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Journal articles on the topic 'Protesi mammaria'

Author: Grafiati

Published: 4 June 2021

Last updated: 18 February 2022

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1

Schimmele, Bernhard, Nico Gräfe, and Andreas Plückthun. "Ribosome display of mammalian receptor domains." Protein Engineering, Design and Selection 18, no. 6 (2005): 285–94. http://dx.doi.org/10.1093/protein/gzi030.

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2

Li, E., A. Pedraza, M. Bestagno, S. Mancardi, R. Sanchez, and O. Burrone. "Mammalian cell expression of dimeric small immune proteins (SIP)." Protein Engineering Design and Selection 10, no. 6 (1997): 731–36. http://dx.doi.org/10.1093/protein/10.6.731.

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3

Shulga-Morskoy, S., and B. E. Rich. "Bioactive IL7-diphtheria fusion toxin secreted by mammalian cells." Protein Engineering Design and Selection 18, no. 1 (2005): 25–31. http://dx.doi.org/10.1093/protein/gzi007.

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4

Corish, Pete, and Chris Tyler-Smith. "Attenuation of green fluorescent protein half-life in mammalian cells." Protein Engineering, Design and Selection 12, no. 12 (1999): 1035–40. http://dx.doi.org/10.1093/protein/12.12.1035.

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5

Guglielmi, Laurence, Vincent Denis, Nadia Vezzio-Vié, et al. "Selection for intrabody solubility in mammalian cells using GFP fusions." Protein Engineering, Design and Selection 24, no. 12 (2011): 873–81. http://dx.doi.org/10.1093/protein/gzr049.

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6

Majors, B. S., G. G. Chiang, N. E. Pederson, and M. J. Betenbaugh. "Directed evolution of mammalian anti-apoptosis proteins by somatic hypermutation." Protein Engineering Design and Selection 25, no. 1 (2011): 27–38. http://dx.doi.org/10.1093/protein/gzr052.

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7

Launay, G., S. Teletchea, F. Wade, E. Pajot-Augy, J. F. Gibrat, and G. Sanz. "Automatic modeling of mammalian olfactory receptors and docking of odorants." Protein Engineering Design and Selection 25, no. 8 (2012): 377–86. http://dx.doi.org/10.1093/protein/gzs037.

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8

Lorenzo, Consuelo, Jorge E. Bolaños-Citalán, and Oscar G. Retana-Guiascón. "Rediscovery of Heteromys nelsoni in its type locality after over a century." Mammalia 84, no. 1 (2019): 6–9. http://dx.doi.org/10.1515/mammalia-2018-0154.

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Abstract We rediscovered a population of Nelson’s spiny pocket mouse (Heteromys nelsoni; Merriam, 1902) in the type locality of Pinabeto in the Mexican state of Chiapas, 121 years after it was last collected. We describe five topotype specimens according to their morphology and external measurements, and we confirm its identity at the species level in the Basic Local Alignment Search Tool (BLAST) of GenBank. As the population of H. nelsoni in Pinabeto is isolated, it is likely to be susceptible to extinction. There is a need to carry out additional scientific studies of this microendemic speci

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9

Martinez, Marcio A., Manfredo Alejandro Turcios-Casco, and Shasling Pacheco Amador. "On the conservation of Myrmecophaga tridactyla (Pilosa: Myrmecophagidae) in the core of Río Plátano Biosphere Reserve, Honduras." Mammalia 84, no. 6 (2020): 581–85. http://dx.doi.org/10.1515/mammalia-2019-0152.

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AbstractThe Río Plátano Biosphere Reserve (RPBR) represents the most important region in Honduras for conservation of the biodiversity of the country. From May 2017 to January 2019, we installed 24 camera traps in the RPBR to monitor big mammals, including Myrmecophaga tridactyla. In 1512 camera-trapping hours, the giant anteater was recorded in two photos. The photos presented herein of M. tridactyla are the first records of the species in the core of the RPBR. The protection of a vulnerable species such as M. tridactyla in the RPBR could also help to protect other species (Pecari tajacu, Tay

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10

Kvam, Erik, Michael R. Sierks, Charles B. Shoemaker, and Anne Messer. "Physico-chemical determinants of soluble intrabody expression in mammalian cell cytoplasm." Protein Engineering, Design and Selection 23, no. 6 (2010): 489–98. http://dx.doi.org/10.1093/protein/gzq022.

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11

Baltz, Jay M., P. Oneeka Williams, and Richard A. Cone. "Dense Fibers Protect Mammalian Sperm Against Damage1." Biology of Reproduction 43, no. 3 (1990): 485–91. http://dx.doi.org/10.1095/biolreprod43.3.485.

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12

Cols, Neus, Núria Romero-Isart, Roger Bofill та ін. "In vivo copper- and cadmium-binding ability of mammalian metallothionein β domain". Protein Engineering, Design and Selection 12, № 3 (1999): 265–69. http://dx.doi.org/10.1093/protein/12.3.265.

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13

Paborsky, Lisa R., Brain M. Fendly, Karen L. Fisher, et al. "Mammalian cell transient expression of tissue factor for the production of antigen." "Protein Engineering, Design and Selection" 3, no. 6 (1990): 547–53. http://dx.doi.org/10.1093/protein/3.6.547.

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14

Kuhnel, B., J. Alcantara, J. Boothe, G. van Rooijen, and M. Moloney. "Precise and efficient cleavage of recombinant fusion proteins using mammalian aspartic proteases." Protein Engineering Design and Selection 16, no. 10 (2003): 777–83. http://dx.doi.org/10.1093/protein/gzg091.

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15

Cho, Yong Ku, and Eric V. Shusta. "Antibody library screens using detergent-solubilized mammalian cell lysates as antigen sources." Protein Engineering, Design and Selection 23, no. 7 (2010): 567–77. http://dx.doi.org/10.1093/protein/gzq029.

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16

León-Tapia, M. Ángel, and Fernando A. Cervantes. "Noteworthy records and ecological niche modeling of the rare and endangered Goldman’s diminutive woodrat Nelsonia goldmani (Rodentia: Cricetidae) endemic to central Mexican highlands." Mammalia 83, no. 4 (2019): 330–42. http://dx.doi.org/10.1515/mammalia-2018-0023.

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Abstract Nelsonia goldmani is an uncommon rodent, endemic to highland microhabitats in central Mexico. Few individuals have been reported in scarce localities after being discovered in 1903 resulting in a lack of knowledge about its geographic distribution and actual presence in its habitat; such situation makes this species of national interest priority for conservation. Therefore, the aim of this study was to summarize collecting records, confirm the presence of this species in the field and estimate its ecological niche. We searched specimens in biological collections, carried out an ecolog

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17

Lo, K. M., Y. Sudo, J. Chen, et al. "High level expression and secretion of Fc-X fusion proteins in mammalian cells." Protein Engineering Design and Selection 11, no. 6 (1998): 495–500. http://dx.doi.org/10.1093/protein/11.6.495.

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18

Albarran, Brian, Richard To, and Patrick S. Stayton. "A TAT–streptavidin fusion protein directs uptake of biotinylated cargo into mammalian cells." Protein Engineering, Design and Selection 18, no. 3 (2005): 147–52. http://dx.doi.org/10.1093/protein/gzi014.

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19

Hötzel, Isidro, Vicki Chiang, Jingyu Diao, Homer Pantua, Henry R. Maun, and Sharookh B. Kapadia. "Efficient production of antibodies against a mammalian integral membrane protein by phage display." Protein Engineering, Design and Selection 24, no. 9 (2011): 679–89. http://dx.doi.org/10.1093/protein/gzr039.

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20

O’Rourke, Sara M., Giora I. Morozov, Jacob T. Roberts, Adam W. Barb, and Nikolaos G. Sgourakis. "Production of soluble pMHC-I molecules in mammalian cells using the molecular chaperone TAPBPR." Protein Engineering, Design and Selection 32, no. 12 (2019): 525–32. http://dx.doi.org/10.1093/protein/gzaa015.

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Abstract Current approaches for generating major histocompatibility complex (MHC) Class-I proteins with desired bound peptides (pMHC-I) for research, diagnostic and therapeutic applications are limited by the inherent instability of empty MHC-I molecules. Using the properties of the chaperone TAP-binding protein related (TAPBPR), we have developed a robust method to produce soluble, peptide-receptive MHC-I molecules in Chinese Hamster Ovary cells at high yield, completely bypassing the requirement for laborious refolding from inclusion bodies expressed in E.coli. Purified MHC-I/TAPBPR complexe

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21

Kikuchi, Hiroto, Hiroshi Fujisaki, Tadaomi Furuta, Ken Okamoto, and Takeshi Nishino. "3P047 Mutation studies on the mammalian and the baterial XORs with inhibitors(01A. Protein: Structure,Poster)." Seibutsu Butsuri 53, supplement1-2 (2013): S219. http://dx.doi.org/10.2142/biophys.53.s219_5.

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22

Romero, Francisco, Ana M. Gil-Bernabé, Carmen Sáez, Miguel A. Japón, José A. Pintor-Toro, and María Tortolero. "Securin Is a Target of the UV Response Pathway in Mammalian Cells." Molecular and Cellular Biology 24, no. 7 (2004): 2720–33. http://dx.doi.org/10.1128/mcb.24.7.2720-2733.2004.

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ABSTRACT All eukaryotic cells possess elaborate mechanisms to protect genome integrity and ensure survival after DNA damage, ceasing proliferation and granting time for DNA repair. Securin is an inhibitory protein that is bound to a protease called Separase to inhibit sister chromatid separation until the onset of anaphase. At the metaphase-to-anaphase transition, Securin is degraded by the anaphase-promoting complex or cyclosome, and Separase contributes to the release of cohesins from the chromosome, allowing for the segregation of sister chromatids to opposite spindle poles. Here we provide

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23

Hamann, C. S., S. Lentainge, L. S. Li, J. S. Salem, F. D. Yang, and B. S. Cooperman. "Chimeric small subunit inhibitors of mammalian ribonucleotide reductase: a dual function for the R2 C-terminus?" Protein Engineering Design and Selection 11, no. 3 (1998): 219–24. http://dx.doi.org/10.1093/protein/11.3.219.

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24

Sangrar, W., S. M. Marcovina, and M. L. Koschinsky. "Expression and characterization of apolipoprotein(a) kringle IV types 1, 2 and 10 in mammalian cells." "Protein Engineering, Design and Selection" 7, no. 5 (1994): 723–31. http://dx.doi.org/10.1093/protein/7.5.723.

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25

Young, Robert J., Raymond J. Owens, Graham A. Mackay, et al. "Secretion of recombinant human IgE-Fc by mammalian cells and biological activity of glycosylation site mutants." "Protein Engineering, Design and Selection" 8, no. 2 (1995): 193–99. http://dx.doi.org/10.1093/protein/8.2.193.

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26

Chen, C. P., Y. T. Hsieh, Z. M. Prijovich, et al. "ECSTASY, an adjustable membrane-tethered/soluble protein expression system for the directed evolution of mammalian proteins." Protein Engineering Design and Selection 25, no. 7 (2012): 367–75. http://dx.doi.org/10.1093/protein/gzs033.

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27

Tesar, D., and I. Hotzel. "A dual host vector for Fab phage display and expression of native IgG in mammalian cells." Protein Engineering Design and Selection 26, no. 10 (2013): 655–62. http://dx.doi.org/10.1093/protein/gzt050.

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28

McClellan, Holly L., Susan J. Miller, and Peter E. Hartmann. "Evolution of lactation: nutritionv.protection with special reference to five mammalian species." Nutrition Research Reviews 21, no. 2 (2008): 97–116. http://dx.doi.org/10.1017/s0954422408100749.

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The evolutionary origin of the mammary gland has been difficult to establish because little knowledge can be gained on the origin of soft tissue organs from fossil evidence. One approach to resolve the origin of lactation has compared the anatomy of existing primitive mammals to skin glands, whilst another has examined the metabolic and molecular synergy between mammary gland development and the innate immune system. We have reviewed the physiology of lactation in five mammalian species with special reference to these theories. In all species, milk fulfils dual functions of providing protectio

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29

Schedin, P., R. Strange, T. Mitrenga, P. Wolfe, and M. Kaeck. "Fibronectin fragments induce MMP activity in mouse mammary epithelial cells: evidence for a role in mammary tissue remodeling." Journal of Cell Science 113, no. 5 (2000): 795–806. http://dx.doi.org/10.1242/jcs.113.5.795.

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Mammary gland form and function are regulated by interactions between epithelium and extracellular matrix. Major glycoprotein components of extracellular matrix have been identified that give survival, proliferation and differentiation signals to mammary epithelial cells. We provide evidence that proteolytic fragments of the extracellular matrix glycoprotein, fibronectin, suppress growth and can promote apoptosis of mouse mammary epithelial cells. During mammary gland involution, total fibronectin and fibronectin fragment levels are increased. The peak levels of fibronectin protein and fragmen

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30

Blanche, Carlos, and Alberto Santibanez-Gallerani. "Technique to protect the internal mammary artery pedicle." Annals of Thoracic Surgery 60, no. 6 (1995): 1824–25. http://dx.doi.org/10.1016/0003-4975(95)00661-3.

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31

Chang, Chia-Ching, and P. C. Huang. "Semi-empirical simulation of Zn/Cd binding site preference in the metal binding domains of mammalian metallothionein." "Protein Engineering, Design and Selection" 9, no. 12 (1996): 1165–72. http://dx.doi.org/10.1093/protein/9.12.1165.

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32

Kumar, S., L. Sun, H. Liu, B. K. Muralidhara, and J. R. Halpert. "Engineering mammalian cytochrome P450 2B1 by directed evolution for enhanced catalytic tolerance to temperature and dimethyl sulfoxide." Protein Engineering Design and Selection 19, no. 12 (2006): 547–54. http://dx.doi.org/10.1093/protein/gzl042.

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33

de Lamirande, E., and C. Gagnon. "Effects of protease inhibitors and substrates on motility of mammalian spermatozoa." Journal of Cell Biology 102, no. 4 (1986): 1378–83. http://dx.doi.org/10.1083/jcb.102.4.1378.

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A series of protease inhibitors were tested on the motility of human, rat, bull, and rabbit demembranated reactivated spermatozoa. Some inhibitors, including aprotinin, boc-gln-leu-lys-H, and D-phe-pro-arg-H, could inhibit motility as well as prevent initiation of motility. In general, with the exception of aprotinin, protease inhibitors were more potent in preventing the initiation of movement than in blocking motility of demembranated spermatozoa. Protease substrates could also block sperm motility. Of the substrates tested only those with arg or lys ester bonds were active. The inhibition o

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34

BERGER, JOEL, and STEVEN L. CAIN. "Moving Beyond Science to Protect a Mammalian Migration Corridor." Conservation Biology 28, no. 5 (2014): 1142–50. http://dx.doi.org/10.1111/cobi.12327.

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35

Adrain, Colin, Kvido Strisovsky, Markus Zettl, Landian Hu, Marius K. Lemberg, and Matthew Freeman. "Mammalian EGF receptor activation by the rhomboid protease RHBDL2." EMBO reports 12, no. 5 (2011): 421–27. http://dx.doi.org/10.1038/embor.2011.50.

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36

Bragg, Jack T., Hannah K. D'Ambrosio, Timothy J. Smith, et al. "Esterified Trehalose Analogues Protect Mammalian Cells from Heat Shock." ChemBioChem 18, no. 18 (2017): 1863–70. http://dx.doi.org/10.1002/cbic.201700302.

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37

Lunde, Ngoc Nguyen, Tatjana Bosnjak, Rigmor Solberg, and Harald Thidemann Johansen. "Mammalian legumain – A lysosomal cysteine protease with extracellular functions?" Biochimie 166 (November 2019): 77–83. http://dx.doi.org/10.1016/j.biochi.2019.06.002.

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38

Bukowska, D., B. Kempisty, H. Piotrowska, et al. " The structure and role of mammalian sperm RNA: a review." Veterinární Medicína 58, No. 2 (2013): 57–64. http://dx.doi.org/10.17221/6696-vetmed.

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The main role of sperm is the delivery of the paternal genome into the oocyte during fertilisation. However, several lines of evidence have indicated that mammalian spermatozoa contribute more than just their DNA, namely, they also deliver a large range of RNA molecules. Microarray analysis has revealed a complex population of 3000 different kinds of messenger RNA that are delivered to oocytes by sperm and ejaculated spermatozoa are estimated to contain about 0.015 pg of total RNA. Some of the transcripts encode proteins crucial for early embryo development. Messenger RNAs from sperm also help

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39

McMullen, T. W. P., J. Li, P. J. Sheffield, et al. "The functional implications of the dimerization of the catalytic subunits of the mammalian brain platelet-activating factor acetylhydrolase (Ib)." Protein Engineering, Design and Selection 13, no. 12 (2000): 865–71. http://dx.doi.org/10.1093/protein/13.12.865.

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40

Zuberbuhler, K., A. Palumbo, C. Bacci, et al. "A general method for the selection of high-level scFv and IgG antibody expression by stably transfected mammalian cells." Protein Engineering Design and Selection 22, no. 3 (2008): 169–74. http://dx.doi.org/10.1093/protein/gzn068.

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41

Sabariegos, Rosario, Fernando Picazo, Beatriz Domingo, Sandra Franco, Miguel-Angel Martinez, and Juan Llopis. "Fluorescence Resonance Energy Transfer-Based Assay for Characterization of Hepatitis C Virus NS3-4A Protease Activity in Live Cells." Antimicrobial Agents and Chemotherapy 53, no. 2 (2008): 728–34. http://dx.doi.org/10.1128/aac.01029-08.

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ABSTRACT The NS3/4A protease from hepatitis C virus (HCV) plays a key role in viral replication. We report a system for monitoring the activity of this enzyme in single living mammalian cells. We constructed a fluorescence resonance energy transfer (FRET) probe that consists of an enhanced cyan fluorescent protein-citrine fusion, with a cleavage site for HCV NS3/4A protease embedded within the linker between them. Expression of the biosensor in mammalian cells resulted in a FRET signal, and cotransfection with the NS3/4A expression vector produced a significant reduction in FRET, indicating th

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42

Hasan, Md Kamrul, Samir El Qaidi, and Philip R. Hardwidge. "The T3SS Effector Protease NleC Is Active within Citrobacter rodentium." Pathogens 10, no. 5 (2021): 589. http://dx.doi.org/10.3390/pathogens10050589.

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Whether type III secretion system (T3SS) effector proteins encoded by Gram-negative bacterial pathogens have intra-bacterial activities is an important and emerging area of investigation. Gram-negative bacteria interact with their mammalian hosts by using secretion systems to inject virulence proteins directly into infected host cells. Many of these injected protein effectors are enzymes that modify the structure and inhibit the function of mammalian proteins. The underlying dogma is that T3SS effectors are inactive until they are injected into host cells, where they then fold into their activ

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43

Luo, Jie, Wei Lv, Ying Deng, and Yuyu Sun. "Cellulose–Ethylenediaminetetraacetic Acid Conjugates Protect Mammalian Cells from Bacterial Cells." Biomacromolecules 14, no. 4 (2013): 1054–62. http://dx.doi.org/10.1021/bm301922z.

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44

Otto, James C., Edward Kim, Stephen G. Young, and Patrick J. Casey. "Cloning and Characterization of a Mammalian Prenyl Protein-specific Protease." Journal of Biological Chemistry 274, no. 13 (1999): 8379–82. http://dx.doi.org/10.1074/jbc.274.13.8379.

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45

SHIMOMURA, Takeshi, and Kazuhiro NAGAIKE. "Cultured mammalian cells for production of bioactive macromolecules. Protease inhibitor." Journal of the agricultural chemical society of Japan 63, no. 2 (1989): 192–95. http://dx.doi.org/10.1271/nogeikagaku1924.63.192.

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46

Eguchi, Masaharu. "Protein protease inhibitors in insects and comparison with mammalian inhibitors." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 105, no. 3-4 (1993): 449–56. http://dx.doi.org/10.1016/0305-0491(93)90073-e.

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47

Shang, Yonglei, Devin Tesar, and Isidro Hötzel. "Modular protein expression by RNAtrans-splicing enables flexible expression of antibody formats in mammalian cells from a dual-host phage display vector." Protein Engineering Design and Selection 28, no. 10 (2015): 437–44. http://dx.doi.org/10.1093/protein/gzv018.

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48

Puente, X. S., L. M. Sánchez, A. Gutiérrez-Fernández, G. Velasco, and C. López-Otín. "A genomic view of the complexity of mammalian proteolytic systems." Biochemical Society Transactions 33, no. 2 (2005): 331–34. http://dx.doi.org/10.1042/bst0330331.

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Proteolytic enzymes play an essential role in different physiological processes, including development, reproduction and host defence, as well as in numerous pathologies, like inflammatory diseases, neurological disorders or cancer. The completion of the human genome sequence allowed us to determine that more than 2% of all human genes are proteases or protease inhibitors, reflecting the importance of proteolysis in human biology. To understand better the complexity of proteases in human and other model organisms, we have used the available genome sequences of different mammalian organisms, in

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49

Jain, Abhinav R., Zachary T. Britton, Chester E. Markwalter, and Anne S. Robinson. "Improved ligand-binding- and signaling-competent human NK2R yields in yeast using a chimera with the rat NK2R C-terminus enable NK2R-G protein signaling platform." Protein Engineering, Design and Selection 32, no. 10 (2019): 459–69. http://dx.doi.org/10.1093/protein/gzaa009.

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Abstract The tachykinin 2 receptor (NK2R) plays critical roles in gastrointestinal, respiratory and mental disorders and is a well-recognized target for therapeutic intervention. To date, therapeutics targeting NK2R have failed to meet regulatory agency approval due in large part to the limited characterization of the receptor-ligand interaction and downstream signaling. Herein, we report a protein engineering strategy to improve ligand-binding- and signaling-competent human NK2R that enables a yeast-based NK2R signaling platform by creating chimeras utilizing sequences from rat NK2R. We demon

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50

Narhi, Linda O., Tsutomu Arakawa, Kenneth Aoki, et al. "Asn to Lys mutations at three sites which are N-glycosylated in the mammalian protein decrease the aggregation of Escherichia coli-derived erythropoietin." Protein Engineering, Design and Selection 14, no. 2 (2001): 135–40. http://dx.doi.org/10.1093/protein/14.2.135.

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