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Journal articles on the topic 'Specific protein'

Author: Grafiati

Published: 25 May 2024

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1

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

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2

Hunte, C. "Specific protein–lipid interactions in membrane proteins." Biochemical Society Transactions 33, no. 5 (2005): 938. http://dx.doi.org/10.1042/bst20050938.

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3

Hunte, C. "Specific protein–lipid interactions in membrane proteins." Biochemical Society Transactions 33, no. 5 (2005): 938–42. http://dx.doi.org/10.1042/bst0330938.

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Many membrane proteins selectively bind defined lipid species. This specificity has an impact on correct insertion, folding, structural integrity and full functionality of the protein. How are these different tasks achieved? Recent advances in structural research of membrane proteins provide new information about specific protein–lipid interactions. Tightly bound lipids in membrane protein structures are described and general principles of the binding interactions are deduced. Lipid binding is stabilized by multiple non-covalent interactions from protein residues to lipid head groups and hydro

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4

Baldrich, Marcus, and Werner Goebel. "Rapid and efficient site-specific mutagenesis." "Protein Engineering, Design and Selection" 3, no. 6 (1990): 563. http://dx.doi.org/10.1093/protein/3.6.563.

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5

Parsons, Helen L., John C. Earnshaw, Jane Wilton, et al. "Directing phage selections towards specific epitopes." "Protein Engineering, Design and Selection" 9, no. 11 (1996): 1043–49. http://dx.doi.org/10.1093/protein/9.11.1043.

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6

Jongen-Rêlo, Ana L., and Joram Feldon. "Specific neuronal protein." Physiology & Behavior 76, no. 4-5 (2002): 449–56. http://dx.doi.org/10.1016/s0031-9384(02)00732-1.

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7

Prasad Bahadur, Ranjit, Pinak Chakrabarti, Francis Rodier, and Joël Janin. "A Dissection of Specific and Non-specific Protein–Protein Interfaces." Journal of Molecular Biology 336, no. 4 (2004): 943–55. http://dx.doi.org/10.1016/j.jmb.2003.12.073.

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8

Kusakabe, Takahiro, Kiyohisa Motoki, Yasushi Sugimoto, Yozo Takasaki, and Katsuji Hori. "Human aldolase B: liver-specific properties of the isozyme depend on type B isozyme group-specific sequences." "Protein Engineering, Design and Selection" 7, no. 11 (1994): 1387–93. http://dx.doi.org/10.1093/protein/7.11.1387.

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9

Tindbaek, Nikolaj, Allan Svendsen, Peter Rahbek Oestergaard, and Henriette Draborg. "Engineering a substrate‐specific cold‐adapted subtilisin." Protein Engineering, Design and Selection 17, no. 2 (2004): 149–56. http://dx.doi.org/10.1093/protein/gzh019.

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10

Kumar, Challa V., Apinya Buranaprapuk, and Jyotsna Thota. "Protein scissors: Photocleavage of proteins at specific locations." Journal of Chemical Sciences 114, no. 6 (2002): 579–92. http://dx.doi.org/10.1007/bf02708852.

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11

Paoni, Nicholas F., Alice M. Chow, Luis C. Peña, Bruce A. Keyt, Mark J. Zoller, and William F. Bennett. "Making tissue-type plasminogen activator more fibrin specific." "Protein Engineering, Design and Selection" 6, no. 5 (1993): 529–34. http://dx.doi.org/10.1093/protein/6.5.529.

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12

Wingfield, Paul T., Robert J. Mattaliano, H. Robson MacDonald та ін. "Recombinant-derived interleukin-1α stabilized against specific deamidation". "Protein Engineering, Design and Selection" 1, № 5 (1987): 413–17. http://dx.doi.org/10.1093/protein/1.5.413.

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13

Richter, Susanne A., Kay Stubenrauch, Hauke Lilie, and Rainer Rudolph. "Polyionic fusion peptides function as specific dimerization motifs." Protein Engineering, Design and Selection 14, no. 10 (2001): 775–83. http://dx.doi.org/10.1093/protein/14.10.775.

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14

Nyikos, Lajos, Ágnes Simon, Péter Barabás, and Julianna Kardos. "Ligand-specific conformations of an ionotropic glutamate receptor." Protein Engineering, Design and Selection 15, no. 9 (2002): 717–20. http://dx.doi.org/10.1093/protein/15.9.717.

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15

Jäger, Marcus, Xavier Michalet, and Shimon Weiss. "Protein-protein interactions as a tool for site-specific labeling of proteins." Protein Science 14, no. 8 (2005): 2059–68. http://dx.doi.org/10.1110/ps.051384705.

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16

Jonczyk, P., and A. Nowicka. "Specific in vivo protein-protein interactions between Escherichia coli SOS mutagenesis proteins." Journal of bacteriology 178, no. 9 (1996): 2580–85. http://dx.doi.org/10.1128/jb.178.9.2580-2585.1996.

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17

Lawrence, David S., and Jinkui Niu. "Protein Kinase InhibitorsThe Tyrosine-Specific Protein Kinases." Pharmacology & Therapeutics 77, no. 2 (1998): 81–114. http://dx.doi.org/10.1016/s0163-7258(97)00052-1.

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18

Schmid, Stefan W., Waldemar Uhl, Anne Steinle, Bettina Rau, Christian Seiler, and Markus W. Büchler. "Human pancreas-specific protein." International Journal of Pancreatology 19, no. 3 (1996): 165–70. http://dx.doi.org/10.1007/bf02787364.

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19

Stein, Richard A. "Protein-Specific Discovery Strategies." Genetic Engineering & Biotechnology News 34, no. 6 (2014): 1, 12, 13, 15. http://dx.doi.org/10.1089/gen.34.06.01.

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20

Parekh, R. B. "Site-specific protein glycosylation." Advanced Drug Delivery Reviews 13, no. 3 (1994): 251–66. http://dx.doi.org/10.1016/0169-409x(94)90014-0.

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21

Ebke, Lindsey A., Satyabrata Sinha, Gayle J. T. Pauer, and Stephanie A. Hagstrom. "Photoreceptor Compartment-Specific TULP1 Interactomes." International Journal of Molecular Sciences 22, no. 15 (2021): 8066. http://dx.doi.org/10.3390/ijms22158066.

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Photoreceptors are highly compartmentalized cells with large amounts of proteins synthesized in the inner segment (IS) and transported to the outer segment (OS) and synaptic terminal. Tulp1 is a photoreceptor-specific protein localized to the IS and synapse. In the absence of Tulp1, several OS-specific proteins are mislocalized and synaptic vesicle recycling is impaired. To better understand the involvement of Tulp1 in protein trafficking, our approach in the current study was to physically isolate Tulp1-containing photoreceptor compartments by serial tangential sectioning of retinas and to id

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22

De Rosa, Lucia, Aitziber L. Cortajarena, Alessandra Romanelli, Lynne Regan, and Luca Domenico D'Andrea. "Site-specific protein double labeling by expressed protein ligation: applications to repeat proteins." Org. Biomol. Chem. 10, no. 2 (2012): 273–80. http://dx.doi.org/10.1039/c1ob06397a.

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23

Baldwin, Jack E., Stephen L. Martin, and John D. Sutherland. "Site-specific forced misincorporation mutagenesis using modified T7 DNA polymerase." "Protein Engineering, Design and Selection" 4, no. 5 (1991): 579–84. http://dx.doi.org/10.1093/protein/4.5.579.

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24

Casey, J. L., A. M. Sanalla, D. Tamvakis, et al. "Peptides specific for Mycobacterium avium subspecies paratuberculosis infection: diagnostic potential." Protein Engineering Design and Selection 24, no. 8 (2011): 589–96. http://dx.doi.org/10.1093/protein/gzr026.

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25

Daffu, Gurdip K., Patricia Lopez, Francine Katz, et al. "Sulfhydryl-specific PEGylation of phosphotriesterase cysteine mutants for organophosphate detoxification." Protein Engineering Design and Selection 28, no. 11 (2015): 501–6. http://dx.doi.org/10.1093/protein/gzv036.

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26

Nicholson, Thomas B., and Clifford P. Stanners. "Specific inhibition of GPI-anchored protein function by homing and self-association of specific GPI anchors." Journal of Cell Biology 175, no. 4 (2006): 647–59. http://dx.doi.org/10.1083/jcb.200605001.

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The functional specificity conferred by glycophosphatidylinositol (GPI) anchors on certain membrane proteins may arise from their occupancy of specific membrane microdomains. We show that membrane proteins with noninteractive external domains attached to the same carcinoembryonic antigen (CEA) GPI anchor, but not to unrelated neural cell adhesion molecule GPI anchors, colocalize on the cell surface, confirming that the GPI anchor mediates association with specific membrane domains and providing a mechanism for specific signaling. This directed targeting was exploited by coexpressing an externa

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27

Stolarski, Ryszard. "Thermodynamics of specific protein-RNA interactions." Acta Biochimica Polonica 50, no. 2 (2003): 297–318. http://dx.doi.org/10.18388/abp.2003_3688.

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Description of the recognition specificity between proteins and nucleic acids at the level of molecular interactions is one of the most challenging tasks in biophysics. It is key to understanding the course and control of gene expression and to the application of the thus acquired knowledge in chemotherapy. This review presents experimental results of thermodynamic studies and a discussion of the role of thermodynamics in formation and stability of functional protein-RNA complexes, with a special attention to the interactions involving mRNA 5' cap and cap-binding proteins in the initiation of

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28

Nalawansha, Dhanusha A., Ke Li, John Hines, and Craig M. Crews. "Hijacking Methyl Reader Proteins for Nuclear-Specific Protein Degradation." Journal of the American Chemical Society 144, no. 12 (2022): 5594–605. http://dx.doi.org/10.1021/jacs.2c00874.

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29

Rose, Megan L. H., and Maxwell T. Hincke. "Protein constituents of the eggshell: eggshell-specific matrix proteins." Cellular and Molecular Life Sciences 66, no. 16 (2009): 2707–19. http://dx.doi.org/10.1007/s00018-009-0046-y.

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30

Glover, Claiborne V. C. "Sequence-specific protein-DNA recognition by transcriptional regulatory proteins." Plant Molecular Biology Reporter 7, no. 3 (1989): 183–208. http://dx.doi.org/10.1007/bf02668686.

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31

Löwenadler, B., B. Nilsson, L. Abrahmsén, et al. "Production of specific antibodies against protein A fusion proteins." EMBO Journal 5, no. 9 (1986): 2393–98. http://dx.doi.org/10.1002/j.1460-2075.1986.tb04509.x.

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32

Hemler, Martin E. "Specific tetraspanin functions." Journal of Cell Biology 155, no. 7 (2001): 1103–8. http://dx.doi.org/10.1083/jcb.200108061.

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Relatively little attention has been given to the large family of abundantly expressed transmembrane proteins known as tetraspanins. Now, the importance of tetraspanins is strongly supported by emerging genetic evidence, coupled with new insights into the biochemistry and functions of tetraspanin protein complexes.

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33

Dan, Feng, and Zeng Zong-Hao. "Specific and Non-Specific Contacts in Protein Crystals." Protein & Peptide Letters 11, no. 4 (2004): 361–66. http://dx.doi.org/10.2174/0929866043406959.

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34

Janin, Joël. "Specific versus non-specific contacts in protein crystals." Nature Structural Biology 4, no. 12 (1997): 973–74. http://dx.doi.org/10.1038/nsb1297-973.

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35

Gentzsch, Martina, and Widmar Tanner. "Protein-O-glycosylation in yeast: protein-specific mannosyltransferases." Glycobiology 7, no. 4 (1997): 481–86. http://dx.doi.org/10.1093/glycob/7.4.481.

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36

Lyons, Alan, David J. King, Raymond J. Owens, et al. "Site-specific attachment to recombinant antibodies via introduced surface cysteine residues." "Protein Engineering, Design and Selection" 3, no. 8 (1990): 703–8. http://dx.doi.org/10.1093/protein/3.8.703.

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37

Hong, S. H., Q. Hao, and W. Maret. "Domain-specific fluorescence resonance energy transfer (FRET) sensors of metallothionein/thionein." Protein Engineering, Design and Selection 18, no. 6 (2005): 255–63. http://dx.doi.org/10.1093/protein/gzi031.

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38

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 (2009): 357–66. http://dx.doi.org/10.1093/protein/gzp011.

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39

Koide, A., J. Wojcik, R. N. Gilbreth, A. Reichel, J. Piehler, and S. Koide. "Accelerating phage-display library selection by reversible and site-specific biotinylation." Protein Engineering Design and Selection 22, no. 11 (2009): 685–90. http://dx.doi.org/10.1093/protein/gzp053.

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40

Arai, Tomonori, Masayoshi Uehata, Hiroyuki Akatsuka, and Tsutomu Kamiyama. "A quantitative analysis to unveil specific binding proteins for bioactive compounds." Protein Engineering, Design and Selection 26, no. 4 (2012): 249–54. http://dx.doi.org/10.1093/protein/gzs103.

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41

Hanioka, Nobumitsu, Kenneth Korzekwa, and Frank J. Gonzalez. "Sequence requirements for cytochromes P450IIA1 and P450IIA2 catalytic activity: evidence for both specific and non-specific substrate binding interactions through use of chimeric cDNAs and cDNA expression." "Protein Engineering, Design and Selection" 3, no. 7 (1990): 571–75. http://dx.doi.org/10.1093/protein/3.7.571.

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42

Wouters-Tyrou, D., A. Martin-Ponthieu, N. Ledoux-Andula, et al. "Squid spermiogenesis: molecular characterization of testis-specific pro-protamines." Biochemical Journal 309, no. 2 (1995): 529–34. http://dx.doi.org/10.1042/bj3090529.

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Cuttlefish spermiogenesis is characterized by a two-step nuclear protein transition: histones-->spermatid-specific protein (protein T)-->sperm protamine (protein Sp). A similar situation can be observed in another Cephalopod species, the squid Loligo pealeii. The protein T from Loligo consists of two structural variants, T1 and T2 (molecular masses: 10788 and 10791 Da respectively), phosphorylated to different degrees (2-6 phosphate groups). The primary structures of these two variants and of the protamine variant Sp2 were established from sequence analysis and mass spectrometric data of

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43

Best, Robert B., Wenwei Zheng, and Jeetain Mittal. "Balanced Protein–Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association." Journal of Chemical Theory and Computation 10, no. 11 (2014): 5113–24. http://dx.doi.org/10.1021/ct500569b.

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44

Jonczyk, Piotr, Adrianna Nowicka, and Iwona J. Fijalkowska. "P III B.4 Specific protein-protein interactions between E. coll DNA replication proteins." Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis 379, no. 1 (1997): S22. http://dx.doi.org/10.1016/s0027-5107(97)82666-8.

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45

Strandmann, E. P. v., C. Zoidl, H. Nakhei, et al. "A highly specific and sensitive monoclonal antibody detecting histidine-tagged recombinant proteins." Protein Engineering Design and Selection 8, no. 7 (1995): 733–35. http://dx.doi.org/10.1093/protein/8.7.733.

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46

Shukla, G. S., and D. N. Krag. "Cancer cell-specific internalizing ligands from phage displayed -lactamase-peptide fusion libraries." Protein Engineering Design and Selection 23, no. 6 (2010): 431–40. http://dx.doi.org/10.1093/protein/gzq013.

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47

Nisbet, R. M., J. Nigro, K. Breheney, J. Caine, M. K. Hattarki, and S. D. Nuttall. "Central amyloid- -specific single chain variable fragment ameliorates A aggregation and neurotoxicity." Protein Engineering Design and Selection 26, no. 10 (2013): 571–80. http://dx.doi.org/10.1093/protein/gzt025.

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48

Barinka, Cyril, Jakub Ptacek, Antonia Richter, Zora Novakova, Volker Morath, and Arne Skerra. "Selection and characterization of Anticalins targeting human prostate-specific membrane antigen (PSMA)." Protein Engineering Design and Selection 29, no. 3 (2016): 105–15. http://dx.doi.org/10.1093/protein/gzv065.

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49

Gunneriusson, E., K. Nord, M. Uhlén, and P. Å. Nygren. "Affinity maturation of a Taq DNA polymerase specific affibody by helix shuffling." Protein Engineering, Design and Selection 12, no. 10 (1999): 873–78. http://dx.doi.org/10.1093/protein/12.10.873.

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50

Gould, Christine, and Chung F. Wong. "Designing specific protein kinase inhibitors:." Pharmacology & Therapeutics 93, no. 2-3 (2002): 169–78. http://dx.doi.org/10.1016/s0163-7258(02)00186-9.

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