Relevant bibliographies by topics / Protein N-terminal modifications

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Reports

Academic literature on the topic 'Protein N-terminal modifications'

Author: Grafiati
Published: 21 December 2024
Last updated: 28 July 2025

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Journal articles on the topic "Protein N-terminal modifications"

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Lai, Zon W., Agnese Petrera, and Oliver Schilling. "Protein amino-terminal modifications and proteomic approaches for N-terminal profiling." Current Opinion in Chemical Biology 24 (February 2015): 71–79. http://dx.doi.org/10.1016/j.cbpa.2014.10.026.

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Voronina, A. I., Yu V. Miroshnichenko, and V. S. Skvortsov. "Bioinformatic identification of proteins with altered PTM levels in a mouse line established to study the mechanisms of the development of fibromuscular dysplasia." Biomeditsinskaya Khimiya 70, no. 4 (2024): 248–55. http://dx.doi.org/10.18097/pbmc20247004248.

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Data from a mass spectrometry experiment of a mouse line developed to study the mechanisms of fibromuscular dysplasia and deposited by d'Escamard et al. in ProteomeXchange (PXD051750) have been analyzed. Identification of peptides with post-translational modifications (PTMs) was repeated using more stringent conditions than in the original work. The following modifications were considered during analysis of changes in the PTM levels in experimental and control groups of mice: acetylation of lysine residue and N-terminal protein peptide, ubiquitination of lysine residue, phosphorylation of seri
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Yu, Guann-Yi, Ki-Jeong Lee, Lu Gao, and Michael M. C. Lai. "Palmitoylation and Polymerization of Hepatitis C Virus NS4B Protein." Journal of Virology 80, no. 12 (2006): 6013–23. http://dx.doi.org/10.1128/jvi.00053-06.

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ABSTRACT Hepatitis C Virus (HCV) NS4B protein induces a specialized membrane structure which may serve as the replication platform for HCV RNA replication. In the present study, we demonstrated that NS4B has lipid modifications (palmitoylation) on two cysteine residues (cysteines 257 and 261) at the C-terminal end. Site-specific mutagenesis of these cysteine residues on individual NS4B proteins and on an HCV subgenomic replicon showed that the lipid modifications, particularly of Cys261, are important for protein-protein interaction in the formation of the HCV RNA replication complex. We furth
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Meinnel, Thierry, and Carmela Giglione. "Tools for analyzing and predicting N-terminal protein modifications." PROTEOMICS 8, no. 4 (2008): 626–49. http://dx.doi.org/10.1002/pmic.200700592.

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Dissmeyer, Nico. "Conditional Protein Function via N-Degron Pathway–Mediated Proteostasis in Stress Physiology." Annual Review of Plant Biology 70, no. 1 (2019): 83–117. http://dx.doi.org/10.1146/annurev-arplant-050718-095937.

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The N-degron pathway, formerly the N-end rule pathway, regulates functions of regulatory proteins. It impacts protein half-life and therefore directs the actual presence of target proteins in the cell. The current concept holds that the N-degron pathway depends on the identity of the amino (N)-terminal amino acid and many other factors, such as the follow-up sequence at the N terminus, conformation, flexibility, and protein localization. It is evolutionarily conserved throughout the kingdoms. One possible entry point for substrates of the N-degron pathway is oxidation of N-terminal Cys residue
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Lee, Seon Hwa, and Tomoyuki Oe. "Oxidative stress-mediated N-terminal protein modifications and MS-based approaches for N-terminal proteomics." Drug Metabolism and Pharmacokinetics 31, no. 1 (2016): 27–34. http://dx.doi.org/10.1016/j.dmpk.2015.12.002.

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Rose, K., P. O. Regamey, R. Anderegg, T. N. C. Wells, and A. E. I. Proudfoot. "Human interleukin-5 expressed in Escherichia coli has N-terminal modifications." Biochemical Journal 286, no. 3 (1992): 825–28. http://dx.doi.org/10.1042/bj2860825.

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Recombinant human interleukin-5 exists as four major isoforms all possessing N-terminal methionine. Peptide mapping and subsequent analysis by fast-atom-bombardment mass spectrometry (f.a.b.-m.s.) have shown that N-terminal modifications are the cause of the charge heterogeneity. In order of decreasing abundance, these are unmodified methionine, retention of N-terminal formyl group, oxidation of N-terminal methionine to sulphoxide and carbamoylation of the N-terminus. These results were confirmed by analysis of the reduced and alkylated intact protein by electrospray-ionization mass spectromet
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Van Damme, Petra. "Charting the N-Terminal Acetylome: A Comprehensive Map of Human NatA Substrates." International Journal of Molecular Sciences 22, no. 19 (2021): 10692. http://dx.doi.org/10.3390/ijms221910692.

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N-terminal acetylation (Nt-acetylation) catalyzed by conserved N-terminal acetyltransferases or NATs embodies a modification with one of the highest stoichiometries reported for eukaryotic protein modifications to date. Comprising the catalytic N-alpha acetyltransferase (NAA) subunit NAA10 plus the ribosome anchoring regulatory subunit NAA15, NatA represents the major acetyltransferase complex with up to 50% of all mammalian proteins representing potential substrates. Largely in consequence of the essential nature of NatA and its high enzymatic activity, its experimentally confirmed mammalian
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Ouidir, Tassadit, Frédérique Jarnier, Pascal Cosette, Thierry Jouenne, and Julie Hardouin. "Characterization of N-terminal protein modifications in Pseudomonas aeruginosa PA14." Journal of Proteomics 114 (January 2015): 214–25. http://dx.doi.org/10.1016/j.jprot.2014.11.006.

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Giglione, Carmela, Sonia Fieulaine, and Thierry Meinnel. "N-terminal protein modifications: Bringing back into play the ribosome." Biochimie 114 (July 2015): 134–46. http://dx.doi.org/10.1016/j.biochi.2014.11.008.

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Dissertations / Theses on the topic "Protein N-terminal modifications"

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Xie, Dong. "Uncovering the maturation pathway of plant Rubisco." Electronic Thesis or Diss., université Paris-Saclay, 2024. http://www.theses.fr/2024UPASL080.

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Lors de la photosynthèse, l’assimilation sous formes de glucides du dioxyde de carbone atmosphérique (CO₂), le principal gaz à effet de serre anthropique, est catalysée par l'enzyme Rubisco, la protéine la plus abondante sur terre. La grande sous-unité de la Rubisco (RbcL) subit une voie de maturation unique conduisant à des modifications N-terminales inhabituelles. Ce mécanisme conservé chez les plantes, résulte en une proline acétylée N-terminale en position 3. Décrypter la voie de maturation de Rubisco est donc une question clé pour la fixation du CO₂ dans le contexte des changements climat
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Connor, Rebecca E. Barton Jacqueline K. Tirrell David A. "N-terminal modification and codon reassignment with non-canonical amino acids in proteins /." Diss., Pasadena, Calif. : California Institute of Technology, 2008. http://resolver.caltech.edu/CaltechETD:etd-03052008-065324.

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Liu, Li. "Purification and characterization of a protein palmitoyltransferase that acts on H-Ras protein and on a C-terminal N-Ras peptide /." Thesis, Connect to this title online; UW restricted, 1996. http://hdl.handle.net/1773/8664.

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Lavecchia, Francesco. "Integrative Approaches to Decode the Co-translational Role of the Phage Vp16 Peptide Deformylase and how it Compromises Host Viability." Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLS004/document.

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L'excision de la méthionine N-terminale (NME) est la première modification se produisant au N-terminal des protéines (NPM). Les peptides déformylases (PDF) sont les enzymes impliquées dans ce processus co-traductionnel essentiel et conservé. Les PDFs suppriment le groupe formyle lié à la méthionine initiatrice (iMet) présente au début de toutes les chaînes procaryotes naissantes. Les PDFs agissent au niveau du tunnel de sortie des ribosomes, plaque tournante de nombreux facteurs de biogénèse des protéines associées aux ribosomes (PRB), impliqués non seulement sur les MNP, mais également dans l
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Kshetri, Man B. "N-TERMINAL DOMAIN OF rRNA METHYLTRANSFERASE ENZYME RsmC IS IMPORTANT FOR ITS BINDING TO RNA AND RNA CHAPERON ACTIVITY." Kent State University Honors College / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=ksuhonors1621007414429417.

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El, Barbry Houssam. "Découverte du rôle crucial du résidu en position 2 des séquences MTS d’adressage mitochondrial." Electronic Thesis or Diss., Sorbonne université, 2023. http://www.theses.fr/2023SORUS035.

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Les mitochondries sont des organites complexes impliquant un millier de protéines, la plupart codées dans le génome nucléaire. Leur biogenèse a nécessité au cours de l’évolution la mise en place de systèmes efficaces d’adressage et d’import protéique, et des défaillances de ces systèmes sont associées à des pathologies graves, neuropathies, troubles cardiovasculaires, myopathies, maladies neurodégénératives ainsi que cancers. De nombreuses protéines mitochondriales possèdent en N-terminal une séquence d’adressage appelée MTS (Mitochondrial Targeting sequence) qui forme une hélice alpha amphiph
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Zákoucká, Eva. "Proteomická a bioinformatická charakterizace N-terminálních sekvencí proteinů modifikovaných po importu do hydrogenosomu Trichomonas vaginalis." Master's thesis, 2014. http://www.nusl.cz/ntk/nusl-337356.

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Trichomonas vaginalis is a human pathogen causing trichomoniasis, one of the most common non-viral sexually transmitted diseases in both men and women. Trichomoniasis is currently treated with metronidazole, but the pathogen is known to develop resistance against this drug. However as the pathogen is eukaryotic, the targets for the pathogen elimination without seriously affecting the host are limited. Throughout the evolution Trichomonas vaginalis adapted to anaerobic environments by developing an alternative metabolism resulting in a reduced form of mitochondria named hydrogenosome. Hydrogeno
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Connor, Rebecca Elizabeth. "N-Terminal Modification and Codon Reassignment with Non-Canonical Amino Acids in Proteins." Thesis, 2008. https://thesis.library.caltech.edu/878/8/ConnorTOC.pdf.

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Proteins are ubiquitous macromolecules that effect and control all the processes of life from reproduction to respiration to physical motion. These diverse molecules also provide physical structure and defensive mechanisms. The twenty canonical amino acids can be found in virtually every protein; however, in some organisms, the set of endogenous amino acids also contains residues outside the “canon,” such as pyrrolysine, selenocysteine, and formylmethionine. Although a range of chemistries is available through natural side-chain diversity, some functionalities such as halogens, ketones, azide
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Books on the topic "Protein N-terminal modifications"

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Wetzel, Ronald, and Rakesh Mishra. Structural Biology. Oxford University Press, 2014. http://dx.doi.org/10.1093/med/9780199929146.003.0012.

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The 3,144–amino acid huntingtin protein (HTT) folds in water into a structure consisting of compact, organized domains interspersed with intrinsically disordered protein (IDP) elements. The IDPs function as sites of post-translational modifications and proteolysis as well as in targeting, binding, and aggregation. Although the dominant structural motif of HTT is the α‎-helix–rich HEAT repeat, the expanded polyglutamine (polyQ) toxicity responsible for Huntington’s disease is most likely played out within intrinsically disordered HTT exon 1–like fragments consisting of the 16– to 17–amino acid
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Book chapters on the topic "Protein N-terminal modifications"

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Ciechanover, Aaron. "N-terminal Ubiquitination: No Longer Such a Rare Modification." In Protein Degradation. Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/352760586x.ch2.

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Acikalin Coskun, Kubra, Nazlıcan Yurekli, Elif Cansu Abay, Merve Tutar, Mervenur Al, and Yusuf Tutar. "Structure- and Design-Based Difficulties in Recombinant Protein Purification in Bacterial Expression." In Protein Detection [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.103958.

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Protein purification is not a simple task. Yet, overexpression at bacterial systems with recombinant modifications brings further difficulties. Adding a tag, an affinity label, and expressing particular domains of the whole protein, especially hydrophobic sections, make purification a challenging process. Protein folding pattern may perturb N- or C-terminal tag and this terminal preference may lead to poor purification yield. Codon optimization, solvent content and type, ionic conditions, resin types, and self-cleavage of recombinant proteins bring further difficulties to protein expression an
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Arnesen, Thomas. "Preface – The impact of protein N- and C-terminal modifications." In Methods in Enzymology. Elsevier, 2023. http://dx.doi.org/10.1016/s0076-6879(23)00248-3.

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Barlowe, Charles, Randy Schekman, and Aki Nakano. "Sarlp." In Guidebook to the Sinall GTPases. Oxford University PressOxford, 1995. http://dx.doi.org/10.1093/oso/9780198599456.003.0150.

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Abstract The SAR1 gene (EMBL accession number X51667) contains an intervening sequence that after splicing predicts an open reading frame of 190 amino acids. SAR1 cDNA sequencing confirms the excision of a 139 bp intron. Sari protein contains the four consensus motifs characteristic of GTPases (Bourne et al. 1991), although there are other notable features contained within the protein sequence. Sari p does not contain a C-terminal cysteine or an N-terminal glycine as potential residues for lipid modification, a feature observed in a number of other small GTPases.
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Lahnstein, Jelle, Shanny L. Dyer, Neil H. Goss, Mark Duncan, and Raymond S. Norton. "N-TERMINAL MODIFICATION OF MALARIAL ANTIGENS FROM E. coli." In Techniques in Protein Chemistry IV. Elsevier, 1993. http://dx.doi.org/10.1016/b978-0-12-058757-5.50014-7.

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Wu, Pengguang, and Ludwig Brand. "[15] N-terminal modification of proteins for fluorescence measurements." In Methods in Enzymology. Elsevier, 1997. http://dx.doi.org/10.1016/s0076-6879(97)78017-0.

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Reports on the topic "Protein N-terminal modifications"

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Ehrlich, Marcelo, John S. Parker, and Terence S. Dermody. Development of a Plasmid-Based Reverse Genetics System for the Bluetongue and Epizootic Hemorrhagic Disease Viruses to Allow a Comparative Characterization of the Function of the NS3 Viroporin in Viral Egress. United States Department of Agriculture, 2013. http://dx.doi.org/10.32747/2013.7699840.bard.

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Project Title: "Development of a plasmid-based reverse genetics system for the Bluetongue and Epizootic Hemorrhagic Disease viruses to allow comparative characterization of the function of the NS3 viroporin in viral egress". Project details: No - IS-4192-09; Participants – Ehrlich M. (Tel Aviv University), Parker J.S. (Cornell University), DermodyT.S. (Vanderbilt University); Period - 2009-2013. Orbiviruses are insect-borne infectious agents of ruminants that cause diseases with considerable economical impact in Israel and the United States. The recent outbreaks of BTV in Europe and of Epizoot
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