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Journal articles on the topic 'Protein 1'

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Published: 4 June 2021
Last updated: 20 February 2023

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1

Brown, Andrew, Gordon Stock, Alpesh A. Patel, Chukwuka Okafor, and Alexander Vaccaro. "Osteogenic Protein-1." BioDrugs 20, no. 4 (2006): 243–51. http://dx.doi.org/10.2165/00063030-200620040-00005.

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2

Cook, Stephen D., and David C. Rueger. "Osteogenic Protein-1." Clinical Orthopaedics and Related Research 324 (March 1996): 29–38. http://dx.doi.org/10.1097/00003086-199603000-00005.

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3

Murali, C., and E. H. Creaser. "Protein engineering of alcohol dehydrogenase — 1. Effects of two amino acid changes in the active site of yeast ADH-1." "Protein Engineering, Design and Selection" 1, no. 1 (1986): 55–57. http://dx.doi.org/10.1093/protein/1.1.55.

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4

Hartigan, Nichola, Laure Garrigue-Antar, and Karl E. Kadler. "Bone Morphogenetic Protein-1 (BMP-1)." Journal of Biological Chemistry 278, no. 20 (March 13, 2003): 18045–49. http://dx.doi.org/10.1074/jbc.m211448200.

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5

Ammosova, Tatyana, Marina Jerebtsova, Monique Beullens, Bart Lesage, Angela Jackson, Fatah Kashanchi, William Southerland, Victor R. Gordeuk, Mathieu Bollen, and Sergei Nekhai. "Nuclear Targeting of Protein Phosphatase-1 by HIV-1 Tat Protein." Journal of Biological Chemistry 280, no. 43 (August 29, 2005): 36364–71. http://dx.doi.org/10.1074/jbc.m503673200.

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Transcription of human immunodeficiency virus (HIV)-1 genes is activated by HIV-1 Tat protein, which induces phosphorylation of the C-terminal domain of RNA polymerase-II by CDK9/cyclin T1. We previously showed that Tat-induced HIV-1 transcription is regulated by protein phosphatase-1 (PP1). In the present study we demonstrate that Tat interacts with PP1 and that disruption of this interaction prevents induction of HIV-1 transcription. We show that PP1 interacts with Tat in part through the binding of Val36 and Phe38 of Tat to PP1 and that Tat is involved in the nuclear and subnuclear targeting of PP1. The PP1 binding mutant Tat-V36A/F38A displayed a decreased affinity for PP1 and was a poor activator of HIV-1 transcription. Surprisingly, Tat-Q35R mutant that had a higher affinity for PP1 was also a poor activator of HIV-1 transcription, because strong PP1 binding competed out binding of Tat to CDK9/cyclin T1. Our results suggest that Tat might function as a nuclear regulator of PP1 and that interaction of Tat with PP1 is critical for activation of HIV-1 transcription by Tat.
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6

Miklossy, G., J. Tozser, J. Kadas, R. Ishima, J. M. Louis, and P. Bagossi. "Novel macromolecular inhibitors of human immunodeficiency virus-1 protease." Protein Engineering Design and Selection 21, no. 7 (May 2, 2008): 453–61. http://dx.doi.org/10.1093/protein/gzn022.

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7

Garcia, Alphonse, Xavier Cayla, Bernard Caudron, Éric Deveaud, Fernando Roncal, and Angelita Rebollo. "New insights in protein phosphorylation: a signature for protein phosphatase 1 interacting proteins." Comptes Rendus Biologies 327, no. 2 (February 2004): 93–97. http://dx.doi.org/10.1016/j.crvi.2004.01.001.

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8

Popețiu, Romana Olivia, Silviu Daniel Moldovan, Simona Maria Borta, Oana Lucia Amza, and Maria Puşchiță. "Interrelation between chitinase-3-like protein 1 (CHI3L1) – YKL-40, C-reactive protein and spirometry in chronic lung disease." Romanian Journal of Medical Practice 14, no. 4 (December 31, 2019): 393–95. http://dx.doi.org/10.37897/rjmp.2019.4.9.

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9

Sansom, Clare E., Jin Wu, and Irene T. Weber. "Molecular mechanics analysis of inhibitor binding to HIV-1 protease." "Protein Engineering, Design and Selection" 5, no. 7 (1992): 659–67. http://dx.doi.org/10.1093/protein/5.7.659.

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10

Fogolari, F., G. Esposito, P. Viglino, G. Damante, and A. Pastore. "Homology model building of the thyroid transcription factor 1 homeodomain." "Protein Engineering, Design and Selection" 6, no. 5 (1993): 513–19. http://dx.doi.org/10.1093/protein/6.5.513.

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11

Swindells, Mark B., and Janet M. Thornton. "A study of structural determinants in the interleukin-1 fold." "Protein Engineering, Design and Selection" 6, no. 7 (1993): 711–15. http://dx.doi.org/10.1093/protein/6.7.711.

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12

Oldfield, Thomas J., Peter Murray-Rust, and Roderick E. Hubbard. "Model structures and action of interleukin 1 and its antagonist." "Protein Engineering, Design and Selection" 6, no. 8 (1993): 865–71. http://dx.doi.org/10.1093/protein/6.8.865.

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13

Harrison, Robert W., and Irene T. Weber. "Molecular dynamics simulations of HIV-1 protease with peptide substrate." "Protein Engineering, Design and Selection" 7, no. 11 (1994): 1353–63. http://dx.doi.org/10.1093/protein/7.11.1353.

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14

Zakrzewska, M., D. Krowarsch, A. Wiedlocha, and J. Otlewski. "Design of fully active FGF-1 variants with increased stability." Protein Engineering Design and Selection 17, no. 8 (September 23, 2004): 603–11. http://dx.doi.org/10.1093/protein/gzh076.

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15

Wang, Guozheng, Alicia Ma, Cheok-man Chow, David Horsley, Nicholas R. Brown, Ian G. Cowell, and Prim B. Singh. "Conservation of Heterochromatin Protein 1 Function." Molecular and Cellular Biology 20, no. 18 (September 15, 2000): 6970–83. http://dx.doi.org/10.1128/mcb.20.18.6970-6983.2000.

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ABSTRACT Heterochromatin represents a cytologically visible state of heritable gene repression. In the yeast, Schizosaccharomyces pombe, the swi6 gene encodes a heterochromatin protein 1 (HP1)-like chromodomain protein that localizes to heterochromatin domains, including the centromeres, telomeres, and the donor mating-type loci, and is involved in silencing at these loci. We identify here the functional domains of swi6p and demonstrate that the chromodomain from a mammalian HP1-like protein, M31, can functionally replace that of swi6p, showing that chromodomain function is conserved from yeasts to humans. Site-directed mutagenesis, based on a modeled three-dimensional structure of the swi6p chromodomain, shows that the hydrophobic amino acids which lie in the core of the structure are critical for biological function. Gel filtration, gel overlay experiments, and mass spectroscopy show that HP1 proteins can self-associate, and we suggest that it is as oligomers that HP1 proteins are incorporated into heterochromatin complexes that silence gene activity.
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16

Sear, Richard P. "Specific protein–protein binding in many-component mixtures of proteins." Physical Biology 1, no. 2 (April 29, 2004): 53–60. http://dx.doi.org/10.1088/1478-3967/1/2/001.

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17

Zhuo, Jia L. "Monocyte chemoattractant protein-1." Journal of Hypertension 22, no. 3 (March 2004): 451–54. http://dx.doi.org/10.1097/00004872-200403000-00003.

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18

Hu, Xiaoyi, Kristin Kohler, Arnold M. Falick, Anne M. F. Moore, Patrick R. Jones, O. David Sparkman, and Craig Vierra. "Egg Case Protein-1." Journal of Biological Chemistry 280, no. 22 (March 29, 2005): 21220–30. http://dx.doi.org/10.1074/jbc.m412316200.

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19

Stoffers, Doris A., Melissa K. Thomas, and Joel F. Habener. "Homeodomain Protein IDX-1." Trends in Endocrinology & Metabolism 8, no. 4 (May 1997): 145–51. http://dx.doi.org/10.1016/s1043-2760(97)00008-8.

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20

Menten, Patricia, Anja Wuyts, and Jo Van Damme. "Macrophage inflammatory protein-1." Cytokine & Growth Factor Reviews 13, no. 6 (December 2002): 455–81. http://dx.doi.org/10.1016/s1359-6101(02)00045-x.

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21

Maurer, M., and E. von Stebut. "Macrophage inflammatory protein-1." International Journal of Biochemistry & Cell Biology 36, no. 10 (October 2004): 1882–86. http://dx.doi.org/10.1016/j.biocel.2003.10.019.

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22

Spel, Lotte, Joppe Nieuwenhuis, Rianne Haarsma, Elmer Stickel, Onno B. Bleijerveld, Maarten Altelaar, Jaap Jan Boelens, Thijn R. Brummelkamp, Stefan Nierkens, and Marianne Boes. "Nedd4-Binding Protein 1 and TNFAIP3-Interacting Protein 1 Control MHC-1 Display in Neuroblastoma." Cancer Research 78, no. 23 (September 13, 2018): 6621–31. http://dx.doi.org/10.1158/0008-5472.can-18-0545.

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23

Dennis, S., M. Aikawa, W. Szeto, P. A. d'Amore, and J. Papkoff. "A secreted frizzled related protein, FrzA, selectively associates with Wnt-1 protein and regulates wnt-1 signaling." Journal of Cell Science 112, no. 21 (November 1, 1999): 3815–20. http://dx.doi.org/10.1242/jcs.112.21.3815.

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The Wnt gene family encodes proteins that serve key roles in differentiation and development. Wnt proteins interact with seven transmembrane receptors of the Frizzled family and activate a signaling pathway leading to the nucleus. A primary biochemical effect of Wnt-1 signaling is the stabilization of cytoplasmic (beta)-catenin which, in association with transcription factors of the Lef/tcf family, regulates gene expression. The recent identification of a new class of secreted proteins with similarity to the extracellular, ligand-binding domain of Frizzled proteins, soluble Frizzled related proteins (sFRP), suggested that additional mechanisms could regulate Wnt signaling. Here we demonstrate that FrzA, a sFRP that is highly expressed in vascular endothelium and a variety of epithelium, specifically binds to Wnt-1 protein, but not Wnt-5a protein, and modulates Wnt-1 signaling. FrzA associated with Wnt-1 either when expressed in the same cell or when soluble FrzA was incubated with Wnt-1-expressing cells. FrzA efficiently inhibited the Wnt-1 mediated increase in cytoplasmic (beta)-catenin levels as well as the Wnt-1 induction of transcription from a Lef/tcf reporter gene. The effects of FrzA on (beta)-catenin levels could be demonstrated when co-expressed with Wnt-1 or when individual cells expressing FrzA and Wnt-1 were co-cultured. These data demonstrate the existence of a negative regulatory mechanism mediated by the selective binding of FrzA to Wnt-1 protein.
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24

Jang, Won Hee, and Dae-Hyun Seog. "Kinesin Superfamily-associated Protein 3 (KAP3) Mediates the Interaction between Kinesin-II Motor Subunits and HS-1-associated Protein X-1 (HAX-1) through Direct Binding." Journal of Life Science 23, no. 8 (August 30, 2013): 978–83. http://dx.doi.org/10.5352/jls.2013.23.8.978.

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25

Steiglitz, Barry M., Melvin Ayala, Karthikeyan Narayanan, Anne George, and Daniel S. Greenspan. "Bone Morphogenetic Protein-1/Tolloid-like Proteinases Process Dentin Matrix Protein-1." Journal of Biological Chemistry 279, no. 2 (October 24, 2003): 980–86. http://dx.doi.org/10.1074/jbc.m310179200.

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26

Helder, M. N., H. Karg, T. J. M. Bervoets, S. Vukicevic, E. H. Burger, R. N. D'Souza, J. H. M. Wöltgens, G. Karsenty, and A. L. J. J. Bronckers. "Bone Morphogenetic Protein-7 (Osteogenic Protein-1, OP-1) and Tooth Development." Journal of Dental Research 77, no. 4 (April 1998): 545–54. http://dx.doi.org/10.1177/00220345980770040701.

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27

Ye, Xiao-Xia, Hong Lu, Yao Yu, Ning Ding, Nai-Ling Zhang, Ke-Ke Huo, Da-Fang Wan, Yu-Yang Li, and Jian-Ren Gu. "pp5644 Interacts with phosphatidylinositol-4-phosphate adaptor protein-1 associated protein-1." Molecular and Cellular Biochemistry 271, no. 1-2 (March 2005): 151–58. http://dx.doi.org/10.1007/s11010-005-5907-6.

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28

ATUK KAHRAMAN, Tutku, and Zeynep CAFEROĞLU. "Protein and Fat Counting in Type 1 Diabetes." Turkiye Klinikleri Journal of Pediatrics 30, no. 1 (2021): 63–68. http://dx.doi.org/10.5336/pediatr.2020-78185.

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29

Peti, Wolfgang, Angus C. Nairn, and Rebecca Page. "Folding of Intrinsically Disordered Protein Phosphatase 1 Regulatory Proteins." Current Physical Chemistry 2, no. 1 (January 1, 2012): 107–14. http://dx.doi.org/10.2174/1877946811202010107.

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30

Peti, Wolfgang, Angus C. Nairn, and Rebecca Page. "Folding of Intrinsically Disordered Protein Phosphatase 1 Regulatory Proteins." Current Physical Chemistrye 2, no. 1 (January 1, 2012): 107–14. http://dx.doi.org/10.2174/1877947611202010107.

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31

Choy, Meng S., Rebecca Page, and Wolfgang Peti. "Regulation of protein phosphatase 1 by intrinsically disordered proteins." Biochemical Society Transactions 40, no. 5 (September 19, 2012): 969–74. http://dx.doi.org/10.1042/bst20120094.

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PP1 (protein phosphatase 1) is an essential serine/threonine phosphatase that plays a critical role in a broad range of biological processes, from muscle contraction to memory formation. PP1 achieves its biological specificity by forming holoenzymes with more than 200 known regulatory proteins. Interestingly, most of these regulatory proteins (≥70%) belong to the class of IDPs (intrinsically disordered proteins). Thus structural studies highlighting the interaction of these IDP regulatory proteins with PP1 are an attractive model system because it allows general parameters for a group of diverse IDPs that interact with the same binding partner to be identified, while also providing fundamental insights into PP1 biology. The present review provides a brief overview of our current understanding of IDP–PP1 interactions, including the importance of pre-formed secondary and tertiary structures for PP1 binding, as well as changes of IDP dynamics upon interacting with PP1.
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32

Korrodi-Gregório, Luís, Sara L. C. Esteves, and Margarida Fardilha. "Protein phosphatase 1 catalytic isoforms: specificity toward interacting proteins." Translational Research 164, no. 5 (November 2014): 366–91. http://dx.doi.org/10.1016/j.trsl.2014.07.001.

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33

Gustchina, Alia, Clare Sansom, Martine Prevost, Jean Richelle, Shoshana Y. Wodak, Alexander Wlodawer, and Irene T. Weber. "Energy calculations and analysis of HIV-1 protease-inhibitor crystal structures." "Protein Engineering, Design and Selection" 7, no. 3 (1994): 309–16. http://dx.doi.org/10.1093/protein/7.3.309.

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34

Milovnik, P., D. Ferrari, C. A. Sarkar, and A. Pluckthun. "Selection and characterization of DARPins specific for the neurotensin receptor 1." Protein Engineering Design and Selection 22, no. 6 (April 22, 2009): 357–66. http://dx.doi.org/10.1093/protein/gzp011.

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35

Jayaraman, Murali, Ravindra Kodali, and Ronald Wetzel. "The impact of ataxin-1-like histidine insertions on polyglutamine aggregation." Protein Engineering, Design and Selection 22, no. 8 (June 18, 2009): 469–78. http://dx.doi.org/10.1093/protein/gzp023.

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36

Mader, A., and R. Kunert. "Humanization strategies for an anti-idiotypic antibody mimicking HIV-1 gp41." Protein Engineering Design and Selection 23, no. 12 (October 30, 2010): 947–54. http://dx.doi.org/10.1093/protein/gzq092.

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37

Baldari, C., A. Massone, G. Macchia, and J. L. Telford. "Differential stability of human interleukin 1 beta fragments expressed in yeast." "Protein Engineering, Design and Selection" 1, no. 5 (1987): 433–37. http://dx.doi.org/10.1093/protein/1.5.433.

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38

Stewart, Richard J., Jose N. Varghese, Thomas P. J. Garrett, Peter B. Høj, and Geoffrey B. Fincher. "Mutant barley (1→3,1→4)-β-glucan endohydrolases with enhanced thermostability." Protein Engineering, Design and Selection 14, no. 4 (April 2001): 245–53. http://dx.doi.org/10.1093/protein/14.4.245.

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39

Osuna, Joel, Alejandra Pérez-Blancas, and Xavier Soberón. "Improving a circularly permuted TEM-1 β-lactamase by directed evolution." Protein Engineering, Design and Selection 15, no. 6 (June 2002): 463–70. http://dx.doi.org/10.1093/protein/15.6.463.

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40

Salminen, T. A., D. J. Smith, S. Jalkanen, and M. S. Johnson. "Structural model of the catalytic domain of an enzyme with cell adhesion activity: human vascular adhesion protein-1 (HVAP-1) D4 domain is an amine oxidase." Protein Engineering Design and Selection 11, no. 12 (December 1, 1998): 1195–204. http://dx.doi.org/10.1093/protein/11.12.1195.

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41

Helmer, S. D., P. J. Hansen, R. V. Anthony, W. W. Thatcher, F. W. Bazer, and R. M. Roberts. "Identification of bovine trophoblast protein-1, a secretory protein immunologically related to ovine trophoblast protein-1." Reproduction 79, no. 1 (January 1, 1987): 83–91. http://dx.doi.org/10.1530/jrf.0.0790083.

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42

Ritchie, Helena H., Colin T. Yee, Xu-na Tang, Zhihong Dong, and Robert S. Fuller. "DSP-PP Precursor Protein Cleavage by Tolloid-Related-1 Protein and by Bone Morphogenetic Protein-1." PLoS ONE 7, no. 7 (July 17, 2012): e41110. http://dx.doi.org/10.1371/journal.pone.0041110.

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43

KITAMURA, Yukari, Tadahiro KITAMURA, Hiroshi SAKAUE, Tetsuo MAEDA, Hikaru UENO, Shoko NISHIO, Shigeo OHNO, et al. "Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac." Biochemical Journal 322, no. 3 (March 15, 1997): 873–78. http://dx.doi.org/10.1042/bj3220873.

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Bacterially expressed glutathione S-transferase fusion proteins containing Rac1 were used to identify binding proteins of this Rho family GTPase present in a bovine brain extract. Five proteins of 85, 110, 125, 140 and 170 kDa were detected, all of which were associated exclusively with guanosine 5´-[γ-thio]triphosphate-bound Rac1, not with GDP-bound Rac1. The 85 and 110 kDa proteins were identified as the regulatory and catalytic subunits respectively of phosphatidylinositol 3-kinase. Several lines of evidence suggested that the 125 kDa protein is identical with Nck-associated protein 1 (Nap1). The mobilities of the 125 kDa protein and Nap1 on SDS/PAGE were indistinguishable, and the 125 kDa protein was depleted from brain extract by preincubation with the Src homology 3 domain of Nck to which Nap1 binds. Furthermore, antibodies to Nap1 reacted with the 125 kDa protein. Nap1 was co-immunoprecipitated with a constitutively active form of Rac expressed in Chinese hamster ovary cells. The observation that complex formation between activated Rac and PAK, but not that between Rac and Nap1, could be reproduced in vitro with recombinant proteins indicates that the interaction of Nap1 with Rac is indirect. The 140 kDa Rac-binding protein is a potential candidate for a link that connects Nap1 to Rac. The multimolecular complex comprising Rac, Nap1 and probably the 140 kDa protein might mediate some of the biological effects transmitted by the multipotent GTPase.
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44

Leonard, Edward J., and Teizo Yoshimura. "Human monocyte chemoattractant protein-1 (MCP-1)." Immunology Today 11 (January 1990): 97–101. http://dx.doi.org/10.1016/0167-5699(90)90035-8.

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45

Ross, M., G. L. Francis, L. Szabo, J. C. Wallace, and F. J. Ballard. "Insulin-like growth factor (IGF)-binding proteins inhibit the biological activities of IGF-1 and IGF-2 but not des-(1-3)-IGF-1." Biochemical Journal 258, no. 1 (February 15, 1989): 267–72. http://dx.doi.org/10.1042/bj2580267.

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(1) Many cell types secrete insulin-like growth factor (IGF)-binding proteins that can be expected to sequester free IGF and modify the biological activities of the growth factors. (2) A binding protein purified from bovine kidney (MDBK) cells potently inhibited the ability of IGF-2 to stimulate DNA synthesis or protein accumulation as well as to reduce rates of protein breakdown in chick embryo fibroblasts. The binding protein did not influence the biological activities of des-(1-3)-IGF-1, while effects on IGF-1 were intermediate. Since the chick embryo fibroblasts contain only the type 1 IGF receptor, the MDBK-cell binding protein must have reduced the accessibility of IGF-2 and IGF-1 to that receptor. Binding to the type 2 receptor on L6 myoblasts was also inhibited. (3) Inhibiting effects on both protein breakdown responsiveness to IGF and IGF binding to cell receptors were also observed with human amniotic fluid binding protein, although here IGF-1 and IGF-2 were equipotent. These results contrast with stimulatory responses on different IGF-1 actions of the same binding protein reported previously [Elgin, Busby & Clemmons (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 3254-3258]. (4) The biological potencies of IGF-1, IGF-2 and des-(1-3)-IGF-1 correlate inversely with their binding to proteins released into the medium by cells, so that the enhanced potency of des-(1-3)-IGF-1 is a consequence of it not binding to purified binding proteins or those released by cultured cells.
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46

Allen, P. B., A. T. Greenfield, P. Svenningsson, D. C. Haspeslagh, and P. Greengard. "Phactrs 1-4: A family of protein phosphatase 1 and actin regulatory proteins." Proceedings of the National Academy of Sciences 101, no. 18 (April 23, 2004): 7187–92. http://dx.doi.org/10.1073/pnas.0401673101.

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47

Hejnaes, Kim Ry, Stephen Bayne, Leif Nørskov, Hans Holmegaard, H. H. Sørensen, Johannes Thomsen, Lauge Schäffer, Axel Wollmer, and Lars Skriver. "Development of an optimized refolding process for recombinant Ala–Glu–IGF-1." "Protein Engineering, Design and Selection" 5, no. 8 (1992): 797–806. http://dx.doi.org/10.1093/protein/5.8.797.

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48

Kreiner, M., Z. Li, J. Beattie, S. M. Kelly, H. J. Mardon, and C. F. van der Walle. "Self-assembling multimeric integrin 5 1 ligands for cell attachment and spreading." Protein Engineering Design and Selection 21, no. 9 (May 23, 2008): 553–60. http://dx.doi.org/10.1093/protein/gzn032.

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49

Levin, Aviad, Zvi Hayouka, Ruth Brack-Werner, David J. Volsky, Assaf Friedler, and Abraham Loyter. "Novel regulation of HIV-1 replication and pathogenicity: Rev inhibition of integration." Protein Engineering, Design and Selection 22, no. 12 (October 29, 2009): 753–63. http://dx.doi.org/10.1093/protein/gzp060.

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50

Behravan, G., P. O. Lycksell, and G. Larsson. "Expression, purification and characterization of the homeodomain of rat ISL-1 protein." Protein Engineering Design and Selection 10, no. 11 (November 1, 1997): 1327–31. http://dx.doi.org/10.1093/protein/10.11.1327.

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