The role of structural disorder in cell cycle regulation, related clinical proteomics, disease development and drug targeting

References

• Wright PE, Dyson HJ. Intrinsically disordered proteins in cellular signalling and regulation. Nat Rev Mol Cell Biol 2015;16:18-29
   PubMed Web of Science ®Google Scholar
• Yoon MK, Mitrea DM, Ou L, Kriwacki RW. Cell cycle regulation by the intrinsically disordered proteins p21 and p27. Biochem Soc Trans 2012;40:981-8
   PubMed Web of Science ®Google Scholar
• Habchi J, Tompa P, Longhi S, Uversky VN. Introducing protein intrinsic disorder. Chem Rev 2014;114:6561-88
   PubMed Web of Science ®Google Scholar
• van der Lee R, Buljan M, Lang B, et al. Classification of intrinsically disordered regions and proteins. Chem Rev 2014;114:6589-631
   PubMed Web of Science ®Google Scholar
• Iakoucheva LM, Brown CJ, Lawson JD, et al. Intrinsic disorder in cell-signaling and cancer-associated proteins. J Mol Biol 2002;323:573-84
   PubMed Web of Science ®Google Scholar
• Tompa P. Unstructural biology coming of age. Curr Opin Struct Biol 2011;21:419-25
   PubMed Web of Science ®Google Scholar
• Funk JO. Cell Cycle Checkpoint Genes and Cancer. Encyclopedia of life sciences 2005
   Google Scholar
• Resnitzky D, Hengst L, Reed SI. Cyclin A-associated kinase activity is rate limiting for entrance into S phase and is negatively regulated in G1 by p27Kip1. Mol Cell Biol 1995;15:4347-52
   PubMedGoogle Scholar
• Lukas J, Herzinger T, Hansen K, et al. Cyclin E-induced S phase without activation of the pRb/E2F pathway. Genes Dev 1997;11:1479-92
   PubMed Web of Science ®Google Scholar
• Weber HO, Samuel T, Rauch P, Funk JO. Human p14(ARF)-mediated cell cycle arrest strictly depends on intact p53 signaling pathways. Oncogene 2002;21:3207-12
   PubMed Web of Science ®Google Scholar
• Chan TA, Hermeking H, Lengauer C, et al. 14-3-3Sigma is required to prevent mitotic catastrophe after DNA damage. Nature 1999;401:616-20
   PubMed Web of Science ®Google Scholar
• Vermeulen K, Van Bockstaele DR, Berneman ZN. The cell cycle: a review of regulation, deregulation and therapeutic targets in cancer. Cell Prolif 2003;36:131-49
   PubMed Web of Science ®Google Scholar
• Willis N, Rhind N. Regulation of DNA replication by the S-phase DNA damage checkpoint. Cell Div 2009;4:13
   PubMed Web of Science ®Google Scholar
• Falck J, Mailand N, Syljuasen RG, et al. The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis. Nature 2001;410:842-7
   PubMed Web of Science ®Google Scholar
• Mailand N, Falck J, Lukas C, et al. Rapid destruction of human Cdc25A in response to DNA damage. Science 2000;288:1425-9
   PubMed Web of Science ®Google Scholar
• Sorensen CS, Syljuasen RG. Safeguarding genome integrity: the checkpoint kinases ATR, CHK1 and WEE1 restrain CDK activity during normal DNA replication. Nucleic Acids Res 2012;40:477-86
   PubMed Web of Science ®Google Scholar
• Unsal-Kacmaz K, Chastain PD, Qu PP, et al. The human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacement. Mol Cell Biol 2007;27:3131-42
   PubMed Web of Science ®Google Scholar
• de Klein A, Muijtjens M, van Os R, et al. Targeted disruption of the cell-cycle checkpoint gene ATR leads to early embryonic lethality in mice. Curr Biol 2000;10:479-82
   PubMed Web of Science ®Google Scholar
• Tominaga Y, Li C, Wang RH, Deng CX. Murine Wee1 plays a critical role in cell cycle regulation and pre-implantation stages of embryonic development. Int J Biol Sci 2006;2:161-70
   PubMed Web of Science ®Google Scholar
• Lee S, Bolanos-Garcia VM. The dynamics of signal amplification by macromolecular assemblies for the control of chromosome segregation. Front Physiol 2014;5:368
   PubMed Web of Science ®Google Scholar
• Tompa P, Varadi M. Predicting the predictive power of IDP ensembles. Structure 2014;22:177-8
   PubMed Web of Science ®Google Scholar
• Varadi M, Kosol S, Lebrun P, et al. pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins. Nucleic Acids Res 2014;42:D326-35
   PubMed Web of Science ®Google Scholar
• Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 2005;579:3346-54
   PubMed Web of Science ®Google Scholar
• Besson A, Dowdy SF, Roberts JM. CDK inhibitors: cell cycle regulators and beyond. Dev Cell 2008;14:159-69
   PubMed Web of Science ®Google Scholar
• Cheng M, Olivier P, Diehl JA, et al. The p21(Cip1) and p27(Kip1) CDK ‘inhibitors’ are essential activators of cyclin D-dependent kinases in murine fibroblasts. EMBO J 1999;18:1571-83
   PubMed Web of Science ®Google Scholar
• LaBaer J, Garrett MD, Stevenson LF, et al. New functional activities for the p21 family of CDK inhibitors. Genes Dev 1997;11:847-62
   PubMed Web of Science ®Google Scholar
• Wang Y, Fisher JC, Mathew R, et al. Intrinsic disorder mediates the diverse regulatory functions of the Cdk inhibitor p21. Nat Chem Biol 2011;7:214-21
   PubMed Web of Science ®Google Scholar
• Lacy ER, Wang Y, Post J, et al. Molecular basis for the specificity of p27 toward cyclin-dependent kinases that regulate cell division. J Mol Biol 2005;349:764-73
   PubMedGoogle Scholar
• Shoemaker BA, Portman JJ, Wolynes PG. Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc Natl Acad Sci USA 2000;97:8868-73
   PubMed Web of Science ®Google Scholar
• Quelle DE, Zindy F, Ashmun RA, Sherr CJ. Alternative reading frames of the INK4a tumor suppressor gene encode two unrelated proteins capable of inducing cell cycle arrest. Cell 1995;83:993-1000
   PubMed Web of Science ®Google Scholar
• Bothner B, Lewis WS, DiGiammarino EL, et al. Defining the molecular basis of Arf and Hdm2 interactions. J Mol Biol 2001;314:263-77
   PubMedGoogle Scholar
• Bates S, Phillips AC, Clark PA, et al. p14ARF links the tumour suppressors RB and p53. Nature 1998;395:124-5
   PubMed Web of Science ®Google Scholar
• Zindy F, Eischen CM, Randle DH, et al. Myc signaling via the ARF tumor suppressor regulates p53-dependent apoptosis and immortalization. Genes Dev 1998;12:2424-33
   PubMed Web of Science ®Google Scholar
• Saha T, Kar R K, Sa G. Structural and sequential context of p53: A review of experimental and theoretical evidence. Prog Biophys Mol Biol 2015. [Epub ahead of print]
   PubMed Web of Science ®Google Scholar
• Dawson R, Muller L, Dehner A, et al. The N-terminal domain of p53 is natively unfolded. J Mol Biol 2003;332:1131-41
   Google Scholar
• Kussie PH, Gorina S, Marechal V, et al. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 1996;274:948-53
   PubMed Web of Science ®Google Scholar
• Lukman S, Lane DP, Verma CS. Mapping the structural and dynamical features of multiple p53 DNA binding domains: insights into loop 1 intrinsic dynamics. PLoS One 2013;8:e80221
   Web of Science ®Google Scholar
• Hegyi H, Schad E, Tompa P. Structural disorder promotes assembly of protein complexes. BMC Struct Biol 2007;7:65
   PubMed Web of Science ®Google Scholar
• Ghongane P, Kapanidou M, Asghar A, et al. The dynamic protein Knl1 - a kinetochore rendezvous. J Cell Sci 2014;127:3415-23
   PubMed Web of Science ®Google Scholar
• Caldas GV, DeLuca KF, DeLuca JG. KNL1 facilitates phosphorylation of outer kinetochore proteins by promoting Aurora B kinase activity. J Cell Biol 2013;203:957-69
   PubMed Web of Science ®Google Scholar
• Kiyomitsu T, Obuse C, Yanagida M. Human Blinkin/AF15q14 is required for chromosome alignment and the mitotic checkpoint through direct interaction with Bub1 and BubR1. Dev Cell 2007;13:663-76
   PubMed Web of Science ®Google Scholar
• Petrovic A, Pasqualato S, Dube P, et al. The MIS12 complex is a protein interaction hub for outer kinetochore assembly. J Cell Biol 2010;190:835-52
   PubMed Web of Science ®Google Scholar
• Kops GJ, Kim Y, Weaver BA, et al. ZW10 links mitotic checkpoint signaling to the structural kinetochore. J Cell Biol 2005;169:49-60
   PubMed Web of Science ®Google Scholar
• Liu D, Vleugel M, Backer CB, et al. Regulated targeting of protein phosphatase 1 to the outer kinetochore by KNL1 opposes Aurora B kinase. J Cell Biol 2010;188:809-20
   PubMed Web of Science ®Google Scholar
• Espeut J, Cheerambathur DK, Krenning L, et al. Microtubule binding by KNL-1 contributes to spindle checkpoint silencing at the kinetochore. J Cell Biol 2012;196:469-82
   Google Scholar
• London N, Ceto S, Ranish JA, Biggins S. Phosphoregulation of Spc105 by Mps1 and PP1 regulates Bub1 localization to kinetochores. Curr Biol 2012;22:900-6
   PubMed Web of Science ®Google Scholar
• Kruse T, Zhang G, Larsen MS, et al. Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression. J Cell Sci 2013;126:1086-92
   PubMed Web of Science ®Google Scholar
• Petrovic A, Mosalaganti S, Keller J, et al. Modular assembly of RWD domains on the Mis12 complex underlies outer kinetochore organization. Mol Cell 2014;53:591-605
   PubMed Web of Science ®Google Scholar
• Coster G, Goldberg M. The cellular response to DNA damage: a focus on MDC1 and its interacting proteins. Nucleus 2010;1:166-78
   PubMed Web of Science ®Google Scholar
• Stewart GS, Wang B, Bignell CR, et al. MDC1 is a mediator of the mammalian DNA damage checkpoint. Nature 2003;421:961-6
   PubMed Web of Science ®Google Scholar
• Lou Z, Chen BP, Asaithamby A, et al. MDC1 regulates DNA-PK autophosphorylation in response to DNA damage. J Biol Chem 2004;279:46359-62
   PubMed Web of Science ®Google Scholar
• Eliezer Y, Argaman L, Rhie A, et al. The direct interaction between 53BP1 and MDC1 is required for the recruitment of 53BP1 to sites of damage. J Biol Chem 2009;284:426-35
   PubMed Web of Science ®Google Scholar
• Townsend K, Mason H, Blackford AN, et al. Mediator of DNA damage checkpoint 1 (MDC1) regulates mitotic progression. J Biol Chem 2009;284:33939-48
   PubMed Web of Science ®Google Scholar
• Mark WY, Liao JC, Lu Y, et al. Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions? J Mol Biol 2005;345:275-87
   PubMed Web of Science ®Google Scholar
• Brzovic PS, Keeffe JR, Nishikawa H, et al. Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex. Proc Natl Acad Sci U S A 2003;100:5646-51
   PubMed Web of Science ®Google Scholar
• Williams RS, Green R, Glover JN. Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1. Nat Struct Biol 2001;8:838-42
   PubMedGoogle Scholar
• Savage KI, Harkin DP. BRCA1, a ’complex’ protein involved in the maintenance of genomic stability. FEBS J 2015;282:630-46
   PubMed Web of Science ®Google Scholar
• Xie J, Peng M, Guillemette S, et al. FANCJ/BACH1 acetylation at lysine 1249 regulates the DNA damage response. PLoS Genet 2012;8:e1002786
   PubMed Web of Science ®Google Scholar
• Greenberg RA, Sobhian B, Pathania S, et al. Multifactorial contributions to an acute DNA damage response by BRCA1/BARD1-containing complexes. Genes Dev 2006;20:34-46
   PubMed Web of Science ®Google Scholar
• Zhang F, Ma J, Wu J, et al. PALB2 links BRCA1 and BRCA2 in the DNA-damage response. Curr Biol 2009;19:524-9
   PubMed Web of Science ®Google Scholar
• Iakoucheva LM, Radivojac P, Brown CJ, et al. The importance of intrinsic disorder for protein phosphorylation. Nucleic Acids Res 2004;32:1037-49
   PubMed Web of Science ®Google Scholar
• Tyanova S, Cox J, Olsen J, et al. Phosphorylation variation during the cell cycle scales with structural propensities of proteins. PLoS Comput Biol 2013;9:e1002842
   Google Scholar
• Galea CA, Nourse A, Wang Y, et al. Role of intrinsic flexibility in signal transduction mediated by the cell cycle regulator, p27 Kip1. J Mol Biol 2008;376:827-38
   PubMed Web of Science ®Google Scholar
• Nash P, Tang X, Orlicky S, et al. Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature 2001;414:514-21
   PubMed Web of Science ®Google Scholar
• Schweiger R, Linial M. Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data. Biol Direct 2010;5:6
   Google Scholar
• Zou H, McGarry TJ, Bernal T, Kirschner MW. Identification of a vertebrate sister-chromatid separation inhibitor involved in transformation and tumorigenesis. Science 1999;285:418-22
   PubMed Web of Science ®Google Scholar
• Csizmok V, Felli IC, Tompa P, et al. Structural and dynamic characterization of intrinsically disordered human securin by NMR spectroscopy. J Am Chem Soc 2008;130:16873-9
   PubMedGoogle Scholar
• Hornig NC, Knowles PP, McDonald NQ, Uhlmann F. The dual mechanism of separase regulation by securin. Curr Biol 2002;12:973-82
   PubMed Web of Science ®Google Scholar
• Jallepalli PV, Waizenegger IC, Bunz F, et al. Securin is required for chromosomal stability in human cells. Cell 2001;105:445-57
   PubMedGoogle Scholar
• Barberis M. Sic1 as a timer of Clb cyclin waves in the yeast cell cycle–design principle of not just an inhibitor. FEBS J 2012;279:3386-410
   PubMed Web of Science ®Google Scholar
• Borg M, Mittag T, Pawson T, et al. Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. Proc Natl Acad Sci U S A 2007;104:9650-5
   Web of Science ®Google Scholar
• Pelka P, Ablack JN, Fonseca GJ, et al. Intrinsic structural disorder in adenovirus E1A: a viral molecular hub linking multiple diverse processes. J Virol 2008;82:7252-63
   PubMed Web of Science ®Google Scholar
• Chemes LB, Sanchez IE, Smal C, de Prat-Gay G. Targeting mechanism of the retinoblastoma tumor suppressor by a prototypical viral oncoprotein. Structural modularity, intrinsic disorder and phosphorylation of human papillomavirus E7. FEBS J 2010;277:973-88
   PubMed Web of Science ®Google Scholar
• Dosztanyi Z, Csizmok V, Tompa P, Simon I. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 2005;21:3433-4
   PubMed Web of Science ®Google Scholar
• Dosztanyi Z, Sandor M, Tompa P, Simon I. Prediction of protein disorder at the domain level. Curr Protein Pept Sci 2007;8:161-71
   PubMed Web of Science ®Google Scholar
• Uversky VN, Oldfield CJ, Dunker AK. Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu Rev Biophys 2008;37:215-46
   PubMed Web of Science ®Google Scholar
• Elledge SJ, Winston J, Harper JW. A question of balance: the role of cyclin-kinase inhibitors in development and tumorigenesis. Trends Cell Biol 1996;6:388-92
   PubMed Web of Science ®Google Scholar
• Hall M, Peters G. Genetic alterations of cyclins, cyclin-dependent kinases, and Cdk inhibitors in human cancer. Adv Cancer Res 1996;68:67-108
   PubMed Web of Science ®Google Scholar
• Tsai T, Davalath S, Rankin C, et al. Tumor suppressor gene alteration in adult acute lymphoblastic leukemia (ALL). Analysis of retinoblastoma (Rb) and p53 gene expression in lymphoblasts of patients with de novo, relapsed, or refractory ALL treated in Southwest Oncology Group studies. Leukemia 1996;10:1901-10
   PubMed Web of Science ®Google Scholar
• Greenblatt MS, Bennett WP, Hollstein M, Harris CC. Mutations in the p53 tumor suppressor gene: clues to cancer etiology and molecular pathogenesis. Cancer Res 1994;54:4855-78
   PubMed Web of Science ®Google Scholar
• Crook T, Vousden KH. Interaction of HPV E6 with p53 and associated proteins. Biochem Soc Trans 1994;22:52-5
   PubMed Web of Science ®Google Scholar
• Ball ARJr, Chen YY, Yokomori K. Mechanisms of cohesin-mediated gene regulation and lessons learned from cohesinopathies. Biochim Biophys Acta 2014;1839:191-202
   PubMed Web of Science ®Google Scholar
• Lapenna S, Giordano A. Cell cycle kinases as therapeutic targets for cancer. Nat Rev Drug Discov 2009;8:547-66
   PubMed Web of Science ®Google Scholar
• Vassilev LT, Vu BT, Graves B, et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 2004;303:844-8
   PubMed Web of Science ®Google Scholar
• Sebolt-Leopold JS, English JM. Mechanisms of drug inhibition of signalling molecules. Nature 2006;441:457-62
   PubMed Web of Science ®Google Scholar
• Lagerstrom MC, Schioth HB. Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat Rev Drug Discov 2008;7:339-57
   PubMed Web of Science ®Google Scholar
• Lipinski CA, Lombardo F, Dominy BW, Feeney PJ. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev 2001;46:3-26
   PubMed Web of Science ®Google Scholar
• Drews J. Drug discovery: a historical perspective. Science 2000;287:1960-4
   PubMed Web of Science ®Google Scholar
• Arkin M. Protein-protein interactions and cancer: small molecules going in for the kill. Curr Opin Chem Biol 2005;9:317-24
   PubMed Web of Science ®Google Scholar
• Arkin MR, Wells JA. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov 2004;3:301-17
   PubMed Web of Science ®Google Scholar
• Fuxreiter M, Simon I, Friedrich P, Tompa P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J Mol Biol 2004;338:1015-26
   PubMed Web of Science ®Google Scholar
• Oldfield CJ, Cheng Y, Cortese MS, et al. Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 2005;44:12454-70
   PubMed Web of Science ®Google Scholar
• Diella F, Haslam N, Chica C, et al. Understanding eukaryotic linear motifs and their role in cell signaling and regulation. Front Biosci 2008;13:6580-603
   PubMed Web of Science ®Google Scholar
• Tompa P, Davey NE, Gibson TJ, Babu MM. A million peptide motifs for the molecular biologist. Mol Cell 2014;55:161-9
   PubMed Web of Science ®Google Scholar
• Cheng Y, LeGall T, Oldfield CJ, et al. Rational drug design via intrinsically disordered protein. Trends Biotechnol 2006;24:435-42
   PubMed Web of Science ®Google Scholar
• Lane D, Levine A. p53 Research: the past thirty years and the next thirty years. Cold Spring Harb Perspect Biol 2010;2:a000893
   PubMedGoogle Scholar
• Moll UM, Petrenko O. The MDM2-p53 interaction. Mol Cancer Res 2003;1:1001-8
   PubMed Web of Science ®Google Scholar
• Hammoudeh DI, Follis AV, Prochownik EV, Metallo SJ. Multiple independent binding sites for small-molecule inhibitors on the oncoprotein c-Myc. J Am Chem Soc 2009;131:7390-401
   PubMed Web of Science ®Google Scholar
• Metallo SJ. Intrinsically disordered proteins are potential drug targets. Curr Opin Chem Biol 2010;14:481-8
   PubMed Web of Science ®Google Scholar
• Hegyi H, Buday L, Tompa P. Intrinsic structural disorder confers cellular viability on oncogenic fusion proteins. PLoS Comput Biol 2009;5:e1000552
   PubMed Web of Science ®Google Scholar
• Erkizan HV, Kong Y, Merchant M, et al. A small molecule blocking oncogenic protein EWS-FLI1 interaction with RNA helicase A inhibits growth of Ewing’s sarcoma. Nat Med 2009;15:750-6
   PubMed Web of Science ®Google Scholar
• Krishnan N, Koveal D, Miller DH, et al. Targeting the disordered C terminus of PTP1B with an allosteric inhibitor. Nat Chem Biol 2014;10:558-66
   PubMed Web of Science ®Google Scholar
• Wenthur CJ, Gentry PR, Mathews TP, Lindsley CW. Drugs for allosteric sites on receptors. Annu Rev Pharmacol Toxicol 2014;54:165-84
   PubMed Web of Science ®Google Scholar
• Tompa P. Multisteric regulation by structural disorder in modular signaling proteins: an extension of the concept of allostery. Chem Rev 2014;114:6715-32
   Google Scholar
• Xue L, Wang P, Cao P, et al. Identification of extracellular signal-regulated kinase 1 (ERK1) direct substrates using stable isotope labeled kinase assay-linked phosphoproteomics. Mol Cell Proteomics 2014;13:3199-210
   PubMed Web of Science ®Google Scholar
• Xue L, Wang WH, Iliuk A, et al. Sensitive kinase assay linked with phosphoproteomics for identifying direct kinase substrates. Proc Natl Acad Sci USA 2012;109:5615-20
   PubMed Web of Science ®Google Scholar
• Li Y, Cross FR, Chait BT. Method for identifying phosphorylated substrates of specific cyclin/cyclin-dependent kinase complexes. Proc Natl Acad Sci USA 2014;111:11323-8
   PubMed Web of Science ®Google Scholar
• Blethrow JD, Glavy JS, Morgan DO, Shokat KM. Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates. Proc Natl Acad Sci USA 2008;105:1442-7
   PubMed Web of Science ®Google Scholar
• Archambault V, Chang EJ, Drapkin BJ, et al. Targeted proteomic study of the cyclin-Cdk module. Mol Cell 2004;14:699-711
   PubMed Web of Science ®Google Scholar
• Pagliuca FW, Collins MO, Lichawska A, et al. Quantitative proteomics reveals the basis for the biochemical specificity of the cell-cycle machinery. Mol Cell 2011;43:406-17
   PubMed Web of Science ®Google Scholar
• Kettenbach AN, Schweppe DK, Faherty BK, et al. Quantitative phosphoproteomics identifies substrates and functional modules of Aurora and Polo-like kinase activities in mitotic cells. Sci Signal 2011;4:rs5
   PubMed Web of Science ®Google Scholar
• Smolka MB, Albuquerque CP, Chen SH, Zhou H. Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. Proc Natl Acad Sci USA 2007;104:10364-9
   PubMed Web of Science ®Google Scholar
• Matsuoka S, Ballif BA, Smogorzewska A, et al. ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science 2007;316:1160-6
   PubMed Web of Science ®Google Scholar
• Selenko P, Wagner G. Looking into live cells with in-cell NMR spectroscopy. J Struct Biol 2007;158:244-53
   PubMed Web of Science ®Google Scholar
• Borcherds W, Theillet FX, Katzer A, et al. Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells. Nat Chem Biol 2014;10:1000-2
   PubMed Web of Science ®Google Scholar