Статті в журналах: "Crosslinking mass spectrometry"

1

Sinz, Andrea. "Crosslinking Mass Spectrometry Goes In-Tissue." Cell Systems 6, no. 1 (January 2018): 10–12. http://dx.doi.org/10.1016/j.cels.2018.01.005.

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2

Schneider, Michael, Adam Belsom, and Juri Rappsilber. "Protein Tertiary Structure by Crosslinking/Mass Spectrometry." Trends in Biochemical Sciences 43, no. 3 (March 2018): 157–69. http://dx.doi.org/10.1016/j.tibs.2017.12.006.

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3

Chen, Zhuo Angel, and Juri Rappsilber. "Protein structure dynamics by crosslinking mass spectrometry." Current Opinion in Structural Biology 80 (June 2023): 102599. http://dx.doi.org/10.1016/j.sbi.2023.102599.

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4

Xia, Yingzi. "Exploring misfolded proteins with crosslinking mass spectrometry." Biophysical Journal 123, no. 3 (February 2024): 206a. http://dx.doi.org/10.1016/j.bpj.2023.11.1301.

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5

Petrotchenko, Evgeniy V., and Christoph H. Borchers. "Crosslinking combined with mass spectrometry for structural proteomics." Mass Spectrometry Reviews 29, no. 6 (August 21, 2010): 862–76. http://dx.doi.org/10.1002/mas.20293.

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6

Dancy, Beverley M., Fan Liu, Philip Lössl, Albert J. R. Heck, and Robert S. Balaban. "The mitochondrial interactome visualized by crosslinking mass spectrometry." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1857 (August 2016): e22. http://dx.doi.org/10.1016/j.bbabio.2016.04.045.

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7

Singh, Arunima. "Crosslinking mass spectrometry data bolster protein structure prediction." Nature Methods 20, no. 5 (May 2023): 633. http://dx.doi.org/10.1038/s41592-023-01890-3.

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8

Graziadei, Andrea, and Juri Rappsilber. "Leveraging crosslinking mass spectrometry in structural and cell biology." Structure 30, no. 1 (January 2022): 37–54. http://dx.doi.org/10.1016/j.str.2021.11.007.

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9

Chen, Zhuo A., and Juri Rappsilber. "Protein Dynamics in Solution by Quantitative Crosslinking/Mass Spectrometry." Trends in Biochemical Sciences 43, no. 11 (November 2018): 908–20. http://dx.doi.org/10.1016/j.tibs.2018.09.003.

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10

Bullock, Joshua Matthew Allen, Neeladri Sen, Konstantinos Thalassinos, and Maya Topf. "Modeling Protein Complexes Using Restraints from Crosslinking Mass Spectrometry." Structure 26, no. 7 (July 2018): 1015–24. http://dx.doi.org/10.1016/j.str.2018.04.016.

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11

Kim, Samuel, Jae Kyoo Lee, Hong Gil Nam, and Richard N. Zare. "Photo-Activated Crosslinking Mass Spectrometry for Studying Biomolecular Interactions." Biophysical Journal 106, no. 2 (January 2014): 459a. http://dx.doi.org/10.1016/j.bpj.2013.11.2601.

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12

Wang, Haodong, Min Zhang, and Liang Ge. "Crosslinking and Mass Spectrometry to Identify Regulators in Unconventional Secretion." Trends in Biochemical Sciences 46, no. 8 (August 2021): 701–2. http://dx.doi.org/10.1016/j.tibs.2021.03.006.

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13

Xia, Yingzi, and Stephen D. Fried. "Studying the refoldability of the proteome using crosslinking mass spectrometry." Biophysical Journal 121, no. 3 (February 2022): 184a. http://dx.doi.org/10.1016/j.bpj.2021.11.1800.

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14

Donelan, Chelsee A., Rathna Veeramachaneni, David J. Lapinsky, and Michael Cascio. "Using Crosslinking and Mass Spectrometry to Study Glycine Receptor Allostery." Biophysical Journal 102, no. 3 (January 2012): 612a. http://dx.doi.org/10.1016/j.bpj.2011.11.3336.

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15

Muizebelt, W. J., and M. W. F. Nielen. "Oxidative Crosslinking of Unsaturated Fatty Acids Studied with Mass Spectrometry." Journal of Mass Spectrometry 31, no. 5 (May 1996): 545–54. http://dx.doi.org/10.1002/(sici)1096-9888(199605)31:5<545::aid-jms329>3.0.co;2-1.

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16

Makepeace, Karl A. T., Yassene Mohammed, Elena L. Rudashevskaya, Evgeniy V. Petrotchenko, F. Nora Vögtle, Chris Meisinger, Albert Sickmann, and Christoph H. Borchers. "Improving Identification of In-organello Protein-Protein Interactions Using an Affinity-enrichable, Isotopically Coded, and Mass Spectrometry-cleavable Chemical Crosslinker." Molecular & Cellular Proteomics 19, no. 4 (February 12, 2020): 624–39. http://dx.doi.org/10.1074/mcp.ra119.001839.

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Анотація:

An experimental and computational approach for identification of protein-protein interactions by ex vivo chemical crosslinking and mass spectrometry (CLMS) has been developed that takes advantage of the specific characteristics of cyanurbiotindipropionylsuccinimide (CBDPS), an affinity-tagged isotopically coded mass spectrometry (MS)-cleavable crosslinking reagent. Utilizing this reagent in combination with a crosslinker-specific data-dependent acquisition strategy based on MS2 scans, and a software pipeline designed for integrating crosslinker-specific mass spectral information led to demonstrated improvements in the application of the CLMS technique, in terms of the detection, acquisition, and identification of crosslinker-modified peptides. This approach was evaluated on intact yeast mitochondria, and the results showed that hundreds of unique protein-protein interactions could be identified on an organelle proteome-wide scale. Both known and previously unknown protein-protein interactions were identified. These interactions were assessed based on their known sub-compartmental localizations. Additionally, the identified crosslinking distance constraints are in good agreement with existing structural models of protein complexes involved in the mitochondrial electron transport chain.

17

Hagen, Susan E., Kun Liu, Yafei Jin, Lolita Piersimoni, Philip C. Andrews, and Hollis D. Showalter. "Synthesis of CID-cleavable protein crosslinking agents containing quaternary amines for structural mass spectrometry." Organic & Biomolecular Chemistry 16, no. 37 (2018): 8245–48. http://dx.doi.org/10.1039/c8ob00329g.

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Two novel cyclic quaternary amine crosslinking probes are synthesized for structural mass spectrometry of protein complexes in solution and for analysis of protein interactions in organellar and whole cell extracts.

18

Tang, Xiaoting, Helisa H. Wippel, Juan D. Chavez, and James E. Bruce. "Crosslinking mass spectrometry: A link between structural biology and systems biology." Protein Science 30, no. 4 (March 6, 2021): 773–84. http://dx.doi.org/10.1002/pro.4045.

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19

Topf, Maya. "Modeling Protein Monomers and Complexes using Restraints from Crosslinking Mass Spectrometry." Biophysical Journal 116, no. 3 (February 2019): 330a. http://dx.doi.org/10.1016/j.bpj.2018.11.1790.

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20

Perdivara, Irina, Mitsuo Yamauchi, and Kenneth B. Tomer. "Molecular Characterization of Collagen Hydroxylysine O-Glycosylation by Mass Spectrometry: Current Status." Australian Journal of Chemistry 66, no. 7 (2013): 760. http://dx.doi.org/10.1071/ch13174.

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The most abundant proteins in vertebrates – the collagen family proteins – play structural and biological roles in the body. The predominant member, type I collagen, provides tissues and organs with structure and connectivity. This protein has several unique post-translational modifications that take place intra- and extra-cellularly. With growing evidence of the relevance of such post-translational modifications in health and disease, the biological significance of O-linked collagen glycosylation has recently drawn increased attention. However, several aspects of this unique modification – the requirement for prior lysyl hydroxylation as a substrate, involvement of at least two distinct glycosyl transferases, its involvement in intermolecular crosslinking – have made its molecular mapping and quantitative characterization challenging. Such characterization is obviously crucial for understanding its biological significance. Recent progress in mass spectrometry has provided an unprecedented opportunity for this type of analysis. This review summarizes recent advances in the area of O-glycosylation of fibrillar collagens and their characterization using state-of-the-art liquid chromatography–mass spectrometry-based methodologies, and perspectives on future research. The analytical characterization of collagen crosslinking and advanced glycation end-products are not addressed here.

21

HAH, Sang Soo. "Determination of Protein-Ligand Interactions Using Accelerator Mass Spectrometry: Modified Crosslinking Assay." Analytical Sciences 25, no. 5 (2009): 731–33. http://dx.doi.org/10.2116/analsci.25.731.

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22

Felker, Dana, Haoming Zhang, Zhiyuan Bo, Miranda Lau, Yoshihiro Morishima, Santiago Schnell, and Yoichi Osawa. "Mapping protein-protein interactions in homodimeric CYP102A1 by crosslinking and mass spectrometry." Biophysical Chemistry 274 (July 2021): 106590. http://dx.doi.org/10.1016/j.bpc.2021.106590.

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23

Fasci, Domenico, Hugo van Ingen, Richard A. Scheltema, and Albert J. R. Heck. "Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei." Molecular & Cellular Proteomics 17, no. 10 (July 18, 2018): 2018–33. http://dx.doi.org/10.1074/mcp.ra118.000924.

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24

Castellano, Elizabeth. "Identification of Fluoxetine-Serotonin Transporter Interactions using Crosslinking-Mass Spectrometry (CX-MS)." Biophysical Journal 112, no. 3 (February 2017): 343a. http://dx.doi.org/10.1016/j.bpj.2016.11.1861.

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25

Müller, Fränze, Andrea Graziadei, and Juri Rappsilber. "Quantitative Photo-crosslinking Mass Spectrometry Revealing Protein Structure Response to Environmental Changes." Analytical Chemistry 91, no. 14 (June 17, 2019): 9041–48. http://dx.doi.org/10.1021/acs.analchem.9b01339.

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26

Castellano, Elizabeth. "Mapping the Extracellular Loops of the Serotonin Transporter Using Crosslinking-Mass Spectrometry." Biophysical Journal 116, no. 3 (February 2019): 52a. http://dx.doi.org/10.1016/j.bpj.2018.11.327.

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27

Stevenson Keller, T. C., Brant E. Isakson, and Linda Columbus. "Molecular Modeling of the Alpha Globin/eNOS Complex via Crosslinking Mass Spectrometry." Biophysical Journal 116, no. 3 (February 2019): 168a. http://dx.doi.org/10.1016/j.bpj.2018.11.933.

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28

Nagy, Lajos, Bence Vadkerti, Csilla Lakatos, Péter Pál Fehér, Miklós Zsuga, and Sándor Kéki. "Kinetically Equivalent Functionality and Reactivity of Commonly Used Biocompatible Polyurethane Crosslinking Agents." International Journal of Molecular Sciences 22, no. 8 (April 14, 2021): 4059. http://dx.doi.org/10.3390/ijms22084059.

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In this paper, the kinetics of the reaction of phenyl isocyanate with crosslinking agents such as sucrose, sorbitol, and glycerol are reported. Crosslinking agents were used in high molar excess to isocyanate to obtain pseudo-first-order rate dependencies, and the reaction products were separated by high-performance liquid chromatography and detected by UV spectroscopy and mass spectrometry. It was found that the glycerol’s primary hydroxyl groups were approximately four times reactive than the secondary ones. However, in the case of sorbitol, the two primary OH groups were found to be the most reactive, and the reactivity of hydroxyl groups decreased in the order of kOH(6)(8.43) > kOH(1)(6.91) > kOH(5)(1.19) > kOH(2)(0.98) > kOH(3)(0.93) > kOH(4)(0.64), where the numbers in the subscript and in the brackets denote the position of OH groups and the pseudo-first-order rate constants, respectively. The Atomic Polar Tenzor (APT) charges of OH groups and dipole moments of monosubstituted sorbitol derivatives calculated by density functional theory (DFT) also confirmed the experimental results. On the other hand, the reactions of phenyl isocyanate with crosslinking agents were also performed using high excess isocyanate in order to determine the number of OH-groups participating effectively in the crosslinking process. However, due to the huge number of derivatives likely formed in these latter reactions, a simplified reaction scheme was introduced to describe the resulting product versus reaction time distributions detected by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-TOF MS). Based on the results, the kinetically equivalent functionality (fk) of each crosslinking agent was determined and found to be 2.26, 2.6, and 2.96 for glycerol, sorbitol, and sucrose, respectively.

29

Röth, Daniel, Jessica Molina-Franky, John C. Williams, and Markus Kalkum. "Mass Spectrometric Detection of Formaldehyde-Crosslinked PBMC Proteins in Cell-Free DNA Blood Collection Tubes." Molecules 28, no. 23 (November 30, 2023): 7880. http://dx.doi.org/10.3390/molecules28237880.

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Streck tubes are commonly used to collect blood samples to preserve cell-free circulating DNA. They contain imidazolidinyl urea as a formaldehyde-releasing agent to stabilize cells. We investigated whether the released formaldehyde leads to crosslinking of intracellular proteins. Therefore, we employed a shotgun proteomics experiment on human peripheral blood mononuclear cells (PBMCs) that were isolated from blood collected in Streck tubes, EDTA tubes, EDTA tubes containing formaldehyde, or EDTA tubes containing allantoin. The identified crosslinks were validated in parallel reaction monitoring LC/MS experiments. In total, we identified and validated 45 formaldehyde crosslinks in PBMCs from Streck tubes, which were also found in PBMCs from formaldehyde-treated blood, but not in EDTA- or allantoin-treated samples. Most were derived from cytoskeletal proteins and histones, indicating the ability of Streck tubes to fix cells. In addition, we confirm a previous observation that formaldehyde crosslinking of proteins induces a +24 Da mass shift more frequently than a +12 Da shift. The crosslinking capacity of Streck tubes needs to be considered when selecting blood-collection tubes for mass-spectrometry-based proteomics or metabolomic experiments.

30

Faustino, Anneliese M., and Stephen D. Fried. "Mapping Structural Intermediates during Co-Translational Folding of Hsp70 with Crosslinking Mass Spectrometry." Biophysical Journal 120, no. 3 (February 2021): 197a. http://dx.doi.org/10.1016/j.bpj.2020.11.1356.

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31

Livney, Y. D., A. L. Schwan та D. G. Dalgleish. "A Study of β-Casein Tertiary Structure by Intramolecular Crosslinking and Mass Spectrometry". Journal of Dairy Science 87, № 11 (листопад 2004): 3638–47. http://dx.doi.org/10.3168/jds.s0022-0302(04)73502-x.

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32

HAH, Sang Soo. "Retraction: Determination of Protein-Ligand Interactions Using Accelerator Mass Spectrometry: Modified Crosslinking Assay." Analytical Sciences 28, no. 8 (2012): 827. http://dx.doi.org/10.2116/analsci.28.827.

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33

Bullock, Joshua M. A., Konstantinos Thalassinos, and Maya Topf. "Jwalk and MNXL web server: model validation using restraints from crosslinking mass spectrometry." Bioinformatics 34, no. 20 (May 7, 2018): 3584–85. http://dx.doi.org/10.1093/bioinformatics/bty366.

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34

Debelyy, Mykhaylo O., Patrice Waridel, Manfredo Quadroni, Roger Schneiter, and Andreas Conzelmann. "Chemical crosslinking and mass spectrometry to elucidate the topology of integral membrane proteins." PLOS ONE 12, no. 10 (October 26, 2017): e0186840. http://dx.doi.org/10.1371/journal.pone.0186840.

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35

Fukumoto, Jutaro, Helena Hernández-Cuervo, Venkata Ramireddy Narala, Sahebgowda S. Patil, Ramani Soundararajan, Matthew Alleyn, Mason T. Breitzig, Richard F. Lockey, and Narasaiah Kolliputi. "Identification of ALDH2 Interacting Proteins by Chemical Crosslinking, Co-Immunoprecipitation and Mass Spectrometry." Journal of Allergy and Clinical Immunology 141, no. 2 (February 2018): AB176. http://dx.doi.org/10.1016/j.jaci.2017.12.559.

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36

Chavez, Juan D., Chi Fung Lee, Arianne Caudal, Andrew Keller, Rong Tian, and James E. Bruce. "Chemical Crosslinking Mass Spectrometry Analysis of Protein Conformations and Supercomplexes in Heart Tissue." Cell Systems 6, no. 1 (January 2018): 136–41. http://dx.doi.org/10.1016/j.cels.2017.10.017.

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37

Zhou, Xiangzhe, Feng Liu, Nuomin Li, and Yongqian Zhang. "Large-Scale Qualitative and Quantitative Assessment of Dityrosine Crosslinking Omics in Response to Endogenous and Exogenous Hydrogen Peroxide in Escherichia coli." Antioxidants 12, no. 4 (March 23, 2023): 786. http://dx.doi.org/10.3390/antiox12040786.

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Excessive hydrogen peroxide causes oxidative stress in cells. The oxidation of two tyrosine residues in proteins can generate o,o′-dityrosine, a putative biomarker for protein oxidation, which plays critical roles in a variety of organisms. Thus far, few studies have investigated dityrosine crosslinking under endogenous or exogenous oxidative conditions at the proteome level, and its physiological function remains largely unknown. In this study, to investigate qualitative and quantitative dityrosine crosslinking, two mutant Escherichia coli strains and one mutant strain supplemented with H2O2 were used as models for endogenous and exogenous oxidative stress, respectively. By integrating high-resolution liquid chromatography—mass spectrometry and bioinformatic analysis, we created the largest dityrosine crosslinking dataset in E. coli to date, identifying 71 dityrosine crosslinks and 410 dityrosine loop links on 352 proteins. The dityrosine-linked proteins are mainly involved in taurine and hypotaurine metabolism, citrate cycle, glyoxylate, dicarboxylate metabolism, carbon metabolism, etc., suggesting that dityrosine crosslinking may play a critical role in regulating the metabolic pathways in response to oxidative stress. In conclusion, we have reported the most comprehensive dityrosine crosslinking in E. coli for the first time, which is of great significance in revealing its function in oxidative stress.

38

Endres, Kevin J., Rodger A. Dilla, Matthew L. Becker, and Chrys Wesdemiotis. "Poly(ethylene glycol) Hydrogel Crosslinking Chemistries Identified via Atmospheric Solids Analysis Probe Mass Spectrometry." Macromolecules 54, no. 17 (August 28, 2021): 7754–64. http://dx.doi.org/10.1021/acs.macromol.1c00765.

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39

Sinz, Andrea. "Investigation of protein–protein interactions in living cells by chemical crosslinking and mass spectrometry." Analytical and Bioanalytical Chemistry 397, no. 8 (January 15, 2010): 3433–40. http://dx.doi.org/10.1007/s00216-009-3405-5.

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40

Muizebelt, W. J., J. J. Donkerbroek, M. W. F. Nielen, J. B. Hussem, M. E. F. Biemond, R. P. Klaasen, and K. H. Zabel. "Oxidative crosslinking of alkyd resins studied with mass spectrometry and NMR using model compounds." Journal of Coatings Technology 70, no. 1 (January 1998): 83–93. http://dx.doi.org/10.1007/bf02720501.

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41

Cammarata, Michael B., and Jennifer S. Brodbelt. "Characterization of Intra- and Intermolecular Protein Crosslinking by Top Down Ultraviolet Photodissociation Mass Spectrometry." ChemistrySelect 1, no. 3 (March 2016): 590–93. http://dx.doi.org/10.1002/slct.201600140.

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42

Al-Eryani, Yusra, Morten Ib Rasmussen, Sven Kjellström, Peter Højrup, Cecilia Emanuelsson, and Claes von Wachenfeldt. "Exploring structure and interactions of the bacterial adaptor protein YjbH by crosslinking mass spectrometry." Proteins: Structure, Function, and Bioinformatics 84, no. 9 (June 15, 2016): 1234–45. http://dx.doi.org/10.1002/prot.25072.

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43

Faustino, Anneliese M., and Stephen D. Fried. "Progress toward proteome-wide photo-crosslinking mass spectrometry to interrogate protein networks in vivo." Biophysical Journal 123, no. 3 (February 2024): 347a—348a. http://dx.doi.org/10.1016/j.bpj.2023.11.2112.

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44

van Ooli, W. J., and M. Nahmias. "Surface Characterization of Rubber by Secondary Ion Mass Spectrometry." Rubber Chemistry and Technology 62, no. 4 (September 1, 1989): 656–82. http://dx.doi.org/10.5254/1.3536267.

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Abstract It has been demonstrated that static SIMS is potentially a very useful technique for the characterization of rubber surfaces. Its major capability is to provide molecular structural information of the polymer in addition to elemental analysis, which would also be possible with other surface techniques such as XPS or AES. The SIMS spectra are in many cases highly characteristic, and they can be used to identify the type and structure of the hydrocarbon polymer. In addition, structural changes in the rubber surface can be detected, and very useful information on the types and amounts of sulfur crosslinks can be obtained as well, as has been published elsewhere. Therefore, the technique shows great promise as a tool for the study of surface-related rubber phenomena, such as oxidation, wear, tack, antiozonant and antioxidant performance and mechanisms, and also for the study of the adhesion between dissimilar rubbers or between rubbers and other materials, such as metals. Before SIMS can be routinely used in rubber laboratories, a considerable amount of basic and fundamental work will have to be done because the spectra of many materials are not known, and they cannot always be predicted either. Therefore, a rubber-related data base will have to be built up with well-characterized polymers but also using clean films of various rubber additives. Crosslinking studies will have to be confirmed with compounds of known crosslink structures, e.g., by using different polymers, different types of accelerators, and a series of model compounds of organic sulfides.

45

Argo, Andrew S., Chunxiao Shi, Fan Liu, and Michael B. Goshe. "Performing protein crosslinking using gas-phase cleavable chemical crosslinkers and liquid chromatography-tandem mass spectrometry." Methods 89 (November 2015): 64–73. http://dx.doi.org/10.1016/j.ymeth.2015.06.011.

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46

Ferraro, Nicholas A., and Michael Cascio. "Differential State-Dependent Crosslinking of Azi-Cholesterol with Human A1 Glycine Receptor using Mass Spectrometry." Biophysical Journal 116, no. 3 (February 2019): 223a. http://dx.doi.org/10.1016/j.bpj.2018.11.1227.

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47

Tomcho, Kayce A., Hannah E. Gering, Rathna J. Veeramachaneni, David J. Lapinsky, and Michael Cascio. "Targeted State Dependent Crosslinking Mass Spectrometry (CXMS) of the Human Alpha 1 Glycine Receptor (GLyR)." Biophysical Journal 116, no. 3 (February 2019): 392a. http://dx.doi.org/10.1016/j.bpj.2018.11.2120.

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48

Armony, Gad, Albert J. R. Heck, and Wei Wu. "Extracellular crosslinking mass spectrometry reveals HLA class I – HLA class II interactions on the cell surface." Molecular Immunology 136 (August 2021): 16–25. http://dx.doi.org/10.1016/j.molimm.2021.05.010.

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49

Davydov, Dmitri R., Bikash Dangi, Guihua Yue, Deepak S. Ahire, Bhagwat Prasad, and Victor G. Zgoda. "Exploring the Interactome of Cytochrome P450 2E1 in Human Liver Microsomes with Chemical Crosslinking Mass Spectrometry." Biomolecules 12, no. 2 (January 22, 2022): 185. http://dx.doi.org/10.3390/biom12020185.

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Aiming to elucidate the system-wide effects of the alcohol-induced increase in the content of cytochrome P450 2E1 (CYP2E1) on drug metabolism, we explored the array of its protein-protein interactions (interactome) in human liver microsomes (HLM) with chemical crosslinking mass spectrometry (CXMS). Our strategy employs membrane incorporation of purified CYP2E1 modified with photoreactive crosslinkers benzophenone-4-maleimide and 4-(N-succinimidylcarboxy)benzophenone. Exposure of bait-incorporated HLM samples to light was followed by isolating the His-tagged bait protein and its crosslinked aggregates on Ni-NTA agarose. Analyzing the individual bands of SDS-PAGE slabs of thereby isolated protein with the toolset of untargeted proteomics, we detected the crosslinked dimeric and trimeric complexes of CYP2E1 with other drug-metabolizing enzymes. Among the most extensively crosslinked partners of CYP2E1 are the cytochromes P450 2A6, 2C8, 3A4, 4A11, and 4F2, UDP-glucuronosyltransferases (UGTs) 1A and 2B, fatty aldehyde dehydrogenase (ALDH3A2), epoxide hydrolase 1 (EPHX1), disulfide oxidase 1α (ERO1L), and ribophorin II (RPN2). These results demonstrate the exploratory power of the proposed CXMS strategy and corroborate the concept of tight functional integration in the human drug-metabolizing ensemble through protein-protein interactions of the constituting enzymes.

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Leitner, Alexander, Marco Faini, Florian Stengel, and Ruedi Aebersold. "Crosslinking and Mass Spectrometry: An Integrated Technology to Understand the Structure and Function of Molecular Machines." Trends in Biochemical Sciences 41, no. 1 (January 2016): 20–32. http://dx.doi.org/10.1016/j.tibs.2015.10.008.

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