Skip to main content
SpringerLink
Log in

A Mass Spectrometry View of Stable and Transient Protein Interactions

  • Chapter
  • First Online:
Advancements of Mass Spectrometry in Biomedical Research

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 806))

Abstract

Through an impressive range of dynamic interactions, proteins succeed to carry out the majority of functions in a cell. These temporally and spatially regulated interactions provide the means through which one single protein can perform diverse functions and modulate different cellular pathways. Understanding the identity and nature of these interactions is therefore critical for defining protein functions and their contribution to health and disease processes. Here, we provide an overview of workflows that incorporate immunoaffinity purifications and quantitative mass spectrometry (frequently abbreviated as IP-MS or AP-MS) for characterizing protein–protein interactions. We discuss experimental aspects that should be considered when optimizing the isolation of a protein complex. As the presence of nonspecific associations is a concern in these experiments, we discuss the common sources of nonspecific interactions and present label-free and metabolic labeling mass spectrometry-based methods that can help determine the specificity of interactions. The effective regulation of cellular pathways and the rapid reaction to various environmental stresses rely on the formation of stable, transient, and fast-exchanging protein–protein interactions. While determining the exact nature of an interaction remains challenging, we review cross-linking and metabolic labeling approaches that can help address this important aspect of characterizing protein interactions and macromolecular assemblies.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 109.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 139.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Greco TM et al (2011) Nuclear import of histone deacetylase 5 by requisite nuclear localization signal phosphorylation. Mol Cell Proteomics 10(2):M110 004317

    Google Scholar 

  2. Joshi P et al (2013) The functional interactome landscape of the human histone deacetylase family. Mol Syst Biol 9:672

    Google Scholar 

  3. Malovannaya A et al (2011) Analysis of the human endogenous coregulator complexome. Cell 145(5):787–799

    CAS  Google Scholar 

  4. Tsai YC et al (2012) Functional proteomics establishes the interaction of SIRT7 with chromatin remodeling complexes and expands its role in regulation of RNA polymerase I transcription. Mol Cell Proteomics 11(5):60–76

    CAS  Google Scholar 

  5. Li T et al (2012) Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16. Proc Natl Acad Sci U S A 109(26):10558–10563

    CAS  Google Scholar 

  6. Miteva YV, Cristea IM (2014) A proteomic perspective of SIRT6 phosphorylation and interactions, and their dependence on its catalytic activity. Mol Cell Proteomics 13(1):168–183

    CAS  Google Scholar 

  7. Adam GC, Sorensen EJ, Cravatt BF (2002) Chemical strategies for functional proteomics. Mol Cell Proteomics 1(10):781–790

    CAS  Google Scholar 

  8. Salisbury CM, Cravatt BF (2007) Activity-based probes for proteomic profiling of histone deacetylase complexes. Proc Natl Acad Sci U S A 104(4):1171–1176

    CAS  Google Scholar 

  9. Bantscheff M et al (2011) Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes. Nat Biotechnol 29(3):255–265

    CAS  Google Scholar 

  10. Cen Y et al (2011) Mechanism-based affinity capture of sirtuins. Org Biomol Chem 9(4):987–993

    CAS  Google Scholar 

  11. Ruigrok VJ et al (2011) Alternative affinity tools: more attractive than antibodies? Biochem J 436(1):1–13

    CAS  Google Scholar 

  12. Gronwall C, Stahl S (2009) Engineered affinity proteins—generation and applications. J Biotechnol 140(3–4):254–269

    Google Scholar 

  13. Brody E et al (2012) Life’s simple measures: unlocking the proteome. J Mol Biol 422(5):595–606

    CAS  Google Scholar 

  14. Wiens M et al (2011) Isolation of the silicatein-alpha interactor silintaphin-2 by a novel solid-phase pull-down assay. Biochemistry 50(12):1981–1990

    CAS  Google Scholar 

  15. Hubner NC, Mann M (2011) Extracting gene function from protein-protein interactions using Quantitative BAC InteraCtomics (QUBIC). Methods 53(4):453–459

    CAS  Google Scholar 

  16. Cristea IM et al (2005) Fluorescent proteins as proteomic probes. Mol Cell Proteomics 4(12):1933–1941

    CAS  Google Scholar 

  17. Cristea IM et al (2006) Tracking and elucidating alphavirus-host protein interactions. J Biol Chem 281(40):30269–30278

    CAS  Google Scholar 

  18. Li T, Chen J, Cristea IM (2013) Human cytomegalovirus tegument protein pUL83 inhibits IFI16-mediated DNA sensing for immune evasion. Cell Host Microbe 14(5):591–599

    CAS  Google Scholar 

  19. Li Y (2010) Commonly used tag combinations for tandem affinity purification. Biotechnol Appl Biochem 55(2):73–83

    CAS  Google Scholar 

  20. Gavin AC, Maeda K, Kuhner S (2011) Recent advances in charting protein-protein interaction: mass spectrometry-based approaches. Curr Opin Biotechnol 22(1):42–49

    CAS  Google Scholar 

  21. Rees JS et al (2011) In vivo analysis of proteomes and interactomes using parallel affinity capture (iPAC) coupled to mass spectrometry. Mol Cell Proteomics 10(6):M110 002386

    Google Scholar 

  22. Maine GN et al (2009) Bimolecular affinity purification (BAP): tandem affinity purification using two protein baits. Cold Spring Harb Protoc 2009(11):pdb prot5318

    Google Scholar 

  23. Ayyar BV et al (2012) Affinity chromatography as a tool for antibody purification. Methods 56(2):116–129

    CAS  Google Scholar 

  24. Trinkle-Mulcahy L et al (2008) Identifying specific protein interaction partners using quantitative mass spectrometry and bead proteomes. J Cell Biol 183(2):223–239

    CAS  Google Scholar 

  25. Archambault V et al (2003) Genetic and biochemical evaluation of the importance of Cdc6 in regulating mitotic exit. Mol Biol Cell 14(11):4592–4604

    CAS  Google Scholar 

  26. Cristea IM, Chait BT (2011) Affinity purification of protein complexes. Cold Spring Harb Protoc 2011(5):pdb prot5611

    Google Scholar 

  27. Miteva YV, Budayeva HG, Cristea IM (2013) Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions. Anal Chem 85(2):749–768

    CAS  Google Scholar 

  28. Conlon FL et al (2012) Immunoisolation of protein complexes from Xenopus. Methods Mol Biol 917:369–390

    CAS  Google Scholar 

  29. Cadene M, Chait BT (2000) A robust, detergent-friendly method for mass spectrometric analysis of integral membrane proteins. Anal Chem 72(22):5655–5658

    CAS  Google Scholar 

  30. Norris JL, Porter NA, Caprioli RM (2003) Mass spectrometry of intracellular and membrane proteins using cleavable detergents. Anal Chem 75(23):6642–6647

    CAS  Google Scholar 

  31. Ye X et al (2009) Optimization of protein solubilization for the analysis of the CD14 human monocyte membrane proteome using LC-MS/MS. J Proteomics 73(1):112–122

    CAS  Google Scholar 

  32. Wisniewski JR et al (2009) Universal sample preparation method for proteome analysis. Nat Methods 6(5):359–362

    CAS  Google Scholar 

  33. Darie CC et al (2011) Identifying transient protein-protein interactions in EphB2 signaling by blue native PAGE and mass spectrometry. Proteomics 11(23):4514–4528

    CAS  Google Scholar 

  34. Dubois F et al (2009) Differential 14-3-3 affinity capture reveals new downstream targets of phosphatidylinositol 3-kinase signaling. Mol Cell Proteomics 8(11):2487–2499

    CAS  Google Scholar 

  35. Chait BT (2011) Mass spectrometry in the postgenomic era. Annu Rev Biochem 80:239–246

    CAS  Google Scholar 

  36. Tipton JD et al (2011) Analysis of intact protein isoforms by mass spectrometry. J Biol Chem 286(29):25451–25458

    CAS  Google Scholar 

  37. Aebersold R, Mann M (2003) Mass spectrometry-based proteomics. Nature 422(6928):198–207

    CAS  Google Scholar 

  38. Yates JR, Ruse CI, Nakorchevsky A (2009) Proteomics by mass spectrometry: approaches, advances, and applications. Annu Rev Biomed Eng 11:49–79

    CAS  Google Scholar 

  39. Picotti P, Aebersold R (2012) Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions. Nat Methods 9(6):555–566

    CAS  Google Scholar 

  40. Mellacheruvu D et al (2013) The CRAPome: a contaminant repository for affinity purification-mass spectrometry data. Nat Methods 10(8):730–736

    CAS  Google Scholar 

  41. Alber F et al (2007) Determining the architectures of macromolecular assemblies. Nature 450(7170):683–694

    CAS  Google Scholar 

  42. Selimi F et al (2009) Proteomic studies of a single CNS synapse type: the parallel fiber/purkinje cell synapse. PLoS Biol 7(4):e83

    Google Scholar 

  43. Hendrick JP, Hartl FU (1993) Molecular chaperone functions of heat-shock proteins. Annu Rev Biochem 62:349–384

    CAS  Google Scholar 

  44. Bard-Chapeau EA et al (2013) EVI1 oncoprotein interacts with a large and complex network of proteins and integrates signals through protein phosphorylation. Proc Natl Acad Sci U S A 110(31):E2885–E2894

    CAS  Google Scholar 

  45. Gavin AC et al (2006) Proteome survey reveals modularity of the yeast cell machinery. Nature 440(7084):631–636

    CAS  Google Scholar 

  46. Krogan NJ et al (2006) Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440(7084):637–643

    CAS  Google Scholar 

  47. Collins SR et al (2007) Toward a comprehensive atlas of the physical interactome of Saccharomyces cerevisiae. Mol Cell Proteomics 6(3):439–450

    CAS  Google Scholar 

  48. Babu M et al (2012) Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae. Nature 489(7417):585–589

    CAS  Google Scholar 

  49. Jeronimo C et al (2007) Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme. Mol Cell 27(2):262–274

    CAS  Google Scholar 

  50. Sardiu ME et al (2008) Probabilistic assembly of human protein interaction networks from label-free quantitative proteomics. Proc Natl Acad Sci U S A 105(5):1454–1459

    CAS  Google Scholar 

  51. Sowa ME et al (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138(2):389–403

    CAS  Google Scholar 

  52. Choi H et al (2011) SAINT: probabilistic scoring of affinity purification-mass spectrometry data. Nat Methods 8(1):70–73

    CAS  Google Scholar 

  53. Paoletti AC et al (2006) Quantitative proteomic analysis of distinct mammalian mediator complexes using normalized spectral abundance factors. Proc Natl Acad Sci U S A 103(50): 18928–18933

    CAS  Google Scholar 

  54. Wang M et al (2012) PaxDb, a database of protein abundance averages across all three domains of life. Mol Cell Proteomics 11(8):492–500

    CAS  Google Scholar 

  55. Glatter T et al (2011) Modularity and hormone sensitivity of the Drosophila melanogaster insulin receptor/target of rapamycin interaction proteome. Mol Syst Biol 7:547

    Google Scholar 

  56. Rinner O et al (2007) An integrated mass spectrometric and computational framework for the analysis of protein interaction networks. Nat Biotechnol 25(3):345–352

    CAS  Google Scholar 

  57. Jager S et al (2012) Global landscape of HIV-human protein complexes. Nature 481(7381): 365–370

    Google Scholar 

  58. Oda Y et al (1999) Accurate quantitation of protein expression and site-specific phosphorylation. Proc Natl Acad Sci U S A 96(12):6591–6596

    CAS  Google Scholar 

  59. Ong SE et al (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1(5):376–386

    CAS  Google Scholar 

  60. Tackett AJ et al (2005) I-DIRT, a general method for distinguishing between specific and nonspecific protein interactions. J Proteome Res 4(5):1752–1756

    CAS  Google Scholar 

  61. Selbach M, Mann M (2006) Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK). Nat Methods 3(12):981–983

    CAS  Google Scholar 

  62. Ge F et al (2010) Identification of novel 14-3-3zeta interacting proteins by quantitative immunoprecipitation combined with knockdown (QUICK). J Proteome Res 9(11): 5848–5858

    CAS  Google Scholar 

  63. Meixner A et al (2011) A QUICK screen for Lrrk2 interaction partners—leucine-rich repeat kinase 2 is involved in actin cytoskeleton dynamics. Mol Cell Proteomics 10(1):M110 001172

    Google Scholar 

  64. Zheng P et al (2012) QUICK identification and SPR validation of signal transducers and activators of transcription 3 (Stat3) interacting proteins. J Proteomics 75(3):1055–1066

    CAS  Google Scholar 

  65. Heide H et al (2009) Application of quantitative immunoprecipitation combined with knockdown and cross-linking to Chlamydomonas reveals the presence of vesicle-inducing protein in plastids 1 in a common complex with chloroplast HSP90C. Proteomics 9(11):3079–3089

    CAS  Google Scholar 

  66. Schmollinger S et al (2012) A protocol for the identification of protein-protein interactions based on 15 N metabolic labeling, immunoprecipitation, quantitative mass spectrometry and affinity modulation. J Vis Exp 67(2):4083

    Google Scholar 

  67. Wang X, Huang L (2008) Identifying dynamic interactors of protein complexes by quantitative mass spectrometry. Mol Cell Proteomics 7(1):46–57

    Google Scholar 

  68. Fang L et al (2008) Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. J Proteome Res 7(11):4914–4925

    CAS  Google Scholar 

  69. Zhang XX et al (2012) Nanodiscs and SILAC-based mass spectrometry to identify a membrane protein interactome. J Proteome Res 11(2):1454–1459

    Google Scholar 

  70. Gunaratne J et al (2011) Protein interactions of phosphatase and tensin homologue (PTEN) and its cancer-associated G20E mutant compared by using stable isotope labeling by amino acids in cell culture-based parallel affinity purification. J Biol Chem 286(20):18093–18103

    CAS  Google Scholar 

  71. Gygi SP et al (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17(10):994–999

    CAS  Google Scholar 

  72. Ranish JA, Brand M, Aebersold R (2007) Using stable isotope tagging and mass spectrometry to characterize protein complexes and to detect changes in their composition. Methods Mol Biol 359:17–35

    CAS  Google Scholar 

  73. Ross PL et al (2004) Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics 3(12):1154–1169

    CAS  Google Scholar 

  74. Zieske LR (2006) A perspective on the use of iTRAQ reagent technology for protein complex and profiling studies. J Exp Bot 57(7):1501–1508

    CAS  Google Scholar 

  75. Vogt A et al (2013) Isotope coded protein labeling coupled immunoprecipitation (ICPL-IP): a novel approach for quantitative protein complex analysis from native tissue. Mol Cell Proteomics 12(5):1395–1406

    CAS  Google Scholar 

  76. Chen ZA et al (2010) Architecture of the RNA polymerase II-TFIIF complex revealed by cross-linking and mass spectrometry. EMBO J 29(4):717–726

    CAS  Google Scholar 

  77. Sharon M et al (2006) Structural organization of the 19S proteasome lid: insights from MS of intact complexes. PLoS Biol 4(8):e267

    Google Scholar 

  78. Fu CY et al (2010) A docking model based on mass spectrometric and biochemical data describes phage packaging motor incorporation. Mol Cell Proteomics 9(8):1764–1773

    CAS  Google Scholar 

  79. Herzog F et al (2012) Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry. Science 337(6100):1348–1352

    CAS  Google Scholar 

  80. Leitner A et al (2012) The molecular architecture of the eukaryotic chaperonin TRiC/CCT. Structure 20(5):814–825

    CAS  Google Scholar 

  81. Lanman J et al (2003) Identification of novel interactions in HIV-1 capsid protein assembly by high-resolution mass spectrometry. J Mol Biol 325(4):759–772

    CAS  Google Scholar 

  82. Rozbesky D et al (2013) Structural model of lymphocyte receptor NKR-P1C revealed by mass spectrometry and molecular modeling. Anal Chem 85(3):1597–1604

    CAS  Google Scholar 

  83. Zelter A et al (2010) Isotope signatures allow identification of chemically cross-linked peptides by mass spectrometry: a novel method to determine inter-residue distances in protein structures through cross-linking. J Proteome Res 9(7):3583–3589

    CAS  Google Scholar 

  84. Paramelle D et al (2013) Chemical cross-linkers for protein structure studies by mass spectrometry. Proteomics 13(3–4):438–456

    CAS  Google Scholar 

  85. Chowdhury SM et al (2009) Identification of cross-linked peptides after click-based enrichment using sequential collision-induced dissociation and electron transfer dissociation tandem mass spectrometry. Anal Chem 81(13):5524–5532

    CAS  Google Scholar 

  86. Kao A et al (2011) Development of a novel cross-linking strategy for fast and accurate identification of cross-linked peptides of protein complexes. Mol Cell Proteomics 10(1):M110 002212

    Google Scholar 

  87. Rinner O et al (2008) Identification of cross-linked peptides from large sequence databases. Nat Methods 5(4):315–318

    CAS  Google Scholar 

  88. Tosi A et al (2013) Structure and subunit topology of the INO80 chromatin remodeler and its nucleosome complex. Cell 154(6):1207–1219

    CAS  Google Scholar 

  89. Jennebach S et al (2012) Crosslinking-MS analysis reveals RNA polymerase I domain architecture and basis of rRNA cleavage. Nucleic Acids Res 40(12):5591–5601

    CAS  Google Scholar 

  90. Hernandez P et al (2003) Popitam: towards new heuristic strategies to improve protein identification from tandem mass spectrometry data. Proteomics 3(6):870–878

    CAS  Google Scholar 

  91. Singh P et al (2008) Characterization of protein cross-links via mass spectrometry and an open-modification search strategy. Anal Chem 80(22):8799–8806

    CAS  Google Scholar 

  92. Eng JK, McCormack AL, Yates JR (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5(11):976–989

    CAS  Google Scholar 

  93. McIlwain S et al (2010) Detecting cross-linked peptides by searching against a database of cross-linked peptide pairs. J Proteome Res 9(5):2488–2495

    CAS  Google Scholar 

  94. Walzthoeni T et al (2012) False discovery rate estimation for cross-linked peptides identified by mass spectrometry. Nat Methods 9(9):901–903

    CAS  Google Scholar 

  95. Panchaud A et al (2010) xComb: a cross-linked peptide database approach to protein-protein interaction analysis. J Proteome Res 9(5):2508–2515

    CAS  Google Scholar 

  96. Maiolica A et al (2007) Structural analysis of multiprotein complexes by cross-linking, mass spectrometry, and database searching. Mol Cell Proteomics 6(12):2200–2211

    CAS  Google Scholar 

  97. Chu F et al (2010) Finding chimeras: a bioinformatics strategy for identification of cross-linked peptides. Mol Cell Proteomics 9(1):25–31

    CAS  Google Scholar 

  98. Lee YJ et al (2007) Shotgun cross-linking analysis for studying quaternary and tertiary protein structures. J Proteome Res 6(10):3908–3917

    CAS  Google Scholar 

  99. Nadeau OW et al (2008) CrossSearch, a user-friendly search engine for detecting chemically cross-linked peptides in conjugated proteins. Mol Cell Proteomics 7(4):739–749

    CAS  Google Scholar 

  100. Yang B et al (2012) Identification of cross-linked peptides from complex samples. Nat Methods 9(9):904–906

    CAS  Google Scholar 

  101. Braun P (2012) Interactome mapping for analysis of complex phenotypes: insights from benchmarking binary interaction assays. Proteomics 12(10):1499–1518

    CAS  Google Scholar 

  102. Kaake RM, Wang X, Huang L (2010) Profiling of protein interaction networks of protein complexes using affinity purification and quantitative mass spectrometry. Mol Cell Proteomics 9(8):1650–1665

    CAS  Google Scholar 

  103. Tagwerker C et al (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivo cross-linking. Mol Cell Proteomics 5(4):737–748

    CAS  Google Scholar 

  104. Guerrero C et al (2006) An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network. Mol Cell Proteomics 5(2):366–378

    CAS  Google Scholar 

  105. Suchanek M, Radzikowska A, Thiele C (2005) Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells. Nat Methods 2(4):261–267

    CAS  Google Scholar 

  106. Glembotski CC et al (2012) Mesencephalic astrocyte-derived neurotrophic factor protects the heart from ischemic damage and is selectively secreted upon sarco/endoplasmic reticulum calcium depletion. J Biol Chem 287(31):25893–25904

    CAS  Google Scholar 

  107. Muller VS et al (2011) Membrane-SPINE: an improved method to identify protein-protein interaction partners of membrane proteins in vivo. Proteomics 11(10):2124–2128

    Google Scholar 

  108. Smith AL et al (2012) Association of Rho-associated protein kinase 1 with E-cadherin complexes is mediated by p120-catenin. Mol Biol Cell 23(1):99–110

    CAS  Google Scholar 

  109. Smith AL et al (2011) ReCLIP (reversible cross-link immuno-precipitation): an efficient method for interrogation of labile protein complexes. PLoS One 6(1):e16206

    CAS  Google Scholar 

  110. Smart SK et al (2009) Mapping the local protein interactome of the NuA3 histone acetyltransferase. Protein Sci 18(9):1987–1997

    CAS  Google Scholar 

  111. Byrum S et al (2012) Analysis of stable and transient protein-protein interactions. Methods Mol Biol 833:143–152

    CAS  Google Scholar 

  112. Tang X, Bruce JE (2010) A new cross-linking strategy: protein interaction reporter (PIR) technology for protein-protein interaction studies. Mol Biosyst 6(6):939–947

    CAS  Google Scholar 

  113. Chavez JD et al (2012) Cross-linking measurements of the Potato leafroll virus reveal protein interaction topologies required for virion stability, aphid transmission, and virus-plant interactions. J Proteome Res 11(5):2968–2981

    CAS  Google Scholar 

  114. Zheng C et al (2011) Cross-linking measurements of in vivo protein complex topologies. Mol Cell Proteomics 10(10):M110 006841

    Google Scholar 

  115. Zhang H et al (2009) Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry. Mol Cell Proteomics 8(3):409–420

    CAS  Google Scholar 

  116. Schmitt-Ulms G et al (2004) Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues. Nat Biotechnol 22(6):724–731

    CAS  Google Scholar 

  117. Bai Y et al (2008) The in vivo brain interactome of the amyloid precursor protein. Mol Cell Proteomics 7(1):15–34

    CAS  Google Scholar 

  118. Watts JC et al (2009) Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones. PLoS Pathog 5(10):e1000608

    Google Scholar 

  119. Knobbe CB et al (2011) Choice of biological source material supersedes oxidative stress in its influence on DJ-1 in vivo interactions with Hsp90. J Proteome Res 10(10):4388–4404

    CAS  Google Scholar 

Download references

Acknowledgments

We are grateful for funding from NIH grants DP1DA026192, R21AI102187, and R21 HD073044-01A1, an HFSPO award RGY0079/2009-C to IMC, and an NSF graduate fellowship to HGB.

Author information

Authors and Affiliations

  1. Department of Molecular Biology, 210 Lewis Thomas Laboratory, Princeton University, Princeton, NJ, 08544, USA

    Hanna G. Budayeva & Ileana M. Cristea

Authors
  1. Hanna G. Budayeva
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ileana M. Cristea
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Ileana M. Cristea .

Editor information

Editors and Affiliations

  1. Chemistry and Biomolecular Science Biochemistry and Proteomics Group, Clarkson University, Potsdam, New York, USA

    Alisa G. Woods

  2. Chemistry and Biomolecular Science Biochemistry and Proteomics Group, Clarkson University, Potsdam, New York, USA

    Costel C. Darie

Rights and permissions

Reprints and permissions

Copyright information

© 2014 Springer International Publishing Switzerland

About this chapter

Cite this chapter

Budayeva, H.G., Cristea, I.M. (2014). A Mass Spectrometry View of Stable and Transient Protein Interactions. In: Woods, A., Darie, C. (eds) Advancements of Mass Spectrometry in Biomedical Research. Advances in Experimental Medicine and Biology, vol 806. Springer, Cham. https://doi.org/10.1007/978-3-319-06068-2_11

Download citation

Publish with us

Policies and ethics

Search

Navigation