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Artículos de revistas sobre el tema "PROTEIN N"

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Publicado: 11 de septiembre de 2023

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1

Duclos, S., P. Da Silva, F. Vovelle, F. Piller y V. Piller. "Characterization of the UDP-N-acetylgalactosamine binding domain of bovine polypeptide N-acetylgalactosaminyltransferase T1". Protein Engineering Design and Selection 17, n.º 8 (23 de septiembre de 2004): 635–46. http://dx.doi.org/10.1093/protein/gzh075.

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2

Koyama, Y., M. Hidaka, M. Nishimoto y M. Kitaoka. "Directed evolution to enhance thermostability of galacto-N-biose/lacto-N-biose I phosphorylase". Protein Engineering Design and Selection 26, n.º 11 (24 de septiembre de 2013): 755–61. http://dx.doi.org/10.1093/protein/gzt049.

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3

Gordon, J. I., R. J. Duronio, D. A. Rudnick, S. P. Adams y G. W. Gokel. "Protein N-myristoylation". Journal of Biological Chemistry 266, n.º 14 (mayo de 1991): 8647–50. http://dx.doi.org/10.1016/s0021-9258(18)31490-x.

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4

Flanagan, Karen, John Walshaw, Sarah L. Price y Julia M. Goodfellow. "Solvent interactions with n ring systems in proteins". "Protein Engineering, Design and Selection" 8, n.º 2 (1995): 109–16. http://dx.doi.org/10.1093/protein/8.2.109.

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5

Imberty, A. y S. Perez. "Stereochemistry of the N-glycosylation sites in glycoproteins". Protein Engineering Design and Selection 8, n.º 7 (1 de julio de 1995): 699–709. http://dx.doi.org/10.1093/protein/8.7.699.

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6

Roth, Jürgen, Christian Zuber, Sujin Park, Insook Jang, Yangsin Lee, Katarina Gaplovska Kysela, Valérie Fourn, Roger Santimaria, Bruno Guhl y Jin Won Cho. "Protein N-glycosylation, protein folding, and protein quality control". Molecules and Cells 30, n.º 6 (26 de noviembre de 2010): 497–506. http://dx.doi.org/10.1007/s10059-010-0159-z.

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7

Hope, John N., Hao-Chia Chen y J. Fidding Hejtmancik. "βA3/Al-crystallin association: role of the N-terminal arm". "Protein Engineering, Design and Selection" 7, n.º 3 (1994): 445–51. http://dx.doi.org/10.1093/protein/7.3.445.

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8

Kumar, Kapila, Sreejith Rajasekharan, Sahil Gulati, Jyoti Rana, Reema Gabrani, Chakresh K. Jain, Amita Gupta, Vijay K. Chaudhary y Sanjay Gupta. "Elucidating the Interacting Domains ofChandipuraVirus Nucleocapsid Protein". Advances in Virology 2013 (2013): 1–9. http://dx.doi.org/10.1155/2013/594319.

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The nucleocapsid (N) protein ofChandipuravirus (CHPV) plays a crucial role in viral life cycle, besides being an important structural component of the virion through proper organization of its interactions with other viral proteins. In a recent study, the authors had mapped the associations among CHPV proteins and shown that N protein interacts with four of the viral proteins: N, phosphoprotein (P), matrix protein (M), and glycoprotein (G). The present study aimed to distinguish the regions of CHPV N protein responsible for its interactions with other viral proteins. In this direction, we have generated the structure of CHPV N protein by homology modeling using SWISS-MODEL workspace and Accelrys Discovery Studio client 2.55 and mapped the domains of N protein using PiSQRD. The interactions of N protein fragments with other proteins were determined by ZDOCK rigid-body docking method and validated by yeast two-hybrid and ELISA. The study revealed a unique binding site, comprising of amino acids 1–30 at the N terminus of the nucleocapsid protein (N1) that is instrumental in its interactions with N, P, M, and G proteins. It was also observed that N2 associates with N and G proteins while N3 interacts with N, P, and M proteins.

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9

Doughty, S. W., F. E. Blaney, B. S. Orlek y W. G. Richards. "A molecular mechanism for toxin block in N-type calcium channels". Protein Engineering Design and Selection 11, n.º 2 (1 de febrero de 1998): 95–99. http://dx.doi.org/10.1093/protein/11.2.95.

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10

Li, Hui-Guang, Shi-Zhen Xu, Shen Wu, Li Yan, Jian-Hui Li, Richy N. S. Wong, Qing-Li Shi y Yi-Cheng Dong. "Role of Arg163 in the N-glycosidase activity of neo-trichosanthin". Protein Engineering, Design and Selection 12, n.º 11 (noviembre de 1999): 999–1004. http://dx.doi.org/10.1093/protein/12.11.999.

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11

Medvedkin, Vyacheslav N., Eugene A. Permyakov, Lyubov V. Klimenko, Yuri V. Mitin, Norio Matsushima, Susumu Nakayama y Robert H. Kretsinger. "Interactions of (Ala*Ala*Lys*Pro)n and (Lys*Lys*Ser*Pro)n with DNA. Proposed coiled-coil structure of AlgR3 and AlgP from Pseudomonas aeruginosa". "Protein Engineering, Design and Selection" 8, n.º 1 (1995): 63–70. http://dx.doi.org/10.1093/protein/8.1.63.

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12

Van Damme, Petra, Thomas Arnesen y Kris Gevaert. "Protein alpha-N-acetylation studied by N-terminomics". FEBS Journal 278, n.º 20 (2 de agosto de 2011): 3822–34. http://dx.doi.org/10.1111/j.1742-4658.2011.08230.x.

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13

Boza, Julio J., Olga Martínez-Augustin, Luis Baró, M. Dolores Suarez y Angel Gil. "Protein v. enzymic protein hydrolysates. Nitrogen utilization in starved rats". British Journal of Nutrition 73, n.º 1 (enero de 1995): 65–71. http://dx.doi.org/10.1079/bjn19950009.

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The present study was carried out to compare the effects of four isoenergetic and isonitrogenous diets on the N utilization, total serum protein concentration and serum amino acid profile in starved rats at weaning. These diets differed only in the molecular form of two milk proteins (whey protein and casein), which were either native or partly hydrolysed. Male Wistar rats at weaning were fasted for 3 d and then refed with one of the four diets for 48 h. No differences were observed in the body weight gain, protein digestibility and total serum protein concentration between groups after the refeeding period and all the N balances were positive. N retention was higher in the two groups of rats given the protein-hydrolysate-based diets compared with those given the intact-protein-based diets. This was associated with a lower urinary N excretion in rats, given the whey-protein-hydrolysate and the casein-hydrolysate diets. Despite this fact, the serum amino acid pattern of rats given the hydrolysed protein diet was very similar to that of those given the corresponding native protein diet. In conclusion, we have proved that enzymic hydrolysates from milk proteins have equivalent effects to native proteins in recovery after starvation in rats at weaning, on N absorption, total serum protein concentration and serum amino acid profile, and even give a higher N retention. We did not observe any harmful effect in using protein hydrolysates instead of native proteins.

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14

Gaudry, A., B. Lorber, A. Neuenfeldt, C. Sauter, C. Florentz y M. Sissler. "Re-designed N-terminus enhances expression, solubility and crystallizability of mitochondrial protein". Protein Engineering Design and Selection 25, n.º 9 (7 de agosto de 2012): 473–81. http://dx.doi.org/10.1093/protein/gzs046.

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15

Wang, M., L. S. Lee, A. Nepomich, J. D. Yang, C. Conover, M. Whitlow y D. Filpula. "Single-chain Fv with manifold N-glycans as bifunctional scaffolds for immunomolecules". Protein Engineering Design and Selection 11, n.º 12 (1 de diciembre de 1998): 1277–83. http://dx.doi.org/10.1093/protein/11.12.1277.

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16

Benito, A., M. Bosch, G. Torrent, M. Ribó y M. Vilanova. "Stabilization of human pancreatic ribonuclease through mutation at its N-terminal edge". Protein Engineering, Design and Selection 15, n.º 11 (noviembre de 2002): 887–93. http://dx.doi.org/10.1093/protein/15.11.887.

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17

Hollebeke, Jolien, Petra Van Damme y Kris Gevaert. "N-terminal acetylation and other functions of Nα-acetyltransferases". Biological Chemistry 393, n.º 4 (1 de abril de 2012): 291–98. http://dx.doi.org/10.1515/hsz-2011-0228.

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Abstract Protein N-terminal acetylation by Nα-acetyltransferases (NATs) is an omnipresent protein modification that affects a large number of proteins. The exact biological role of N-terminal acetylation has, however, remained enigmatic for the overall majority of affected proteins, and only for a rather small number of proteins, N-terminal acetylation was linked to various protein features including stability, localization, and interactions. This minireview tries to summarize the recent progress made in understanding the functionality of N-terminal protein acetylation and also focuses on noncanonical functions of the NATs subunits.

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18

Aubol, Brandon E., Ryan M. Plocinik, Malik M. Keshwani, Maria L. McGlone, Jonathan C. Hagopian, Gourisankar Ghosh, Xiang-Dong Fu y Joseph A. Adams. "N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation". Biochemical Journal 462, n.º 1 (24 de julio de 2014): 143–52. http://dx.doi.org/10.1042/bj20140494.

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19

Clerc, Florent, Karli R. Reiding, Bas C. Jansen, Guinevere S. M. Kammeijer, Albert Bondt y Manfred Wuhrer. "Human plasma protein N-glycosylation". Glycoconjugate Journal 33, n.º 3 (10 de noviembre de 2015): 309–43. http://dx.doi.org/10.1007/s10719-015-9626-2.

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20

Wu, Di, Weston B. Struwe, David J. Harvey, Michael A. J. Ferguson y Carol V. Robinson. "N-glycan microheterogeneity regulates interactions of plasma proteins". Proceedings of the National Academy of Sciences 115, n.º 35 (15 de agosto de 2018): 8763–68. http://dx.doi.org/10.1073/pnas.1807439115.

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Altered glycosylation patterns of plasma proteins are associated with autoimmune disorders and pathogenesis of various cancers. Elucidating glycoprotein microheterogeneity and relating subtle changes in the glycan structural repertoire to changes in protein–protein, or protein–small molecule interactions, remains a significant challenge in glycobiology. Here, we apply mass spectrometry-based approaches to elucidate the global and site-specific microheterogeneity of two plasma proteins: α1-acid glycoprotein (AGP) and haptoglobin (Hp). We then determine the dissociation constants of the anticoagulant warfarin to different AGP glycoforms and reveal how subtle N-glycan differences, namely, increased antennae branching and terminal fucosylation, reduce drug-binding affinity. Conversely, similar analysis of the haptoglobin–hemoglobin (Hp–Hb) complex reveals the contrary effects of fucosylation and N-glycan branching on Hp–Hb interactions. Taken together, our results not only elucidate how glycoprotein microheterogeneity regulates protein–drug/protein interactions but also inform the pharmacokinetics of plasma proteins, many of which are drug targets, and whose glycosylation status changes in various disease states.

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21

De Rosa, Lucia, Rossella Di Stasi, Alessandra Romanelli y Luca Domenico D’Andrea. "Exploiting Protein N-Terminus for Site-Specific Bioconjugation". Molecules 26, n.º 12 (9 de junio de 2021): 3521. http://dx.doi.org/10.3390/molecules26123521.

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Although a plethora of chemistries have been developed to selectively decorate protein molecules, novel strategies continue to be reported with the final aim of improving selectivity and mildness of the reaction conditions, preserve protein integrity, and fulfill all the increasing requirements of the modern applications of protein conjugates. The targeting of the protein N-terminal alpha-amine group appears a convenient solution to the issue, emerging as a useful and unique reactive site universally present in each protein molecule. Herein, we provide an updated overview of the methodologies developed until today to afford the selective modification of proteins through the targeting of the N-terminal alpha-amine. Chemical and enzymatic strategies enabling the selective labeling of the protein N-terminal alpha-amine group are described.

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22

Wallin, E. y G. von Heijne. "Properties of N-terminal tails in G-protein coupled receptors: a statistical study". Protein Engineering Design and Selection 8, n.º 7 (1 de julio de 1995): 693–98. http://dx.doi.org/10.1093/protein/8.7.693.

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23

Werten, Paul J. L., John A. Carver, Rainer Jaenicke y Wilfried W. de Jong. "The elusive role of the N-terminal extension of βA3- and βAl-crystallin". "Protein Engineering, Design and Selection" 9, n.º 11 (1996): 1021–28. http://dx.doi.org/10.1093/protein/9.11.1021.

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24

Kwan, Emily M., Alisdair B. Boraston, Bradley W. McLean, Douglas G. Kilburn y R. Antony J. Warren. "N-Glycosidase–carbohydrate-binding module fusion proteins as immobilized enzymes for protein deglycosylation". Protein Engineering, Design and Selection 18, n.º 10 (9 de septiembre de 2005): 497–501. http://dx.doi.org/10.1093/protein/gzi055.

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25

Ishikawa, N., T. Chiba, L. T. Chen, A. Shimizu, M. Ikeguchi y S. Sugai. "Remarkable destabilization of recombinant alpha-lactalbumin by an extraneous N-terminal methionyl residue". Protein Engineering Design and Selection 11, n.º 5 (1 de mayo de 1998): 333–35. http://dx.doi.org/10.1093/protein/11.5.333.

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26

Lins, L., C. Flore, L. Chapelle, P. J. Talmud, A. Thomas y R. Brasseur. "Lipid-interacting properties of the N-terminal domain of human apolipoprotein C-III". Protein Engineering, Design and Selection 15, n.º 6 (junio de 2002): 513–20. http://dx.doi.org/10.1093/protein/15.6.513.

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27

Mammadova-Bach, Elmina, Jaak Jaeken, Thomas Gudermann y Attila Braun. "Platelets and Defective N-Glycosylation". International Journal of Molecular Sciences 21, n.º 16 (6 de agosto de 2020): 5630. http://dx.doi.org/10.3390/ijms21165630.

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N-glycans are covalently linked to an asparagine residue in a simple acceptor sequence of proteins, called a sequon. This modification is important for protein folding, enhancing thermodynamic stability, and decreasing abnormal protein aggregation within the endoplasmic reticulum (ER), for the lifetime and for the subcellular localization of proteins besides other functions. Hypoglycosylation is the hallmark of a group of rare genetic diseases called congenital disorders of glycosylation (CDG). These diseases are due to defects in glycan synthesis, processing, and attachment to proteins and lipids, thereby modifying signaling functions and metabolic pathways. Defects in N-glycosylation and O-glycosylation constitute the largest CDG groups. Clotting and anticlotting factor defects as well as a tendency to thrombosis or bleeding have been described in CDG patients. However, N-glycosylation of platelet proteins has been poorly investigated in CDG. In this review, we highlight normal and deficient N-glycosylation of platelet-derived molecules and discuss the involvement of platelets in the congenital disorders of N-glycosylation.

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28

Munson, Mary y Nia J. Bryant. "A role for the syntaxin N-terminus". Biochemical Journal 418, n.º 1 (28 de enero de 2009): e1-e3. http://dx.doi.org/10.1042/bj20082389.

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Intracellular membrane fusion steps in eukaryotes require the syntaxin family of SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor) proteins. Syntaxins are regulated at several levels through interactions with regulatory proteins, including the SM (Sec1p/Munc18) proteins. Key to understanding this regulation is the characterization of different SM–syntaxin binding interactions at the molecular level and in terms of their contribution to function in vivo. The most conserved SM–syntaxin binding mode is through interaction of the syntaxin's extreme N-terminal peptide with a hydrophobic pocket on the surface of the SM protein. Surprisingly, mutant versions of two different SM proteins abrogated for this binding display no discernable phenotypes in vivo. In this issue of the Biochemical Journal, Johnson et al. demonstrate that loss of the N-terminal binding interaction between the syntaxin UNC-64 and the SM protein UNC-18 severely impairs neuromuscular synaptic transmission in Caenorhabditis elegans, resulting in an unco-ordinated phenotype. In contrast, loss of a second mode of SM–syntaxin binding has no detectable effect. Collectively, these results suggest that, although different membrane trafficking steps are all regulated by SM–syntaxin interactions using similar binding modes, they are differentially regulated, highlighting the need for careful dissection of the binding modes.

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29

Valentine, William M., Venkataraman Amarnath, Kalyani Amarnath, Fred Rimmele y Doyle G. Graham. "Carbon Disulfide Mediated Protein Crosslinking by N,N-Diethyldithiocarbamate". Chemical Research in Toxicology 8, n.º 1 (enero de 1995): 96–102. http://dx.doi.org/10.1021/tx00043a013.

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30

Eldeeb, Mohamed A., Richard P. Fahlman, Mohamed A. Ragheb y Mansoore Esmaili. "Does N‐Terminal Protein Acetylation Lead to Protein Degradation?" BioEssays 41, n.º 11 (24 de septiembre de 2019): 1800167. http://dx.doi.org/10.1002/bies.201800167.

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31

Welke, Robert-William, Hannah Sabeth Sperber, Ronny Bergmann, Amit Koikkarah, Laura Menke, Christian Sieben, Detlev H. Krüger, Salvatore Chiantia, Andreas Herrmann y Roland Schwarzer. "Characterization of Hantavirus N Protein Intracellular Dynamics and Localization". Viruses 14, n.º 3 (23 de febrero de 2022): 457. http://dx.doi.org/10.3390/v14030457.

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Hantaviruses are enveloped viruses that possess a tri-segmented, negative-sense RNA genome. The viral S-segment encodes the multifunctional nucleocapsid protein (N), which is involved in genome packaging, intracellular protein transport, immunoregulation, and several other crucial processes during hantavirus infection. In this study, we generated fluorescently tagged N protein constructs derived from Puumalavirus (PUUV), the dominant hantavirus species in Central, Northern, and Eastern Europe. We comprehensively characterized this protein in the rodent cell line CHO-K1, monitoring the dynamics of N protein complex formation and investigating co-localization with host proteins as well as the viral glycoproteins Gc and Gn. We observed formation of large, fibrillar PUUV N protein aggregates, rapidly coalescing from early punctate and spike-like assemblies. Moreover, we found significant spatial correlation of N with vimentin, actin, and P-bodies but not with microtubules. N constructs also co-localized with Gn and Gc albeit not as strongly as the glycoproteins associated with each other. Finally, we assessed oligomerization of N constructs, observing efficient and concentration-dependent multimerization, with complexes comprising more than 10 individual proteins.

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32

Ray, L. Bryan. "Providing for protein synthesis". Science 372, n.º 6545 (27 de mayo de 2021): 929.14–929. http://dx.doi.org/10.1126/science.372.6545.929-n.

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33

Szuromi, Phil. "Probing protein-nanorod aggregates". Science 365, n.º 6460 (26 de septiembre de 2019): 1414.14–1416. http://dx.doi.org/10.1126/science.365.6460.1414-n.

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34

Naidoo, K. J., D. Denysyk y J. W. Brady. "Molecular dynamics simulations of the N-linked oligosaccharide of the lectin from Erythrina corallodendron". Protein Engineering Design and Selection 10, n.º 11 (1 de noviembre de 1997): 1249–61. http://dx.doi.org/10.1093/protein/10.11.1249.

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35

Utsumi, Toshihikto, Masahiro Sato y Rumi Ishisaka. "Analysis of N-terminal sequence requirements for protein N-myristoylation and protein N-acetylation by in vitro translation system". Biochemical Society Transactions 28, n.º 5 (1 de octubre de 2000): A355. http://dx.doi.org/10.1042/bst028a355b.

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36

Stokes, H. L., A. J. Easton y A. C. Marriott. "Chimeric pneumovirus nucleocapsid (N) proteins allow identification of amino acids essential for the function of the respiratory syncytial virus N protein". Journal of General Virology 84, n.º 10 (1 de octubre de 2003): 2679–83. http://dx.doi.org/10.1099/vir.0.19370-0.

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The nucleocapsid (N) protein of the pneumovirus respiratory syncytial virus (RSV) is a major structural protein which encapsidates the RNA genome and is essential for replication and transcription of the RSV genome. The N protein of the related virus pneumonia virus of mice (PVM) is functionally unable to replace the RSV N protein in a minigenome replication assay. Using chimeric proteins, in which the immediate C-terminal part of the RSV N protein was replaced with the equivalent region of the PVM N protein, it was shown that six amino acid residues near the C terminus of the N protein (between residues 352–369) are essential for its function in replication and for the ability of the N protein to bind to the viral phosphoprotein, P.

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37

Yamamoto, Etsushi, Satoshi Yamaguchi y Teruyuki Nagamune. "Protein Refolding by N-Alkylpyridinium and N-Alkyl-N-methylpyrrolidinium Ionic Liquids". Applied Biochemistry and Biotechnology 164, n.º 6 (8 de febrero de 2011): 957–67. http://dx.doi.org/10.1007/s12010-011-9187-1.

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38

Rezwan, Mandana y Daniel Auerbach. "Yeast “N”-hybrid systems for protein–protein and drug–protein interaction discovery". Methods 57, n.º 4 (agosto de 2012): 423–29. http://dx.doi.org/10.1016/j.ymeth.2012.06.006.

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39

Haque, Absarul y Mohammad A. Mir. "Interaction of Hantavirus Nucleocapsid Protein with Ribosomal Protein S19". Journal of Virology 84, n.º 23 (15 de septiembre de 2010): 12450–53. http://dx.doi.org/10.1128/jvi.01388-10.

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ABSTRACT Hantaviruses, members of the Bunyaviridae family, are emerging category A pathogens that initiate the translation of their capped mRNAs by a novel mechanism mediated by viral nucleocapsid protein (N). N specifically binds to the mRNA 5′ m7G cap and 40S ribosomal subunit, a complex of 18S rRNA and multiple ribosomal proteins. Here, we show that N specifically interacts with the ribosomal protein S19 (RPS19), located at the head region of the 40S subunit. We suggest that this N-RPS19 interaction facilitates ribosome loading on capped mRNAs during N-mediated translation initiation.

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40

elMasry, Nadia F. y Alan R. Fersht. "Mutational analysis of the N-capping box of the α-helix of chymotrypsin inhibitor 2". "Protein Engineering, Design and Selection" 7, n.º 6 (1994): 777–82. http://dx.doi.org/10.1093/protein/7.6.777.

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41

Rodenburg, Kees W., Emma Scheeren-Groot, Gert Vriend y Paul JJ Hooykaas. "The N-terminal domain of VirG of Agrobacterium tumefadens: modelling and analysis of mutant phenotypes". "Protein Engineering, Design and Selection" 7, n.º 7 (1994): 905–9. http://dx.doi.org/10.1093/protein/7.7.905.

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42

Clark, S. E., E. H. Muslin y C. A. Henson. "Effect of adding and removing N-glycosylation recognition sites on the thermostability of barley -glucosidase". Protein Engineering Design and Selection 17, n.º 3 (27 de febrero de 2004): 245–49. http://dx.doi.org/10.1093/protein/gzh028.

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43

Barrientos, Laura G., Elena Matei, Fátima Lasala, Rafael Delgado y Angela M. Gronenborn. "Dissecting carbohydrate–Cyanovirin-N binding by structure-guided mutagenesis: functional implications for viral entry inhibition". Protein Engineering, Design and Selection 19, n.º 12 (29 de septiembre de 2006): 525–35. http://dx.doi.org/10.1093/protein/gzl040.

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44

Arima, J., Y. Uesugi, M. Iwabuchi y T. Hatanaka. "Streptomyces aminopeptidase P: biochemical characterization and insight into the roles of its N-terminal domain". Protein Engineering Design and Selection 21, n.º 1 (19 de diciembre de 2007): 45–53. http://dx.doi.org/10.1093/protein/gzm068.

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45

Foophow, T., S. Tanaka, Y. Koga, K. Takano y S. Kanaya. "Subtilisin-like serine protease from hyperthermophilic archaeon Thermococcus kodakaraensis with N- and C-terminal propeptides". Protein Engineering Design and Selection 23, n.º 5 (25 de enero de 2010): 347–55. http://dx.doi.org/10.1093/protein/gzp092.

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46

Imberty, A., V. Piller, F. Piller y C. Breton. "Fold recognition and molecular modeling of a lectin-like domain in UDP- GalNac:polypeptide N-acetylgalactosaminyltransferases". Protein Engineering Design and Selection 10, n.º 12 (1 de diciembre de 1997): 1353–56. http://dx.doi.org/10.1093/protein/10.12.1353.

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47

Begley, Thomas J. y Richard P. Cunningham. "Methanobacterium thermoformicicum thymine DNA mismatch glycosylase: conversion of an N-glycosylase to an AP lyase". Protein Engineering, Design and Selection 12, n.º 4 (abril de 1999): 333–40. http://dx.doi.org/10.1093/protein/12.4.333.

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Raha, T., E. Samal, A. Majumdar, S. Basak, D. Chattopadhyay y D. J. Chattopadhyay. "N-terminal region of P protein of Chandipura virus is responsible for phosphorylation-mediated homodimerization". Protein Engineering, Design and Selection 13, n.º 6 (junio de 2000): 437–44. http://dx.doi.org/10.1093/protein/13.6.437.

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Tanaka, Takuji y Rickey Y. Yada. "N-terminal portion acts as an initiator of the inactivation of pepsin at neutral pH". Protein Engineering, Design and Selection 14, n.º 9 (septiembre de 2001): 669–74. http://dx.doi.org/10.1093/protein/14.9.669.

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Shinkai, Akeo, Mayumi Komuta-Kunitomo, Naoko Sato-Nakamura y Hideharu Anazawa. "N-terminal domain of eotaxin-3 is important for activation of CC chemokine receptor 3". Protein Engineering, Design and Selection 15, n.º 11 (noviembre de 2002): 923–29. http://dx.doi.org/10.1093/protein/15.11.923.

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