Academic literature on the topic 'Protein-protein'

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Journal articles on the topic "Protein-protein"

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Velesinović, Aleksandar, and Goran Nikolić. "Protein-protein interaction networks and protein-ligand docking: Contemporary insights and future perspectives." Acta Facultatis Medicae Naissensis 38, no. 1 (2021): 5–17. http://dx.doi.org/10.5937/afmnai38-28322.

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Traditional research means, such as in vitro and in vivo models, have consistently been used by scientists to test hypotheses in biochemistry. Computational (in silico) methods have been increasingly devised and applied to testing and hypothesis development in biochemistry over the last decade. The aim of in silico methods is to analyze the quantitative aspects of scientific (big) data, whether these are stored in databases for large data or generated with the use of sophisticated modeling and simulation tools; to gain a fundamental understanding of numerous biochemical processes related, in particular, to large biological macromolecules by applying computational means to big biological data sets, and by computing biological system behavior. Computational methods used in biochemistry studies include proteomics-based bioinformatics, genome-wide mapping of protein-DNA interaction, as well as high-throughput mapping of the protein-protein interaction networks. Some of the vastly used molecular modeling and simulation techniques are Monte Carlo and Langevin (stochastic, Brownian) dynamics, statistical thermodynamics, molecular dynamics, continuum electrostatics, protein-ligand docking, protein-ligand affinity calculations, protein modeling techniques, and the protein folding process and enzyme action computer simulation. This paper presents a short review of two important methods used in the studies of biochemistry - protein-ligand docking and the prediction of protein-protein interaction networks.
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Acuner Ozbabacan, S. E., H. B. Engin, A. Gursoy, and O. Keskin. "Transient protein-protein interactions." Protein Engineering Design and Selection 24, no. 9 (June 15, 2011): 635–48. http://dx.doi.org/10.1093/protein/gzr025.

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Schaeffer, R. D., and V. Daggett. "Protein folds and protein folding." Protein Engineering Design and Selection 24, no. 1-2 (November 3, 2010): 11–19. http://dx.doi.org/10.1093/protein/gzq096.

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Finkelstein, A. V. "Can protein unfolding simulate protein folding?" Protein Engineering Design and Selection 10, no. 8 (August 1, 1997): 843–45. http://dx.doi.org/10.1093/protein/10.8.843.

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Vakser, IIya A. "Main-chain complementarity in protein-protein recognition." "Protein Engineering, Design and Selection" 9, no. 9 (1996): 741–44. http://dx.doi.org/10.1093/protein/9.9.741.

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Lei, H., and Y. Duan. "Incorporating intermolecular distance into protein-protein docking." Protein Engineering Design and Selection 17, no. 12 (February 16, 2005): 837–45. http://dx.doi.org/10.1093/protein/gzh100.

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Abdullah, Syahid, Wisnu Ananta Kusuma, and Sony Hartono Wijaya. "Sequence-based prediction of protein-protein interaction using autocorrelation features and machine learning." Jurnal Teknologi dan Sistem Komputer 10, no. 1 (January 4, 2022): 1–11. http://dx.doi.org/10.14710/jtsiskom.2021.13984.

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Protein-protein interaction (PPI) can define a protein's function by knowing the protein's position in a complex network of protein interactions. The number of PPIs that have been identified is relatively small. Therefore, several studies were conducted to predict PPI using protein sequence information. This research compares the performance of three autocorrelation methods: Moran, Geary, and Moreau-Broto, in extracting protein sequence features to predict PPI. The results of the three extractions are then applied to three machine learning algorithms, namely k-Nearest Neighbor (KNN), Random Forest, and Support Vector Machine (SVM). The prediction models with the three autocorrelation methods can produce predictions with high average accuracy, which is 95.34% for Geary in KNN, 97.43% for Geary in RF, and 97.11% for Geary and Moran in SVM. In addition, the interacting protein pairs tend to have similar autocorrelation characteristics. Thus, the autocorrelation method can be used to predict PPI well.
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Diansyah, Mohammad Romano, Wisnu Ananta Kusuma, and Annisa Annisa. "Identification of significant protein in protein-protein interaction of Alzheimer disease using top-k representative skyline query." Jurnal Teknologi dan Sistem Komputer 9, no. 3 (April 24, 2021): 126–32. http://dx.doi.org/10.14710/jtsiskom.2021.13985.

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Alzheimer's disease is the most common neurodegenerative disease. This study aims to analyze protein-protein interaction (PPI) to provide a better understanding of multifactorial neurodegenerative diseases and can be used to find proteins that have a significant role in Alzheimer's disease. PPI data were obtained from experimental and computational predictions and analyzed using centrality measures. The Top-k RSP method was applied to find significant proteins in PPI networks using the dominance rule. The method was applied to the PPI data with the interaction sources from the experimental and experiment+prediction. The results indicate that APP and PSEN1 are significant proteins for Alzheimer's disease. This study also showed that both data sources (experiment+prediction) and the Top-k RSP algorithm proved useful for PPI analysis of Alzheimer's disease.
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Leatherbarrow, Robin J., and Alan R. Fersht. "Protein engineering." "Protein Engineering, Design and Selection" 1, no. 1 (1986): 7–16. http://dx.doi.org/10.1093/protein/1.1.7.

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Dill, Ken A. "Protein surgery." "Protein Engineering, Design and Selection" 1, no. 5 (1987): 369–71. http://dx.doi.org/10.1093/protein/1.5.369.

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Dissertations / Theses on the topic "Protein-protein"

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Jones, Susan. "Protein-protein interactions." Thesis, University College London (University of London), 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.338952.

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Cooper, Simon T. "PAX6 protein-protein interactions." Thesis, University of Edinburgh, 2005. http://hdl.handle.net/1842/29070.

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The gene PAX6 is located on chromosome 11 (11p13) and encodes a transcription factor (PAX6) that is expressed early in development. The PAX6 protein is expressed in the developing eye, regions of the brain, central nervous system (CNS), nasal epithelium and pancreas. PAX6 is best known for its role eye development with heterozygous mutations causing congenital ocular malformations. However, it must be remembered that PAX6 has multiple functions in the brain including specification of neuronal subtypes and axon guidance. There is growing understanding of the role of PAX6 as a transcription factor during development, and many of its DNA targets have recently been defined. However, almost nothing is known about the proteins with which PAX6 interacts. In the initial stage of my research I identified a conserved region consisting of the final 32 amino acids of the PST (proline, serine and threonine rich) domain of PAX6. Based on sequence homology and secondary structure predictions I classed this region as a novel domain, the ‘C terminal domain’. Next I used the yeast 2-hybrid system to investigate possible PAX6 protein interactions. By screening a mouse brain cDNA library with the C terminal domain and whole PST domain, I identified three novel and interesting interactors, HOMER3, DNCL1 and TRIM11. I re-confirmed these interactions in a pairwise manner using the yeast 2-hybrid system, and I showed that the C terminal domain was vital for the interactions between PAX6 and HOMER3 or DNCL1. Furthermore, certain C terminal mutations that are known to cause ocular malformations in patients are also sufficient to reduce or abolish these interactions. I attempted to further characterise the interactions by co-immunoprecipitation. However, this was not possible due to technical difficulties.
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Braute, Petter, and Jorg Eliassen Rødsjø. "Protein function prediction using annotated protein-protein interaction networks." Thesis, Norwegian University of Science and Technology, Department of Computer and Information Science, 2005. http://urn.kb.se/resolve?urn=urn:nbn:no:ntnu:diva-9177.

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Govers-Riemslag, Josepha Wilhelmina Philomena. "Protein-protein and protein-membrane interactions in prothrombin activation." Maastricht : Maastricht : Rijksuniversiteit Limburg ; University Library, Maastricht University [Host], 1994. http://arno.unimaas.nl/show.cgi?fid=6949.

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Lendel, Christofer. "Molecular principles of protein stability and protein-protein interactions." Doctoral thesis, Stockholm, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-480.

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Kneissl, Sabine. "Photocontrol of protein-protein and protein-nucleic acid interactions." Thesis, Cardiff University, 2009. http://orca.cf.ac.uk/54835/.

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Proteins often depend on a-helices for binding to other biomacromolecules. Reversible control of a-helix stability was accomplished in previous studies by incorporating a photoisomerisable azobenzene cross-linker into peptides, subsequently enabling the optical control of DNA-protein interactions. This approach was extended in this study to include protein-protein and protein-RNA interactions. One of the primary regulatory components in apoptosis signalling is the antiapoptotic protein Bcl-xL which interacts with the a-helical BH3 domain of the Bak protein. The Rev/RRE interaction is crucially involved in the life cycle of Human Immunodeficiency Virus. These interactions were targeted by designing peptides based on the BH3 domain of Bak and on the RNA-binding domain of Rev these peptides are activated by external light pulses after the incorporation of the cross-linker. The ability to control cross-linker conformation and hence peptide secondary structure was demonstrated by CD and UV/Vis spectroscopy. The binding to the target structure and complex disruption was determined in the dark-adapted and irradiated states using fluorescence based assays. Structural studies using NMR spectroscopy demonstrated that the alkylated peptides bind to the same part of the target molecule as the wild-type peptide, regardless of their structure. Moreover, one of the BH3 domain-based peptides and the light-controllable transcription factor PhotoMyoD were modified with protein transduction domains to enable future in vivo studies. Overall, this work opens the possibility to interfere reversibly and specifically with protein-protein and protein-RNA interactions and to study and modulate cellular function by optical control.
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Moont, Gidon. "Computational modelling of protein/protein and protein/DNA docking." Thesis, University College London (University of London), 2005. http://discovery.ucl.ac.uk/1445703/.

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The docking problem is to start with unbound conformations for the components of a complex, and computationally model a near-native structure for the complex. This thesis describes work in developing computer programs to tackle both protein/protein and protein/DNA docking. Empirical pair potential functions are generated from datasets of residue/residue interactions. A scoring function was parameterised and then used to screen possible complexes, generated by the global search computer algorithm FTDOCK using shape complementarity and electrostatics, for 9 systems. A correct docking (RMSD < 2.5A) is placed within the top 12% of the pair potential score ranked complexes for all systems. The computer software FTDOCK is modified for the docking of proteins to DNA, starting from the unbound protein and DNA coordinates modelled computationally. Complexes are then ranked by protein/DNA pair potentials derived from a database of 20 protein/DNA complexes. A correct docking (at least 65% of correct contacts) was identified at rank < 4 for 3 of the 8 complexes. This improved to 4 out of 8 when the complexes were filtered using experimental data defining the DNA footprint. The FTDOCK program was rewritten, and improved pair potential functions were developed from a set of non-homologous protein/protein interfaces. The algorithms were tested on a non-homologous set of 18 protein/protein complexes, starting with unbound conformations. Us ing cross-validated pair potential functions and the energy rninimisation software MultiDock, a correct docking ( RMSD of CQ interface 25% correct contacts) is found in the top 10 ranks in 6 out of 18 systems. The current best computational docking algorithms are discussed, and strategies for improvement are suggested.
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Chen, Dan. "Regulation of protein kinase C by protein-protein interactions /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2003. http://wwwlib.umi.com/cr/ucsd/fullcit?p3112821.

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Ginn, C. L. "Protein PEGylation on protein folding." Thesis, University College London (University of London), 2013. http://discovery.ucl.ac.uk/1403227/.

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E.coli is one of the most widely utilised hosts for protein expression due to its rapid growth, low production costs and high product yields. Often proteins are deposited as insoluble inclusion bodies that later require refolding to achieve biological activity. As a result of misfolding and aggregation for many proteins refolding is the yield limiting step in their production. Relevant therapeutic proteins obtained from E.coli include the α-helical barrel proteins (e.g. interferon-α2). Many proteins derived from E.coli are further modified after refolding by the covalent conjugation of poly(ethylene glycol) (PEG). This is known as PEGylation and several PEGylated α-helical barrel proteins are now routinely used in the clinic. PEGylation is used to address the short circulation half-life, immunogenicity and poor stability associated with many protein-based therapeutics. Our method of PEGylation is site specific. Conjugation occurs by bis-alkylation and takes advantage of the presence of the two free thiols from native disulfide bonds that have been reduced. The conjugated product has PEG linked to the protein through a three-carbon bridge spanning the two thiols derived from the native disulfide. Currently proteins are first purified and then a PEG reagent is used to covalently conjugate PEG to the protein. The PEG-protein conjugate is then purified. This means the protein has to be purified twice which can reduce yields. PEGylating the protein during its initial refolding would avoid the need of two downstream purification processes resulting in a more efficient process with an improved product yield. Therefore the aim of this project is to integrate the process of protein folding and PEGylation to make the production of PEGylated proteins more economically viable allowing their widespread use in the clinic. In this project the following hypotheses will be tested i) Reducing the number of purification steps that need to be performed to improve the overall yield of recovered protein, ii) The ability of PEG to impart the properties of a glycosyl group or a chaperone and protect the protein against aggregation during the folding process, iii) our method of PEGylation in particular should promote the formation of the protein’s disulfides bond and therefore the protein’s thermodynamically stable native state and iv) that the specificity of the conjugation can still be maintained despite the exposure of more sites of conjugation. Here we examine this process with different model alpha helical barrel proteins namely leptin, IFN-β and EPO. In each case the protein was denatured and fully reduced then refolded in the presence of a thiol specific, bis-alkylation PEG reagent allowing us to effectively capture the cysteine thiols during the refolding process. For IFN-β which is highly prone to aggregation, refolding yields in the presence of the PEG reagent were much improved suggesting that our method of PEGylation had a stabilising effect on the protein structure during refolding. This improved stability was also found to benefit the protein after PEGylation. Isolation of the purified PEGylated IFN- conjugate could be achieved in a single purification step in good yield. A similar activity to that generated on PEGylation of the fully folded protein was observed suggesting that for a protein with an accessible disulfide PEGylation did not significantly affect its folding. Some work was also carried out on RNase A and T1 which contain multiple inaccessible disulfides. In this instance PEGylation appeared to hinder the refolding process either by sterically hindering the formation of the protein’s native structure or by incorrect disulfide bond formation. The work described herein therefore suggests that it is possible to refold and PEGylate proteins within a single step but the effectiveness of this approach is likely to be protein dependant.
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McDowall, Mark. "Human protein-protein interaction prediction." Thesis, University of Dundee, 2011. https://discovery.dundee.ac.uk/en/studentTheses/697e465a-edbd-41d2-acda-5910a49e4157.

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Protein-protein interactions are essential for the survival of all living cells, allowing for processes such as cell signalling, metabolism and cell division to occur. Yet in humans there are only >38k annotated interactions of an interactome estimated to range between 150k to 600k interactions and out of a potential 300M protein pairs.Experimental methods to define the human interactome generate high quality results, but are expensive and slow. Computational methods play an important role to fill the gap.To further this goal, the prediction of human protein-protein interactions was investigated by the development of new predictive modules and the analysis of diverse datasets within the framework of the previously established PIPs protein-protein interaction predictor Scott and Barton 2007. New features considered include the semantic similarity of Gene Ontology annotating terms, clustering of interaction networks, primary sequences and gene co-expression. Integrating the new features in a naive Bayesian manner as part of the PIPs 2 predictor resulted in two sets of predictions. With a conservative threshold, the union of both sets is >300k predicted human interactions with an intersect of >94k interactions, of which a subset have been experimentally validated. The PIPs 2 predictor is also capable of making predictions in organisms that have no annotated interactions. This is achieved by training the PIPs 2 predictor based on a set of evidence and annotated interactions in another organism resulting in a ranking of protein pairs in the original organism of interest. Such an approach allows for predictions to be made across the whole proteome of poorly characterised organism, rather than being limited only to proteins with known orthologues. The work described here has increased the coverage of the human interactome and introduced a method to predict interactions in organisms that have previously had limited or no annotated interactions. The thesis aims to provide a stepping stone towards the completion of the human interactome and a way of predicting interactions in organisms that have been less well studied, but are often clinically relevant.
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Books on the topic "Protein-protein"

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Helmsen, Sabine. Protein-Ligand-, Protein-Inhibitor- und Protein-Protein-Wechselwirkungen. Wiesbaden: Springer Fachmedien Wiesbaden, 2020. http://dx.doi.org/10.1007/978-3-658-30151-4.

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Joël, Janin, and Wodak Shoshana J, eds. Protein modules and protein-protein interaction. Amsterdam: Academic Press, 2002.

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Fu, Haian. Protein-Protein Interactions. New Jersey: Humana Press, 2004. http://dx.doi.org/10.1385/1592597629.

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Poluri, Krishna Mohan, Khushboo Gulati, and Sharanya Sarkar. Protein-Protein Interactions. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-1594-8.

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Meyerkord, Cheryl L., and Haian Fu, eds. Protein-Protein Interactions. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2425-7.

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Wendt, Michael D., ed. Protein-Protein Interactions. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-28965-1.

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Werther, Meike, and Harald Seitz, eds. Protein – Protein Interaction. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-68820-4.

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service), SpringerLink (Online, ed. Protein-Protein Interactions. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012.

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Colin, Kleanthous, ed. Protein-protein recognition. Oxford: Oxford University Press, 2000.

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Protein-protein interactions. Hauppauge, N.Y: Nova Science Publisher's, 2010.

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Book chapters on the topic "Protein-protein"

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Martin, Shawn, W. Michael Brown, and Jean-Loup Faulon. "Using Product Kernels to Predict Protein Interactions." In Protein – Protein Interaction, 215–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/10_2007_084.

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Pitre, Sylvain, Md Alamgir, James R. Green, Michel Dumontier, Frank Dehne, and Ashkan Golshani. "Computational Methods For Predicting Protein–Protein Interactions." In Protein – Protein Interaction, 247–67. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2007_089.

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Chan, Catherine S., Tara M. L. Winstone, and Raymond J. Turner. "Investigating Protein–Protein Interactions by Far-Westerns." In Protein – Protein Interaction, 195–214. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2007_090.

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Abu-Farha, Mohamed, Fred Elisma, and Daniel Figeys. "Identification of Protein–Protein Interactions by Mass Spectrometry Coupled Techniques." In Protein – Protein Interaction, 67–80. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2007_091.

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Guan, Hongtao, and Endre Kiss-Toth. "Advanced Technologies for Studies on Protein Interactomes." In Protein – Protein Interaction, 1–24. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2007_092.

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Shin, Sung-Young, Sang-Mok Choo, Sun-Hee Woo, and Kwang-Hyun Cho. "Cardiac Systems Biology and Parameter Sensitivity Analysis: Intracellular Ca2+ Regulatory Mechanisms in Mouse Ventricular Myocytes." In Protein – Protein Interaction, 25–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2007_093.

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Beutling, Ulrike, Kai Städing, Theresia Stradal, and Ronald Frank. "Large-Scale Analysis of Protein–Protein Interactions Using Cellulose-Bound Peptide Arrays." In Protein – Protein Interaction, 115–52. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2008_096.

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Zhu, Yonggang, and Barbara E. Power. "Lab-on-a-chip in Vitro Compartmentalization Technologies for Protein Studies." In Protein – Protein Interaction, 81–114. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2008_098.

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Korf, Ulrike, Frauke Henjes, Christian Schmidt, Achim Tresch, Heiko Mannsperger, Christian Löbke, Tim Beissbarth, and Annemarie Poustka. "Antibody Microarrays as an Experimental Platform for the Analysis of Signal Transduction Networks." In Protein – Protein Interaction, 153–75. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2008_101.

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Chappell, Thomas G., and Phillip N. Gray. "Protein Interactions: Analysis Using Allele Libraries." In Protein – Protein Interaction, 47–66. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2008_102.

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Conference papers on the topic "Protein-protein"

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HSU, WEI-LUN, CHRISTOPHER OLDFIELD, JINGWEI MENG, FEI HUANG, BIN XUE, VLADIMIR N. UVERSKY, PEDRO ROMERO, and A. KEITH DUNKER. "INTRINSIC PROTEIN DISORDER AND PROTEIN-PROTEIN INTERACTIONS." In Proceedings of the Pacific Symposium. WORLD SCIENTIFIC, 2011. http://dx.doi.org/10.1142/9789814366496_0012.

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Sun, Dengdi, and Maolin Hu. "Determining Protein Function by Protein-Protein Interaction Network." In 2007 1st International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2007. http://dx.doi.org/10.1109/icbbe.2007.12.

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Chua, Hon Nian, Kang Ning, Wing-Kin Sung, Hon Wai Leong, and Limsoon Wong. "USING INDIRECT PROTEIN-PROTEIN INTERACTIONS FOR PROTEIN COMPLEX PREDICTION." In Proceedings of the CSB 2007 Conference. PUBLISHED BY IMPERIAL COLLEGE PRESS AND DISTRIBUTED BY WORLD SCIENTIFIC PUBLISHING CO., 2007. http://dx.doi.org/10.1142/9781860948732_0014.

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Doong, Shing, and Shu-Fen Hong. "Protein-Protein Interaction Document Mining." In 9th Joint Conference on Information Sciences. Paris, France: Atlantis Press, 2006. http://dx.doi.org/10.2991/jcis.2006.250.

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Hashmi, Irina, and Amarda Shehu. "Informatics-driven Protein-protein Docking." In BCB'13: ACM-BCB2013. New York, NY, USA: ACM, 2013. http://dx.doi.org/10.1145/2506583.2506709.

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Xue, Li C., Rafael A. Jordan, Yasser El-Manzalawy, Drena Dobbs, and Vasant Honavar. "Ranking docked models of protein-protein complexes using predicted partner-specific protein-protein interfaces." In the 2nd ACM Conference. New York, New York, USA: ACM Press, 2011. http://dx.doi.org/10.1145/2147805.2147866.

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Maruyama, Osamu, and Yuki Kuwahara. "RocSampler: Regularizing overlapping protein complexes in protein-protein interaction networks." In 2016 IEEE 6th International Conference on Computational Advances in Bio and Medical Sciences (ICCABS). IEEE, 2016. http://dx.doi.org/10.1109/iccabs.2016.7802774.

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Wu, Feihong, Fadi Towfic, Drena Dobbs, and Vasant Honavar. "Analysis of Protein Protein Dimeric Interfaces." In 2007 IEEE International Conference on Bioinformatics and Biomedicine (BIBM 2007). IEEE, 2007. http://dx.doi.org/10.1109/bibm.2007.60.

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Shatnawi, Maad. "Protein-Protein Interaction Prediction: Recent Advances." In 2017 28th International Workshop on Database and Expert Systems Applications (DEXA). IEEE, 2017. http://dx.doi.org/10.1109/dexa.2017.30.

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Xu, Liangliang, and Fei Zhu. "Protein protein interaction visualization using VisANT." In 2011 International Conference on Computer Science and Service System (CSSS). IEEE, 2011. http://dx.doi.org/10.1109/csss.2011.5973926.

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Reports on the topic "Protein-protein"

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Noy, A., T. Sulchek, and R. Friddle. Direct Probing of Protein-Protein Interactions. Office of Scientific and Technical Information (OSTI), March 2005. http://dx.doi.org/10.2172/15015174.

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Blackwell, T. K. C-Myc Protein-Protein and Protein-DNA Interactions: Targets for Therapeutic Intervention. Fort Belvoir, VA: Defense Technical Information Center, September 1998. http://dx.doi.org/10.21236/ada371161.

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Blackwell, T. K. C-Myc Protein-Protein and Protein-DNA Interactions: Targets for Therapeutic Intervention. Fort Belvoir, VA: Defense Technical Information Center, September 1997. http://dx.doi.org/10.21236/ada344737.

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Blackwell, T. K. C-MYC Protein-Protein and Protein-DNA Interactions: Targets for Therapeutic Intervention. Fort Belvoir, VA: Defense Technical Information Center, September 1999. http://dx.doi.org/10.21236/ada381686.

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Mural, R. (Protein engineering). Office of Scientific and Technical Information (OSTI), April 1987. http://dx.doi.org/10.2172/5608092.

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Bobe, Gerd, A. E. Gene Freeman, Gary L. Lindberg, and Donald C. Beitz. Milk Protein Genotypes Explain Variation of Milk Protein Composition. Ames (Iowa): Iowa State University, January 2004. http://dx.doi.org/10.31274/ans_air-180814-614.

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Fidelis, K., A. Adzhubej, A. Kryshtafovych, and P. Daniluk. Protein Model Database. Office of Scientific and Technical Information (OSTI), February 2005. http://dx.doi.org/10.2172/15014781.

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Dill, Ken A. Inverse Protein Folding. Fort Belvoir, VA: Defense Technical Information Center, May 1998. http://dx.doi.org/10.21236/ada361002.

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Faulon, Jean-Loup Michel, and Grant S. Heffelfinger. Shotgun protein sequencing. Office of Scientific and Technical Information (OSTI), June 2009. http://dx.doi.org/10.2172/959081.

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Tirrell, David A. Protein-Based Polymers. Fort Belvoir, VA: Defense Technical Information Center, November 1995. http://dx.doi.org/10.21236/ada302424.

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