[1] |
Berggard T, Linse S, James P. Method for the detection and analysis of protein-protein interactions[J]. Proteomics, 2007,7:2833-2842.
doi: 10.1002/pmic.200700131
pmid: 17640003
|
[2] |
Pandey A, Mann M. Proteomics to study genes and genomes[J]. Nature, 2000,405(6788):837-846.
doi: 10.1038/35015709
pmid: 10866210
|
[3] |
Villoutreix B O, Kuenemann M A, Poyet J L, et al. Drug-like protein-protein interaction modulators: challenges and opportunities for drug discovery and chemical biology[J]. Molecular Informatics, 2014,33:414-437.
doi: 10.1002/minf.201400040
pmid: 25254076
|
[4] |
Fernández-Recio J. Prediction of protein binding sites and hot spots[J]. WIREs Computational Molecular Science, 2011,1(5):680-698.
|
[5] |
Ruffner H, Baver A, Bovwmester T. Human protein-protein interaction networks and the value for drug discovery[J]. Drug Discovery Today, 2007,12(17/18):709-716.
doi: 10.1016/j.drudis.2007.07.011
|
[6] |
Shimada S, Shinzawa-Itoh K, Baba J, et al. Complex structure of cytochrome c-cytochrome c oxidase reveals a novel protein-protein interaction mode[J]. The EMBO Journal, 2017,36(3):291-300.
doi: 10.15252/embj.201695021
pmid: 27979921
|
[7] |
Patil S P, Fink M A, Enley E S, et al. Identification of small-molecule inhibitors of PD-1/PD-L1 protein-protein interaction[J]. Chemistry Select, 2018,3:2185-2189.
|
[8] |
Thakur S, Dhiman M, Tell G, et al. A review on protein-protein interaction network of APE1/Ref-1 and its associated biological functions[J]. Cell Biochemistry and Function, 2015,33:101-112.
doi: 10.1002/cbf.3100
pmid: 25790058
|
[9] |
Lemos A, Leão M, Soares J, et al. Medicinal chemistry strategies to disrupt the p53-MDM2/MDMX interaction[J]. Medicinal Research Reviews, 2016,36(5):789-844.
doi: 10.1002/med.21393
pmid: 27302609
|
[10] |
Zhou M, Li Q, Wang R X. Current experimental methods for characterizing protein-protein interactions[J]. ChemMedChem, 2016,11:738-756.
doi: 10.1002/cmdc.201500495
pmid: 26864455
|
[11] |
Rouck J E, Krapf J E, Roy J, et al. Recent advances in nanodic technology for membrane protein studies (2012---2017)[J]. FEBS Letters, 2017,591(14):2057-2088.
pmid: 28581067
|
[12] |
Wu L, Tang H L, Hu S Q, et al. Sensitive and simultaneous surface plasmon resonance detection of free and p53-bound MDM2 proteins from human sarcomas[J]. Analyst, 2018,143(9):2029-2034.
doi: 10.1039/c7an01918a
pmid: 29637949
|
[13] |
Boozer C, Kim G, Cong S X, et al. Looking towards label-free biomolecular interaction analysis in a high-throughput format: a review of new surface plasmon resonance technologies[J]. Current Opinion Biotechnology, 2006,17:400-405.
|
[14] |
Concepcion J, Witte K, Wartchow C, et al. Label-free detection of biomolecular interactions using BioLayer interferometry for kinetic characterization[J]. Combinatorial Chemistry & High Throughput Screening, 2009,12:791-800.
pmid: 19758119
|
[15] |
Sultana A, Lee J E. Measuring protein-protein and protein-nucleic acid interactions by biolayer interferometry [J]. Current Protocols in Protein Science, 2015, 79: 19.25.1-19.25.26.
|
[16] |
Pogoutse A K, Lai C L, Ostan N, et al. A method for measuring binding constants using unpurified in vivo biotinylated ligands[J]. Analytical Biochemistry, 2016,501:35-43.
doi: 10.1016/j.ab.2016.02.001
pmid: 26898305
|
[17] |
Wienken C J, Baaske P, Rothbauer U, et al. Protein-binding assays in biological liquids using microscale thermophoresis[J]. Nature Communications, 2010,1:100.
doi: 10.1038/ncomms1093
pmid: 20981028
|
[18] |
Seidel S A, Dijkman P M, Lea W A, et al. Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions[J]. Methods, 2013,59(3):301-315.
doi: 10.1016/j.ymeth.2012.12.005
pmid: 23270813
|
[19] |
Mao Y X, Yu L L, Yang R, et al. A novel method for the study of molecular interaction by using microscale thermophoresis[J]. Talanta, 2015,132:894-901.
doi: 10.1016/j.talanta.2014.09.038
pmid: 25476394
|
[20] |
Jerabek-Willemsen M, Wienken C J, Braun D, et al. Molecular interaction studies using microscale thermophoresis[J]. Assay and Drug Development Technologies, 2011,9(4):342-353.
doi: 10.1089/adt.2011.0380
pmid: 21812660
|
[21] |
Arbel N, Ben-Hail D, Shoshan-Barmatz V. Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein[J]. Journal of Biological Chemistry, 2012,287(27):23152-23161.
|
[22] |
Lin C C, Melo F A, Ghosh R, et al. Inhibition of basal FGF receptor signaling by dimeric Grb2[J]. Cell, 2012,149(7):1514-1524.
doi: 10.1016/j.cell.2012.04.033
pmid: 22726438
|
[23] |
Bhogaraju S, Cajanek L, Fort C, et al. Molecular basis of tubulin transport within the cilium by IFT74 and IFT81[J]. Science, 2013,341:1009-1012.
doi: 10.1126/science.1240985
pmid: 23990561
|
[24] |
Jerabek-Willemsen M, André T, Wanner R, et al. Microscale thermophoresis: interaction analysis and beyond[J]. Journal of Molecular Structure, 2014,1077:101-113.
doi: 10.1016/j.molstruc.2014.03.009
|
[25] |
Deng S H, Chen J F, Gao Z S, et al. Effects of donor and acceptor's fluorescence lifetimes on the method of applying Förster resonance energy transfer in STED microscopy[J]. Journal of Microscopy, 2018,269(1):59-65.
pmid: 28758683
|
[26] |
Leavesley S J, Britain A L, Cichon L K, et al. Assessing FRET using spectral techniques[J]. Cytometry Part A, 2013,83A:898-912.
|
[27] |
Vu L T, Nguyen T T K, Alam S, et al. Changing blue fluorescent protein to green fluorescent protein using chemical RNA editing as a novel strategy in genetic restoration[J]. Chemical Biology & Drug Design, 2015,86:1242-1252.
doi: 10.1111/cbdd.12592
pmid: 26031895
|
[28] |
Liu R, Hu X J, Ding Y. Rational design of a pH-insensitive cyan fluorescent protein CyPet2 based on the CyPet crystal structure[J]. FEBS Letters, 2017,591:1761-1769.
doi: 10.1002/feb2.2017.591.issue-12
pmid: 28504316
|
[29] |
Otsubo R, Kim M, Lee J, et al. Midori-ishi Cyan/monomeric Kusabira-orange-based fluorescence resonance energy transfer assay for characterization of various E3 ligases[J]. Genes to Cells, 2016,21:608-623.
doi: 10.1111/gtc.12369
pmid: 27091465
|
[30] |
Aker J, Hesselink R, Engel R, et al. In Vivo hexamerization and characterization of the arabidopsis AAA ATPase CDC$_{4}$8A complex using forster resonance energy transfer-fluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy[J]. Plant Physiology, 2007,145:339-350.
doi: 10.1104/pp.107.103986
pmid: 17693538
|
[31] |
Song T, Madahar V, Liao J Y. Development of FRET assay into quantitative and high-throughput screening technology platforms for protein-protein interactions[J]. Ann Biomed Eng, 2011,39:1224-1234.
doi: 10.1007/s10439-010-0225-x
pmid: 21174150
|
[32] |
Kost L J, Mootz H D. A FRET Sensor to Monitor Bivalent SUMO--SIM Interactions in SUMO Chain Binding[J]. ChemBioChem, 2018,19:177-184.
doi: 10.1002/cbic.201700507
pmid: 29120074
|
[33] |
Mahajan P N, Linder K, Berry G, et al. Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer[J]. Nature Biotechnology, 1998,16:547-552.
doi: 10.1038/nbt0698-547
pmid: 9624685
|
[34] |
Yegorova S, Chavaroche A E, Rodriguez M C, et al. Development of an AlphaScreen assay for discovery of inhibitors of low-affinity glycan-lectin interactions[J]. Analytical Biochemistry, 2013,439:121-131.
|
[35] |
Zhang M, Wisniewski J A, Ji H T. AlphaScreen selectivity assay for $\beta $-catenin/B-cell lymphoma 9 inhibitors[J]. Analytical Biochemistry, 2015,469:43-53.
doi: 10.1016/j.ab.2014.09.018
pmid: 25312469
|
[36] |
Hill S J, Williams C, May L T. Insights into GPCR pharmacology from the measurement of changes in intracellular cyclic AMP: advantages and pitfalls of differing methodologies[J]. British Journal of Pharmacology, 2010,161(6):1266-1275.
doi: 10.1111/j.1476-5381.2010.00779.x
pmid: 21049583
|
[37] |
Moad H E, Pioszak A A. Selective CGRP and adrenomedullin peptide binding by tethered RAMP-calcitonin receptor-like receptor extracellular domain fusion proteins[J]. Protein Science, 2013,22:1775-1785.
doi: 10.1002/pro.2377
pmid: 24115156
|
[38] |
Harrison A T, Kriel F H, Papathanasopoulos M A, et al. The evalution of statins as potential inhibitors of the LEDGF/p75-HIV-1 integrase interaction[J]. Chemical Biology & Drug Design, 2015,85:290-295.
doi: 10.1111/cbdd.12384
pmid: 24954548
|
[39] |
Ogita N, Okushima Y, Tokizawa M, et al. Identifying the target genes of SUPPRESSOR OF GAMMARESPONSE 1, a master transcription factor controlling DNA damage response in Arabidopsis[J]. The Plant Journal, 2018,94:439-453.
doi: 10.1111/tpj.13866
pmid: 29430765
|
[40] |
Sierecki E, Stevers L M, Giles N, et al. Rapid mapping of interactions between human SNX-BAR proteins measured in vitro by AlphaScreen and single-molecule spectroscopy[J]. Molecular Cellular Proteomics, 2014,13:2233-2245.
doi: 10.1074/mcp.M113.037275
pmid: 24866125
|
[41] |
Wagstaff K M, Rawlinson S M, Hearps A C, et al. An AlphaScreen-based assay for high-throughput screening for specific inhibitors of nuclear import[J]. Journal of Biomolecular Screening, 2011,16(2):192-200.
doi: 10.1177/1087057110390360
pmid: 21297106
|
[42] |
Montse M, Salvador V, Francesc X. Protein complementation assay: approaches for the in vivo analysis of protein interactions[J]. FEBS Letters, 2009,583:1684-1691.
doi: 10.1016/j.febslet.2009.03.002
pmid: 19269288
|
[43] |
Shibasaki S, Sakata K, Ishii J, et al. Development of a yeast protein fragment complementation assay (PCA) system using dihydrofolate reductase (DHFR) with specific additives[J]. Applied Microbiology Biotechnology, 2008,80(4):735-743.
doi: 10.1007/s00253-008-1624-x
pmid: 18670770
|
[44] |
Nord O, Gustrin A, Nygren P A. Fluorescent of b-lactamase activity in living Escherichia coli cells via esterase supplementation[J]. FEMS Microbilogy Letters, 2005,242:73-79.
|
[45] |
Ozawa T, Nogami S, Sato M, et al. A fluorescent indicator for detecting protein-protein interactions in vivo based on protein splicing[J]. Analytical Chemistry, 2000,72(21):5151-5157.
doi: 10.1021/ac000617z
pmid: 11080857
|
[46] |
Kim S B, Sato M, Tao H. Split Gaussia luciferase-based bioluminescence template for tracing protein dynamics in living cell[J]. Analytical Chemistry, 2009,81(1):67-74.
doi: 10.1021/ac801658y
pmid: 19061336
|
[47] |
Rochette S, Gagnon-Arsenault I, Diss G, et al. Modulation of the yeast protein interactome in response to DNA damage[J]. Journal of Proteomics, 2014,100:25-36.
doi: 10.1016/j.jprot.2013.11.007
pmid: 24262151
|
[48] |
Liu T Y, Chou W C, Chen W Y, et al. Detection of membrane protein-protein interaction in planta based on dual-intein-couple tripartite split-GFP association[J]. Plant Journal, 2018,94:426-438.
|
[49] |
Luo L, King N P, Yeo J C, et al. Single-step protease cleavage elution for identification of protein-protein interactions from GST pull-down and mass spectrometry[J]. Proteomics, 2014,14:19-23.
doi: 10.1002/pmic.201300315
pmid: 24259493
|
[50] |
Schulte R, Talamas J, Doucet C, et al. Single bead affinity detection (SINBAD) for the analysis of protein-protein interactions[J]. PLoS One, 2008,3:e2061.
doi: 10.1371/journal.pone.0002061
pmid: 18446240
|
[51] |
Kamanova J, Sun H, Lara-Tejero M, et al. The salmonella effector protein SopA modulates innate immune responses by targeting TRIM E3 ligase family members[J]. PLoS Pathogens, 2016,12(4):e1005552.
doi: 10.1371/journal.ppat.1005552
pmid: 27058235
|
[52] |
Fedosejevs E T, Liu L N C, Abergel M, et al. Coimmunoprecipitation of reversibly glycosylated polypeptide with sucrose synthase from developing castor oilseeeds[J]. FEBS Letters, 2017,591:3872-3880.
doi: 10.1002/1873-3468.12893
pmid: 29110302
|