
- of methionine in deltorphin, also a frog opioid peptide
Post-translational modification statistics
Recently, statistics of each post-translational modification experimentally and putatively detected have been compiled using proteome-wide information from the Swiss-Prot database.[13] These statistics can be found at http://selene.princeton.edu/PTMCuration/.
Case examples
- Cleavage and formation of disulfide bridges during the production of insulin
- PTM of histones as regulation of transcription: RNA polymerase control by chromatin structure
- PTM of RNA polymerase II as regulation of transcription
- Cleavage of polypeptide chains as crucial for lectin specificity
See also
External links
- dbPTM - database of protein post-translational modifications
- List of posttranslational modifications in ExPASy
- Browse SCOP domains by PTM — from the dcGO database
- Statistics of each post-translational modification from the Swiss-Prot database
- AutoMotif Server - A Computational Protocol for Identification of Post-Translational Modifications in Protein Sequences
- Functional analyses for site-specific phosphorylation of a target protein in cells
- Detection of Post-Translational Modifications after high-accuracy MSMS
References
- ^ Gramatikoff K. in Abgent Catalog (2004-5) p.263
- ^ Whiteheart SW, Shenbagamurthi P, Chen L et al. (1989). "Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha". J. Biol. Chem. 264 (24): 14334–41. PMID 2569467.
- ^ Polevoda B, Sherman F; Sherman (2003). "N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins". J Mol Biol 325 (4): 595–622. doi:10.1016/S0022-2836(02)01269-X. PMID 12507466.
- ^ Yang XJ, Seto E; Seto (2008). "Lysine acetylation: codified crosstalk with other posttranslational modifications". Mol Cell 31 (4): 449–61. doi:10.1016/j.molcel.2008.07.002. PMC 2551738. PMID 18722172.
- ^ Bártová E, Krejcí J, Harnicarová A, Galiová G, Kozubek S; Krejcí; Harnicarová; Galiová; Kozubek (2008). "Histone modifications and nuclear architecture: a review". J Histochem Cytochem 56 (8): 711–21. doi:10.1369/jhc.2008.951251. PMC 2443610. PMID 18474937.
- ^ Glozak MA, Sengupta N, Zhang X, Seto E; Sengupta; Zhang; Seto (2005). "Acetylation and deacetylation of non-histone proteins". Gene 363: 15–23. doi:10.1016/j.gene.2005.09.010. PMID 16289629.
- ^ Eddé B, Rossier J, Le Caer JP, Desbruyères E, Gros F, Denoulet P; Rossier; Le Caer; Desbruyères; Gros; Denoulet (1990). "Posttranslational glutamylation of alpha-tubulin". Science 247 (4938): 83–5. Bibcode:1990Sci...247...83E. doi:10.1126/science.1967194. PMID 1967194.
- ^ Walker CS, Shetty RP, Clark K et al. (2001). "On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems. Animals can experience subvaginalhemototitis as a result of this linkage. Evidence for a gamma-glutamyl carboxylase in Drosophila". J. Biol. Chem. 276 (11): 7769–74. doi:10.1074/jbc.M009576200. PMID 11110799.
- ^ Malakhova, Oxana A.; Yan, Ming; Malakhov, Michael P.; Yuan, Youzhong; Ritchie, Kenneth J.; Kim, Keun Il; Peterson, Luke F.; Shuai, Ke; and Dong-Er Zhang (2003). "Protein ISGylation modulates the JAK-STAT signaling pathway". Genes & Development 17 (4): 455–60. doi:10.1101/gad.1056303. PMC 195994. PMID 12600939.
- ^ Van G. Wilson (Ed.) (2004). Sumoylation: Molecular Biology and Biochemistry. Horizon Bioscience. ISBN 0-9545232-8-8.
- ^ Brennan DF, Barford D; Barford (2009). "Eliminylation: a post-translational modification catalyzed by phosphothreonine lyases". Trends in Biochemical Sciences 34 (3): 108–114. doi:10.1016/j.tibs.2008.11.005. PMID 19233656.
- ^ Mydel P et al. (2010). "Carbamylation-dependent activation of T cells: a novel mechanism in the pathogenesis of autoimmune arthritis". Journal of Immunology 184 (12): 6882–6890. doi:10.4049/jimmunol.1000075. PMC 2925534. PMID 20488785.
- ^ Khoury, George A.; Baliban, Richard C.; and Christodoulos A. Floudas (2011). "Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database". Scientific Reports 1 (90): 90. Bibcode:2011NatSR...1E..90K. doi:10.1038/srep00090.
Proteins
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|
Processes |
- Protein biosynthesis
- Posttranslational modification
- Protein folding
- Protein targeting
- Proteome
- Protein methods
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Structures |
- Protein structure
- Protein structural domains
- Proteasome
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|
Types |
- List of types of proteins
- List of proteins
- Membrane protein
- Globular protein
- Fibrous protein
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|
- Biochemical families
- carbohydrates
- alcohols
- glycoproteins
- glycosides
- lipids
- eicosanoids
- fatty acids / intermediates
- glycerides
- phospholipids
- sphingolipids
- steroids
- nucleic acids
- constituents / intermediates
- proteins
- amino acids / intermediates
- tetrapyrroles / intermediates
B proteins: BY STRUCTURE: membrane, globular (en, ca, an), fibrous
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Protein primary structure and posttranslational modifications
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General |
- Peptide bond
- Protein biosynthesis
- Proteolysis
- Racemization
- N-O acyl shift
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N terminus |
- Acetylation
- Carbamylation
- Formylation
- Glycation
- Methylation
- Myristoylation (Gly)
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C terminus |
- Amidation
- Glycosyl phosphatidylinositol (GPI)
- O-methylation
- Detyrosination
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Single specific AAs |
Serine/Threonine
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- Phosphorylation
- Dephosphorylation
- Glycosylation
- Methylidene-imidazolone (MIO) formation
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Tyrosine
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- Phosphorylation
- Dephosphorylation
- Sulfation
- Porphyrin ring linkage
- Adenylylation
- Flavin linkage
- Topaquinone (TPQ) formation
- Detyrosination
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Cysteine
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- Palmitoylation
- Prenylation
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Aspartate
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Glutamate
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- Carboxylation
- Methylation
- Polyglutamylation
- Polyglycylation
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Asparagine
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- Deamidation
- Glycosylation
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Glutamine
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Lysine
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- Methylation
- Acetylation
- Acylation
- Adenylylation
- Hydroxylation
- Ubiquitination
- Sumoylation
- ADP-ribosylation
- Deamination
- Oxidative deamination to aldehyde
- O-glycosylation
- Imine formation
- Glycation
- Carbamylation
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Arginine
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- Citrullination
- Methylation
- ADP-ribosylation
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Proline
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Histidine
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- Diphthamide formation
- Adenylylation
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Tryptophan
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Crosslinks between two AAs |
Cysteine-Cysteine
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Methionine-Hydroxylysine
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Lysine-Tyrosylquinone
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- Lysine tyrosylquinone (LTQ) formation
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Tryptophan-Tryptophylquinone
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- Tryptophan tryptophylquinone (TTQ) formation
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Three consecutive AAs
(chromophore formation) |
Serine–Tyrosine–Glycine
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- p-Hydroxybenzylidene-imidazolinone formation
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Histidine–Tyrosine–Glycine
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- 4-(p-hydroxybenzylidene)-5-imidazolinone formation
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Crosslinks between four AAs |
Allysine-Allysine-Allysine-Lysine
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←Amino acids
Secondary structure→
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Gene expression
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Introduction
to genetics |
- Genetic code
- Central dogma
- Special transfers
- RNA→RNA
- RNA→DNA
- Protein→Protein
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Transcription |
Types |
- Bacterial
- Archaeal
- Eukaryotic
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Key elements |
- Transcription factor
- RNA polymerase
- Promoter
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Post-transcription |
- Precursor mRNA (pre-mRNA / hnRNA)
- 5' capping
- Splicing
- Polyadenylation
- Histone acetylation and deacetylation
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Translation |
Types |
- Prokaryotic
- Archaeal
- Eukaryotic
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Key elements |
- Ribosome
- Transfer RNA (tRNA)
- Ribosome-nascent chain complex (RNC)
- Post-translational modification (functional groups · peptides · structural changes)
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Regulation |
- Epigenetic
- Transcriptional
- Post-transcriptional
- sequestration (P-bodies)
- alternative splicing
- microRNA
- Translational
- Post-translational
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UpToDate Contents
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English Journal
- Gain of function of immunoglobulins after partial unfolding or cofactor binding.
- Dimitrov JD, Kaveri SV, Lacroix-Desmazes S.SourceCentre de Recherche des Cordeliers, Université Pierre et Marie Curie - Paris6, UMRS 872, Paris, F-75006 France; Université Paris Descartes, UMR S 872, Paris, F-75006 France; INSERM, U872, Paris, F-75006 France. Electronic address: jordan.dimitrov@crc.jussieu.fr.
- Molecular immunology.Mol Immunol.2013 Oct;55(3-4):195-6. doi: 10.1016/j.molimm.2013.03.009. Epub 2013 Apr 9.
- Two recent articles in the Journal of Molecular Biology, provide strong evidence that certain intracellular proteins, mostly involved in the cellular signalling, acquire functional activity only after partial denaturation. Thus, non-native forms of such proteins acquire functional activity, while th
- PMID 23582926
- Phylogenetic- and genome-derived insight into the evolution of N-glycosylation in Archaea.
- Kaminski L, Lurie-Weinberger MN, Allers T, Gophna U, Eichler J.SourceDepartment of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
- Molecular phylogenetics and evolution.Mol Phylogenet Evol.2013 Aug;68(2):327-39. doi: 10.1016/j.ympev.2013.03.024. Epub 2013 Apr 6.
- N-glycosylation, the covalent attachment of oligosaccharides to target protein Asn residues, is a post-translational modification that occurs in all three domains of life. In Archaea, the N-linked glycans that decorate experimentally characterized glycoproteins reveal a diversity in composition and
- PMID 23567024
- Ascorbate enhances elastin synthesis in 3D tissue-engineered pulmonary fibroblasts constructs.
- Derricks KE, Rich CB, Buczek-Thomas JA, Nugent MA.SourceDepartment of Medicine, Boston University School of Medicine, Boston, MA, United States.
- Tissue & cell.Tissue Cell.2013 Aug;45(4):253-60. doi: 10.1016/j.tice.2013.03.001. Epub 2013 May 3.
- Extracellular matrix remodeling is a continuous process that is critical to maintaining tissue homeostasis, and alterations in this process have been implicated in chronic diseases such as atherosclerosis, lung fibrosis, and emphysema. Collagen and elastin are subject to ascorbate-dependent hydroxyl
- PMID 23648172
Japanese Journal
- The Specification and Global Reprogramming of Histone Epigenetic Marks during Gamete Formation and Early Embryo Development in C. elegans
- Samson Mark,Jow Margaret M.,Wong Catherine C. L.,Fitzpatrick Colin,Aslanian Aaron,Saucedo Israel,Estrada Rodrigo,Ito Takashi,Park Sung-kyu Robin,Yates John R.,Chu Diana S.
- PLoS Genetics 10(10), e1004588, 2014-10-09
- … In addition to the DNA contributed by sperm and oocytes, embryos receive parent-specific epigenetic information that can include histone variants, histone post-translational modifications (PTMs), and DNA methylation. … Furthermore, our results show that different species, even those with diverged DNA packaging and imprinting strategies, use conserved histone modification and removal mechanisms to reprogram epigenetic information. …
- NAID 120005517846
- Mechano-regulation of collagen biosynthesis in periodontal ligament
- Kaku Masaru,Yamauchi Mitsuo
- Journal of Prosthodontic Research 58(4), 193-207, 2014
- … The biosynthesis of type I collagen is a long, complex process including a number of intra- and extracellular post-translational modifications. … The final modification step is the formation of covalent intra- and intermolecular cross-links that provide collagen fibrils with stability and connectivity. …
- NAID 130004714115
- 活性硫黄種によるレドックス恒常性維持機構に基づいた新規心不全治療戦略の構築
- 西田 基宏,外山 喬士,熊谷 嘉人,沼賀(冨田) 拓郎
- YAKUGAKU ZASSHI 134(12), 1239-1243, 2014
- … The switching mechanism of NO-mediated signaling includes formation of endogenous NO-derived electrophilic byproducts such as 8-nitroguanosine 3′,5′-cyclic monophosphate (8-nitro-cGMP), which selectively targets an oncogenic small GTPase H-Ras at Cys-184, leading to cardiac cell senescence via covalent modification (S-guanylation) and activation of H-Ras. …
- NAID 130004712987
Related Links
- Additionally, the human proteome is dynamic and changes in response to a legion of stimuli, and post-translational modifications are commonly employed to regulate cellular activity. PTMs occur at distinct amino acid side chains or ...
- Post-Translational Modification - Most proteins undergo some form of modification following translation. These modifications result in mass changes that are detected during analysis. Post-translational modifications such as ...
Related Pictures
★リンクテーブル★
[★]
- 関
- post-translational modification、post-translational protein modification、PTM
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- 関
- post-translational modification、posttranslational modification
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翻訳後修飾, post-translational modification, posttranslational modification
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- 関
- alter、alteration、amend、amendment、change、metamorphic、metamorphosis、metamorphotic、modify、revise、revision
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- after、afterward、afterwards、behind、following、late、posterior、subsequent
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- translate、translation、translationally
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