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Find link is a tool written by Edward Betts.searching for N-terminal acetylation 33 found (39 total)
alternate case: n-terminal acetylation
Protein acetylation
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involved in central metabolism of Salmonella enterica are acetylated. N-terminal acetylation is one of the most common co-translational covalent modificationsN-alpha-acetyltransferase 10 (5,357 words) [view diff] exact match in snippet view article find links to article
2003). "N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins". Journal of Molecular Biology. 325 (4):LENG9 (1,513 words) [view diff] exact match in snippet view article find links to article
undergo post-translational modifications such as phosphorylation, N-terminal acetylation, sumoylation, and C-terminal Glycosylphosphatidylinositol (GPI)CobB (1,885 words) [view diff] exact match in snippet view article find links to article
"Modulation of the bacterial CobB sirtuin deacylase activity by N-terminal acetylation". Proceedings of the National Academy of Sciences of the UnitedNAA15 (3,013 words) [view diff] exact match in snippet view article find links to article
Arnesen T, Marmorstein R (September 2013). "Molecular basis for N-terminal acetylation by the heterodimeric NatA complex". Nature Structural & MolecularNAA60 (1,282 words) [view diff] exact match in snippet view article find links to article
fragmentation leading to the hypothesis that NAA60 is essential for the N-terminal acetylation of membrane proteins critical for normal Golgi function. ChelbanJean Baum (700 words) [view diff] exact match in snippet view article find links to article
Ashcroft, Alison E.; Radford, Sheena E.; Baum, Jean (July 2012). "N-terminal acetylation of α-synuclein induces increased transient helical propensity andOgden syndrome (1,076 words) [view diff] exact match in snippet view article find links to article
less effective at N-terminal acetylation than the normal protein, causing a multitude of effects for the baby, as N-terminal acetylation is one of the mostSUHW4 (1,163 words) [view diff] exact match in snippet view article find links to article
The glycine residue at position 2 is a probable candidate for N-terminal acetylation. There are seven probable sumoylation sites. ZNF280D is ubiquitouslyPeptide alpha-N-acetyltransferase (277 words) [view diff] exact match in snippet view article find links to article
de Jong WW, Tesser GI, Bloemendal H (1985). "The mechanism of N-terminal acetylation of proteins". CRC Crit. Rev. Biochem. 18 (4): 281–325. doi:10Coactivator (genetics) (1,698 words) [view diff] exact match in snippet view article
(July 2011). "NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation". PLOS GeneticsARFRP1 (733 words) [view diff] exact match in snippet view article find links to article
"Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p". Nat. Cell Biol. 6 (5): 405–13.FAM149A (1,841 words) [view diff] exact match in snippet view article find links to article
NetAcet: Predicts N-terminal acetylation sites. Here are the results: According to NetAcet, there are no N-terminal acetylation sites for FAM149A. SUMOplot/SUMOsp:Protein primary structure (2,599 words) [view diff] exact match in snippet view article find links to article
Fig. 1 N-terminal acetylationTMEM260 (528 words) [view diff] case mismatch in snippet view article find links to article
different kinds of post translational modifications. These include N-terminal Acetylation, N-Glycosylation, and Phosphorylation. GRCh38: Ensembl release 89:R. Kip Guy (487 words) [view diff] exact match in snippet view article find links to article
became the first to show that protein interaction controlled by N-terminal acetylation could be blocked. Following this discovery, Guy was elected a FellowAlpha-1-B glycoprotein (1,379 words) [view diff] exact match in snippet view article find links to article
Kiemer L, Bendtsen JD, Blom N (April 2005). "NetAcet: prediction of N-terminal acetylation sites". Bioinformatics. 21 (7): 1269–70. doi:10.1093/bioinformatics/bti130CCDC113 (1,000 words) [view diff] exact match in snippet view article find links to article
predicted post-translational modifications including phosphorylation, N-terminal acetylation, sumoylation, and N-glycosylation. The function of CCDC113 is currentlyC19orf44 (865 words) [view diff] exact match in snippet view article find links to article
tools on ExPASy and are shown in the protein illustration below. N-terminal acetylation is predicted at S3. There is also a predicted sumoylation motifProtein sequencing (2,836 words) [view diff] exact match in snippet view article find links to article
too short or too long), being post-translationally modified (e.g. N-terminal acetylation) or genuinely differing from the prediction. Post-translationalZC3H12B (1,010 words) [view diff] exact match in snippet view article find links to article
(July 2011). "NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation". PLOS GeneticsTransmembrane protein 251 (1,086 words) [view diff] exact match in snippet view article find links to article
phosphorylation sites. PKC phosphorylation site on Threonine-26. N-terminal acetylation site at the A position of –MLAFSE. SUMO interaction site on aminoPrimary familial brain calcification (2,509 words) [view diff] exact match in snippet view article find links to article
Kaiyrzhanov, Rauan (2024-03-13). "Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications"Rüdiger Hell (903 words) [view diff] exact match in snippet view article find links to article
Giglione, C., Hell, R., Wirtz, M. (2015). "Proteome imprinting by N-terminal acetylation is a vital hormone-regulated switch during drought stress". NatureTMEM171 (1,630 words) [view diff] exact match in snippet view article find links to article
non-cytosolic domains. TMEM171 undergoes methionine cleavage and N-terminal acetylation, which is one of the most common modifications of eukaryotic proteinsYIF1A (1,714 words) [view diff] exact match in snippet view article find links to article
extracellular C-terminus. YIF1A undergoes methionine cleavage and N-terminal acetylation, which is one of the most common post translation modificationsCoiled-coil domain-containing 37 (FLJ40083) (820 words) [view diff] case mismatch in snippet view article
Lars, Kyrlov Bendtsen, and Blom, Nikolai. NetAcet: Prediction of N-terminal Acetylation Sites. Bioinformatics, 2004. A. Reinhardt and T. Hubbard, NucleicC2orf16 (1,941 words) [view diff] exact match in snippet view article find links to article
Kiemer L, Bendtsen JD, Blom N (April 2005). "NetAcet: prediction of N-terminal acetylation sites". Bioinformatics. 21 (7): 1269–70. doi:10.1093/bioinformatics/bti130MGC50722 (1,555 words) [view diff] exact match in snippet view article find links to article
also predict more phosphorylation sites (NetPhos 2.0 Server), a N-terminal acetylation site (NetAcet 1.0 Server), glycation sites (NetGlycate 1.0 Server)S100A10 (4,728 words) [view diff] exact match in snippet view article find links to article
recombinant annexin II tetramer purified from bacteria: role of N-terminal acetylation". Biochemistry. 36 (8): 2041–50. doi:10.1021/bi962569b. PMID 9047302FAM149B1 (1,887 words) [view diff] exact match in snippet view article find links to article
2017-05-07. "PSORT prediction tool". GenScript. NetAcet: Prediction of N-terminal acetylation sites., Accessed through Expasy. Lars Kiemer, Jannick Dyrløv BendtsenAlpha-synuclein (9,387 words) [view diff] case mismatch in snippet view article find links to article
PMC 3548493. PMID 23184946. Trexler AJ, Rhoades E (May 2012). "N-Terminal acetylation is critical for forming α-helical oligomer of α-synuclein". ProteinCCDC130 (2,561 words) [view diff] exact match in snippet view article find links to article
Kiemer L, Bendtsen JD, Blom N (2005). "NetAcet: prediction of N-terminal acetylation sites". Bioinformatics. 21 (7): 1269–70. doi:10.1093/bioinformatics/bti130