Gotowa bibliografia na temat „N-terminal modification enzymes”
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Artykuły w czasopismach na temat "N-terminal modification enzymes"
Nakano, Miyako, Sushil K. Mishra, Yuko Tokoro, Keiko Sato, Kazuki Nakajima, Yoshiki Yamaguchi, Naoyuki Taniguchi i Yasuhiko Kizuka. "Bisecting GlcNAc Is a General Suppressor of Terminal Modification of N-glycan". Molecular & Cellular Proteomics 18, nr 10 (2.08.2019): 2044–57. http://dx.doi.org/10.1074/mcp.ra119.001534.
Pełny tekst źródłaSakato-Antoku, Miho, Jeremy L. Balsbaugh i Stephen M. King. "N-Terminal Processing and Modification of Ciliary Dyneins". Cells 12, nr 20 (20.10.2023): 2492. http://dx.doi.org/10.3390/cells12202492.
Pełny tekst źródłaSTOUGHTON, Daniel M., Gerardo ZAPATA, Robert PICONE i Willie F. VANN. "Identification of Arg-12 in the active site of Escherichia coli K1 CMP-sialic acid synthetase". Biochemical Journal 343, nr 2 (8.10.1999): 397–402. http://dx.doi.org/10.1042/bj3430397.
Pełny tekst źródłaRoll-Mecak, Antonina, Agnieszka Szyk i Vasilisa Kormendi. "Microtubule chemical complexity: mechanism of tubulin modification enzymes". Acta Crystallographica Section A Foundations and Advances 70, a1 (5.08.2014): C1286. http://dx.doi.org/10.1107/s2053273314087130.
Pełny tekst źródłaLubelski, Jacek, Wout Overkamp, Leon D. Kluskens, Gert N. Moll i Oscar P. Kuipers. "Influence of Shifting Positions of Ser, Thr, and Cys Residues in Prenisin on the Efficiency of Modification Reactions and on the Antimicrobial Activities of the Modified Prepeptides". Applied and Environmental Microbiology 74, nr 15 (6.06.2008): 4680–85. http://dx.doi.org/10.1128/aem.00112-08.
Pełny tekst źródłaNakonieczna, Joanna, Tadeusz Kaczorowski, Agnieszka Obarska-Kosinska i Janusz M. Bujnicki. "Functional Analysis of MmeI from Methanol Utilizer Methylophilus methylotrophus, a Subtype IIC Restriction-Modification Enzyme Related to Type I Enzymes". Applied and Environmental Microbiology 75, nr 1 (7.11.2008): 212–23. http://dx.doi.org/10.1128/aem.01322-08.
Pełny tekst źródłaKelley, M., i D. A. Vessey. "Structural comparison between the mitochondrial aralkyl-CoA and arylacetyl-CoA N-acyltransferases". Biochemical Journal 288, nr 1 (15.11.1992): 315–17. http://dx.doi.org/10.1042/bj2880315.
Pełny tekst źródłaSmith, Clyde A., Marta Toth, Nichole K. Stewart, Lauren Maltz i Sergei B. Vakulenko. "Structural basis for the diversity of the mechanism of nucleotide hydrolysis by the aminoglycoside-2′′-phosphotransferases". Acta Crystallographica Section D Structural Biology 75, nr 12 (29.11.2019): 1129–37. http://dx.doi.org/10.1107/s2059798319015079.
Pełny tekst źródłaCaillava, Celine, Jean Sevalle i Frederic Checler. "P2-219: identification of enzymes involved in n-terminal truncation and modification of amyloid peptide". Alzheimer's & Dementia 7 (lipiec 2011): S382. http://dx.doi.org/10.1016/j.jalz.2011.05.1101.
Pełny tekst źródłaNashed, Salomé, Houssam El Barbry, Médine Benchouaia, Angélie Dijoux-Maréchal, Thierry Delaveau, Nadia Ruiz-Gutierrez, Lucie Gaulier i in. "Functional mapping of N-terminal residues in the yeast proteome uncovers novel determinants for mitochondrial protein import". PLOS Genetics 19, nr 8 (16.08.2023): e1010848. http://dx.doi.org/10.1371/journal.pgen.1010848.
Pełny tekst źródłaRozprawy doktorskie na temat "N-terminal modification enzymes"
Sunde, Margaret. "N-terminal modification of S-adenosylmethionine decarboxylase". Thesis, University of Cambridge, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.318198.
Pełny tekst źródłaEl, 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.
Pełny tekst źródłaMitochondria are complex organelles involving a thousand proteins, most of which are encoded in the nuclear genome. Their biogenesis has required the evolutionary development of efficient protein addressing and import systems, and failures of these systems are associated with serious pathologies, neuropathies, cardiovascular disorders, myopathies, neurodegenerative diseases and cancers.Many mitochondrial proteins have an N-terminal addressing sequence called MTS (Mitochondrial Targeting Sequence) which forms an amphiphilic alpha helix essential for their mitochondrial import. However, the sequence of the various MTSs is highly variable and their critical characteristics are not yet well understood. The starting point of my thesis was the discovery in yeast of an overrepresentation of 4 hydrophobic amino acids (F, L, I, W) at position 2 of the MTSs sequences. During my thesis, I was able to confirm the critical role of the nature of the residue in position 2 of the MTSs through directed mutagenesis experiments. Indeed, thanks to the development of an innovative system for screening import defects based on the functional rescue of the toxicity of a mitochondrial protein, I was able to observe that only residues overrepresented at position 2 of mitochondrial proteins allowed efficient import. My work has thus demonstrated the existence of strong evolutionary constraints at position 2 of MTSs, the understanding of which could ultimately be useful for optimising the mitochondrial addressing of therapeutic proteins in patients suffering from mitochondrial diseases
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.
Pełny tekst źródłaBoisson, Bertrand. "Caractérisation et fonction de la N-myristoylation du protéome d'Arabidopsis thaliana". Paris 6, 2003. http://www.theses.fr/2003PA066367.
Pełny tekst źródłaPiontek, Alexander. "Deciphering the Catalytic Mechanism of the Zn Enzyme Glutaminyl Cyclase and the Deduction of Transition-State Analog Inhibitors". Doctoral thesis, 2014. http://hdl.handle.net/11858/00-1735-0000-0022-605A-C.
Pełny tekst źródłaCzęści książek na temat "N-terminal modification enzymes"
Pennings, Sari, Timothy E. O’Neill, Geert Meersseman, i E. Morton Bradbury. "Nucleosomes: dynamic repressors of transcription". W Nuclear Organization, Chromatin Structure, and Gene Expression, 3–18. Oxford University PressOxford, 1997. http://dx.doi.org/10.1093/oso/9780198549239.003.0001.
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