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Peter Tompa

Dictionary
Publications
Publications

Articles

1.   Schad E, Kalmar L and Tompa P (2013) [23460204]
  Exon-phase symmetry and intrinsic structural disorder promote modular evolution in the human genome.
  Nucleic Acids Res notSet,
2.   Bhowmick P, Pancsa R, Guharoy M and Tompa P (2013) [23734257]
  Functional diversity and structural disorder in the human ubiquitination pathway.
  PLoS ONE 8, e65443
3.   Guharoy M, Szabo B, Martos SC, Kosol S and Tompa P (2013) [23761374]
  Intrinsic structural disorder in cytoskeletal proteins.
  Cytoskeleton (hoboken) notSet,
4.   Herbert C, Schieborr U, Saxena K, Juraszek J, De Smet F, Alcouffe C, Bianciotto M, Saladino G, Sibrac D, Kudlinzki D, Sreeramulu S, Brown A, Rigon P, Herault JP, Lassalle G, Blundell TL, Rousseau F, Gils A, Schymkowitz J, Tompa P, Herbert JM, Carmeliet P, Gervasio FL, Schwalbe H and Bono F (2013) [23597563]
  Molecular Mechanism of SSR128129E, an Extracellularly Acting, Small-Molecule, Allosteric Inhibitor of FGF Receptor Signaling.
  Cancer Cell 23, 489-501
5.   Bánóczi Z, Tantos A, Farkas A, Majer Z, Dókus LE, Tompa P and Hudecz F (2013) [23613308]
  New m-calpain substrate-based azapeptide inhibitors.
  J Pept Sci notSet,
6.   Tantos A, Szrnka K, Szabo B, Bokor M, Kamasa P, Matus P, Bekesi A, Tompa K, Han KH and Tompa P (2013) [22906532]
  Structural disorder and local order of hNopp140.
  Bba-proteins Proteom 1834, 342-50
7.   Kovacs D and Tompa P (2012) [22988848]
  Diverse functional manifestations of intrinsic structural disorder in molecular chaperones.
  Biochem Soc T 40, 963-8
8.   Fuxreiter M and Tompa P (2012) [22399315]
  Fuzzy complexes: a more stochastic view of protein function.
  Adv Exp Med Biol 725, 1-14
9.   Tantos A and Tompa P (2012) [22821526]
  Identification of Intrinsically Disordered Proteins by a Special 2D Electrophoresis.
  Methods Mol Biol 896, 215-22
10.   Hegyi H and Tompa P (2012) [22105808]
  Increased structural disorder of proteins encoded on human sex chromosomes.
  Mol Biosyst 8, 229-36
11.   Tantos A, Han KH and Tompa P (2012) [21782886]
  Intrinsic disorder in cell signaling and gene transcription.
  Mol Cell Endocrinol 348, 457-65
12.   Kovacs D, Szabo B, Pancsa R and Tompa P (2012) [23142500]
  Intrinsically disordered proteins undergo and assist folding transitions in the proteome.
  Arch Biochem Biophys notSet,
13.   Tompa P (2012) [22989858]
  Intrinsically disordered proteins: a 10-year recap.
  Trends Biochem Sci 37, 509-16
14.   Kalmar L, Acs V, Silhavy D and Tompa P (2012) [22971338]
  Long-range interactions in nonsense-mediated mRNA decay are mediated by intrinsically disordered protein regions.
  J Mol Biol 424, 125-31
15.   Tompa P (2012) [22710296]
  On the supertertiary structure of proteins.
  Nat Chem Biol 8, 597-600
16.   Tantos A and Tompa P (2012) [22821542]
  Proteomic methods for the identification of intrinsically disordered proteins.
  Methods Mol Biol 896, 429-37
17.   Pancsa R and Tompa P (2012) [22496841]
  Structural disorder in eukaryotes.
  PLoS ONE 7, e34687
18.   Kalmar L, Homola D, Varga G and Tompa P (2012) [22634174]
  Structural disorder in proteins brings order to crystal growth in biomineralization.
  Bone 51, 528-34
19.   Tompa K, Bokor M and Tompa P (2012) [22760320]
  Wide-line NMR and protein hydration.
  Methods Mol Biol 895, 167-96
20.   Hazy E, Bokor M, Kalmar L, Gelencser A, Kamasa P, Han KH, Tompa K and Tompa P (2011) [22067166]
  Distinct Hydration Properties of Wild-Type and Familial Point Mutant A53T of α-Synuclein Associated with Parkinsons Disease.
  Biophys J 101, 2260-6
21.   Szalainé Ágoston B, Kovács D, Tompa P and Perczel A (2011) [21336827]
  Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14.
  Biomol Nmr Assign 5, 189-93
22.   Szasz CS, Alexa A, Toth K, Rakacs M, Langowski J and Tompa P (2011) [21634433]
  Protein disorder prevails under crowded conditions.
  Biochemistry-us 50, 5834-44
23.   Rantalainen KI, Eskelin K, Tompa P and Mäkinen K (2011) [21177813]
  Structural Flexibility Allows the Functional Diversity of Potyvirus Genome-Linked Protein VPg.
  J Virol 85, 2449-57
24.   Tompa P and Rose GD (2011) [21987416]
  The Levinthal paradox of the interactome.
  Protein Sci 20, 2074-9
25.   Schad E, Tompa P and Hegyi H (2011) [22182830]
  The relationship between proteome size, structural disorder and organism complexity.
  Genome Biol 12, R120
26.   Tompa P (2011) [21514142]
  Unstructural biology coming of age.
  Curr Opin Struc Biol 21, 419-25
27.   Hegyi H, Kalmar L, Horvath T and Tompa P (2011) [20972208]
  Verification of alternative splicing variants based on domain integrity, truncation length and intrinsic protein disorder.
  Nucleic Acids Res 39, 1208-19
28.   Buday L and Tompa P (2010) [21069901]
  Accessory proteins in signal transduction: scaffold proteins and beyond.
  FEBS J 277, 4347
29.   Kovacs E, Tompa P, Liliom K and Kalmar L (2010) [20212158]
  Dual coding in alternative reading frames correlates with intrinsic protein disorder.
  P Natl Acad Sci Usa 107, 5429-34
30.   Buday L and Tompa P (2010) [20883491]
  Functional classification of scaffold proteins and related molecules.
  FEBS J 277, 4348-55
31.   Tompa K, Bánki P, Bokor M, Kamasa P, Rácz P and Tompa P (2010) [20412792]
  Hydration water/interfacial water in crystalline lens.
  Exp Eye Res 91, 76-84
32.   Tompa P and Kovacs D (2010) [20453919]
  Intrinsically disordered chaperones in plants and animals.
  Biochem Cell Biol 88, 167-74
33.   Bánóczi Z, Dókus EL, Tantos Á, Farkas A, Tompa P, Friedrich P and Hudecz F (2010) [-100056194]
  Novel calpain inhibitors
  Proteins , 606-607
34.   Tompa P and Kalmar L (2010) [20816987]
  Power law distribution defines structural disorder as a structural element directly linked with function.
  J Mol Biol 403, 346-50
35.   Burra PV, Kalmar L and Tompa P (2010) [20711457]
  Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.
  PLoS ONE 5, e12069
36.   Tompa P, Fuxreiter M, Oldfield CJ, Simon I, Dunker AK and Uversky VN (2009) [19260013]
  Close encounters of the third kind: disordered domains and the interactions of proteins.
  Bioessays 31, 328-35
37.   Tantos A, Friedrich P and Tompa P (2009) [19121309]
  Cold stability of intrinsically disordered proteins.
  FEBS Lett 583, 465-9
38.   Fuxreiter M and Tompa P (2009) [19019685]
  Fuzzy interactome: the limitations of models in molecular biology.
  Trends Biochem Sci 34, 3
39.   Bermel W, Bertini I, Csizmok V, Felli IC, Pierattelli R and Tompa P (2009) [19307141]
  H-start for exclusively heteronuclear NMR spectroscopy: The case of intrinsically disordered proteins.
  J Magn Reson 198, 275-81
40.   Balázs A, Csizmok V, Buday L, Rakács M, Kiss R, Bokor M, Udupa R, Tompa K and Tompa P (2009) [19523119]
  High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1.
  FEBS J 276, 3744-56
41.   Tompa K, Bánki P, Bokor M, Kamasa P, Lasanda G and Tompa P (2009) [19348762]
  Interfacial water at protein surfaces: wide-line NMR and DSC characterization of hydration in ubiquitin solutions.
  Biophys J 96, 2789-98
42.   Hegyi H, Buday L and Tompa P (2009) [19888473]
  Intrinsic structural disorder confers cellular viability on oncogenic fusion proteins.
  PLoS Comput Biol 5, e1000552
43.   Kovacs D, Rakacs M, Agoston B, Lenkey K, Semrad K, Schroeder R and Tompa P (2009) [19071121]
  Janus chaperones: assistance of both RNA- and protein-folding by ribosomal proteins.
  FEBS Lett 583, 88-92
44.   Hazy E and Tompa P (2009) [19462392]
  Limitations of induced folding in molecular recognition by intrinsically disordered proteins.
  Chemphyschem 10, 1415-9
45.   Tompa P (2009) [19712107]
  Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins.
  FEBS J 276, 5406-15
46.   Kovacs D, Vassos E, Liu X, Sun X, Hu J, Breen G, Tompa P, Collier DA and Li T (2009) [19261388]
  The androgen receptor gene polyglycine repeat polymorphism is associated with memory performance in healthy Chinese individuals.
  Psychoneuroendocrino 34, 947-52
47.   Kiss R, Bozoky Z, Kovács D, Róna G, Friedrich P, Dvortsák P, Weisemann R, Weisemann R, Tompa P and Perczel A (2008) [18519038]
  Calcium-induced tripartite binding of intrinsically disordered calpastatin to its cognate enzyme, calpain.
  FEBS Lett 582, 2149-54
48.   Kovacs D, Kalmar E, Torok Z and Tompa P (2008) [18359842]
  Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins.
  Plant Physiol 147, 381-90
49.   Banoczi Z, Farkas A, Alexa A, Tantos A, Tompa P, Friedrich P and Hudecz F (2008) [-100017845]
  Detection and modification of intracellular calpain activity by cell penetrating peptide conjugate
  J Pept Sci 14, 21-21
50.   Kovacs D, Agoston B and Tompa P (2008) [19704836]
  Disordered plant LEA proteins as molecular chaperones.
  Plant Signal Behav 3, 710-3
51.   Tompa P and Fuxreiter M (2008) [18054235]
  Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions.
  Trends Biochem Sci 33, 2-8
52.   Szollosi E, Bokor M, Bodor A, Perczel A, Klement E, Medzihradszky KF, Tompa K and Tompa P (2008) [18484763]
  Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities.
  J Proteome Res 7, 2291-9
53.   Hegyi H and Tompa P (2008) [18369417]
  Intrinsically disordered proteins display no preference for chaperone binding in vivo.
  PLoS Comput Biol 4, e1000017
54.   Kiss R, Kovács D, Tompa P and Perczel A (2008) [18537264]
  Local structural preferences of calpastatin, the intrinsically unstructured protein inhibitor of calpain.
  Biochemistry-us 47, 6936-45
55.   Fuxreiter M, Tompa P, Simon I, Uversky VN, Hansen JC and Asturias FJ (2008) [19008886]
  Malleable machines take shape in eukaryotic transcriptional regulation.
  Nat Chem Biol 4, 728-37
56.   Dosztányi Z and Tompa P (2008) [18542859]
  Prediction of protein disorder.
  Methods Mol Biol 426, 103-15
57.   Csizmok V, Felli IC, Tompa P, Banci L and Bertini I (2008) [19053469]
  Structural and dynamic characterization of intrinsically disordered human securin by NMR spectroscopy.
  J Am Chem Soc 130, 16873-9
58.   Tompa P, Prilusky J, Silman I and Sussman JL (2008) [18004785]
  Structural disorder serves as a weak signal for intracellular protein degradation.
  Proteins 71, 903-9
59.   Tusnády GE, Kalmár L, Hegyi H, Tompa P and Simon I (2008) [18434342]
  TOPDOM: database of domains and motifs with conservative location in transmembrane proteins.
  Bioinformatics 24, 1469-70
60.   Sickmeier M, Hamilton JA, LeGall T, Vacic V, Cortese MS, Tantos A, Szabo B, Tompa P, Chen J, Uversky VN, Obradovic Z and Dunker AK (2007) [17145717]
  DisProt: the Database of Disordered Proteins.
  Nucleic Acids Res 35, D786-93
61.   Szollosi E, Házy E, Szász C and Tompa P (2007) [17129571]
  Large systematic errors compromise quantitation of intrinsically unstructured proteins.
  Anal Biochem 360, 321-3
62.   Fuxreiter M, Tompa P and Simon I (2007) [17387114]
  Local structural disorder imparts plasticity on linear motifs.
  Bioinformatics 23, 950-6
63.   Mészáros B, Tompa P, Simon I and Dosztányi Z (2007) [17681540]
  Molecular principles of the interactions of disordered proteins.
  J Mol Biol 372, 549-61
64.   Dosztányi Z, Sándor M, Tompa P and Simon I (2007) [17430197]
  Prediction of protein disorder at the domain level.
  Curr Protein Pept Sc 8, 161-71
65.   Hegyi H, Schad E and Tompa P (2007) [17922903]
  Structural disorder promotes assembly of protein complexes.
  Bmc Struct Biol 7, 65
66.   Banóczi Z, Tantos A, Farkas A, Tompa P, Friedrich P and Hudecz F (2007) [17226965]
  Synthesis of cell-penetrating conjugates of calpain activator peptides.
  Bioconjugate Chem 18, 130-7
67.   Csizmók V, Dosztányi Z, Simon I and Tompa P (2007) [17430198]
  Towards proteomic approaches for the identification of structural disorder.
  Curr Protein Pept Sc 8, 173-9
68.   Csizmók V, Szollosi E, Friedrich P and Tompa P (2006) [16223749]
  A novel two-dimensional electrophoresis technique for the identification of intrinsically unstructured proteins.
  Mol Cell Proteomics 5, 265-73
69.   Kókai E, Tantos A, Vissi E, Szöor B, Tompa P, Gausz J, Alphey L, Friedrich P and Dombrádi V (2006) [16631104]
  CG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y.
  Arch Biochem Biophys 451, 59-67
70.   Dosztányi Z, Chen J, Dunker AK, Simon I and Tompa P (2006) [17081050]
  Disorder and sequence repeats in hub proteins and their implications for network evolution.
  J Proteome Res 5, 2985-95
71.   Solt I, Magyar C, Simon I, Tompa P and Fuxreiter M (2006) [16761278]
  Phosphorylation-induced transient intrinsic structure in the kinase-inducible domain of CREB facilitates its recognition by the KIX domain of CBP.
  Proteins 64, 749-57
72.   Tompa P, Dosztányi Z and Simon I (2006) [16889422]
  Prevalent structural disorder in E. coli and S. cerevisiae proteomes.
  J Proteome Res 5, 1996-2000
73.   Tompa P, Bánki P, Bokor M, Kamasa P, Kovács D, Lasanda G and Tompa K (2006) [16798808]
  Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects.
  Biophys J 91, 2243-9
74.   Dosztányi Z, Csizmók V, Tompa P and Simon I (2005) [15955779]
  IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content.
  Bioinformatics 21, 3433-4
75.   Bozóky Z, Alexa A, Tompa P and Friedrich P (2005) [15569003]
  Multiple interactions of the 'transducer' govern its function in calpain activation by Ca2+.
  Biochem J 388, 741-4
76.   Bokor M, Csizmók V, Kovács D, Bánki P, Friedrich P, Tompa P and Tompa K (2005) [15613629]
  NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.
  Biophys J 88, 2030-7
77.   Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K and Tompa P (2005) [15751971]
  Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2.
  Biochemistry-us 44, 3955-64
78.   Tompa P, Szász C and Buday L (2005) [16054818]
  Structural disorder throws new light on moonlighting.
  Trends Biochem Sci 30, 484-9
79.   Tompa P (2005) [15943980]
  The interplay between structure and function in intrinsically unstructured proteins.
  FEBS Lett 579, 3346-54
80.   Dosztányi Z, Csizmók V, Tompa P and Simon I (2005) [15769473]
  The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins.
  J Mol Biol 347, 827-39
81.   Farkas A, Tompa P, Schád E, Sinka R, Jékely G and Friedrich P (2004) [14614768]
  Autolytic activation and localization in Schneider cells (S2) of calpain B from Drosophila.
  Biochem J 378, 299-305
82.   Jánossy J, Ubezio P, Apáti A, Magócsi M, Tompa P and Friedrich P (2004) [15041468]
  Calpain as a multi-site regulator of cell cycle.
  Biochem Pharmacol 67, 1513-21
83.   Alexa A, Bozóky Z, Farkas A, Tompa P and Friedrich P (2004) [14976200]
  Contribution of distinct structural elements to activation of calpain by Ca2+ ions.
  J Biol Chem 279, 20118-26
84.   Friedrich P, Papp H, Halasy K, Farkas A, Farkas B, Tompa P and Kása P (2004) [15078555]
  Differential distribution of calpain small subunit 1 and 2 in rat brain.
  Eur J Neurosci 19, 1819-25
85.   Farkas A, Nardai G, Csermely P, Tompa P and Friedrich P (2004) [15250825]
  DUK114, the Drosophila orthologue of bovine brain calpain activator protein, is a molecular chaperone.
  Biochem J 383, 165-70
86.   Tompa P, Buzder-Lantos P, Tantos A, Farkas A, Szilágyi A, Bánóczi Z, Hudecz F and Friedrich P (2004) [14988399]
  On the sequential determinants of calpain cleavage.
  J Biol Chem 279, 20775-85
87.   Fuxreiter M, Simon I, Friedrich P and Tompa P (2004) [15111064]
  Preformed structural elements feature in partner recognition by intrinsically unstructured proteins.
  J Mol Biol 338, 1015-26
88.   Friedrich P, Tompa P and Farkas A (2004) [15382138]
  The calpain-system of Drosophila melanogaster: coming of age.
  Bioessays 26, 1088-96
89.   Tompa P and Csermely P (2004) [15284216]
  The role of structural disorder in the function of RNA and protein chaperones.
  FASEB J 18, 1169-75
90.   Mucsi Z, Hudecz F, Hollósi M, Tompa P and Friedrich P (2003) [14500891]
  Binding-induced folding transitions in calpastatin subdomains A and C.
  Protein Sci 12, 2327-36
91.   Tompa P (2003) [12938174]
  Intrinsically unstructured proteins evolve by repeat expansion.
  Bioessays 25, 847-55
92.   Spadoni C, Farkas A, Sinka R, Tompa P and Friedrich P (2003) [12646209]
  Molecular cloning and RNA expression of a novel Drosophila calpain, Calpain C.
  Biochem Bioph Res Co 303, 343-9
93.   Farkas A, Tompa P and Friedrich P (2003) [-100002781]
  Revisiting ubiquity and tissue specificity of human calpains.
  Biol Chem 384, 945-949
94.   Tompa P (2003) [-100002801]
  The functional benefits of protein disorder.
  J Mol Struc-theochem 666-667, 361-371
95.   Schád E, Farkas A, Jékely G, Tompa P and Friedrich P (2002) [11853546]
  A novel human small subunit of calpains.
  Biochem J 362, 383-8
96.   Tompa P, Mucsi Z, Orosz G and Friedrich P (2002) [11809743]
  Calpastatin subdomains A and C are activators of calpain.
  J Biol Chem 277, 9022-6
97.   Tompa P (2002) [12368089]
  Intrinsically unstructured proteins.
  Trends Biochem Sci 27, 527-33
98.   Alexa A, Schmidt G, Tompa P, Ogueta S, Vázquez J, Kulcsár P, Kovács J, Dombrádi V and Friedrich P (2002) [12369833]
  The phosphorylation state of threonine-220, a uniquely phosphatase-sensitive protein kinase A site in microtubule-associated protein MAP2c, regulates microtubule binding and stability.
  Biochemistry-us 41, 12427-35
99.   Tompa P, Tusnády GE, Friedrich P and Simon I (2002) [11916832]
  The role of dimerization in prion replication.
  Biophys J 82, 1711-8
100.   Tompa P, Emori Y, Sorimachi H, Suzuki K and Friedrich P (2001) [11162675]
  Domain III of calpain is a ca2+-regulated phospholipid-binding domain.
  Biochem Bioph Res Co 280, 1333-9
101.   Tompa P, Töth-Boconádi R and Friedrich P (2001) [11162853]
  Frequency decoding of fast calcium oscillations by calpain.
  Cell Calcium 29, 161-70
102.   Tompa P, Tusnády GE, Cserző M and Simon I (2001) [11287647]
  Prion protein: evolution caught en route.
  P Natl Acad Sci Usa 98, 4431-6
103.   Tompa P, Schád E and Friedrich P (2000) [10818758]
  A sensitive and continuous fluorometric activity assay using a natural substrate. Microtubule-associated protein 2.
  Methods Mol Biol 144, 137-41
104.   Wronski R, Tompa P, Hutter-Paier B, Crailsheim K, Friedrich P and Windisch M (2000) [10847556]
  Inhibitory effect of a brain derived peptide preparation on the Ca++-dependent protease, calpain.
  J Neural Transm 107, 145-57
105.   Tompa P and Friedrich P (2000) [10818757]
  Kinetic analysis of human mu-calpain autolysis.
  Methods Mol Biol 144, 129-36
106.   Tompa P and Friedrich P (1998) [9697111]
  Prion proteins as memory molecules: an hypothesis.
  Neuroscience 86, 1037-43
107.   Tompa P and Friedrich P (1998) [9530914]
  Synaptic metaplasticity and the local charge effect in postsynaptic densities.
  Trends Neurosci 21, 97-102
108.   Baki A, Tompa P, Alexa A, Molnár O and Friedrich P (1996) [8836135]
  Autolysis parallels activation of mu-calpain.
  Biochem J 318 (Pt 3), 897-901
109.   Alexa A, Tompa P, Baki A, Vereb G and Friedrich P (1996) [8776665]
  Mutual protection of microtubule-associated protein 2 (MAP2) and cyclic AMP-dependent protein kinase II against mu-calpain.
  J Neurosci Res 44, 438-45
110.   Sánchez C, Tompa P, Szücs K, Friedrich P and Avila J (1996) [8944764]
  Phosphorylation and dephosphorylation in the proline-rich C-terminal domain of microtubule-associated protein 2.
  Eur J Biochem 241, 765-71
111.   Tompa P, Baki A, Schád E and Friedrich P (1996) [8969168]
  The calpain cascade. Mu-calpain activates m-calpain.
  J Biol Chem 271, 33161-4
112.   Tompa P, Schád E, Baki A, Alexa A, Batke J and Friedrich P (1995) [8572308]
  An ultrasensitive, continuous fluorometric assay for calpain activity.
  Anal Biochem 228, 287-93
113.   Batke J, Benito VA and Tompa P (1992) [-100016950]
  A Possible Invivo Mechanism of Intermediate Transfer by Glycolytic Enzyme Complexes - Steady-state Fluorescence Anisotropy Analysis of An Enzyme Complex-formation
  Arch Biochem Biophys 296, 654-9
114.   Nazaryan KB, Climent F, Simonian S, Tompa P and Batke J (1992) [-100016959]
  Interaction of Rabbit Muscle Enolase And 3-phosphoglycerate Mutase Studied by Elisa And by Batch Gel-filtration
  Arch Biochem Biophys 296, 650-3
115.   Tompa P and Batke J (1990) [-100005949]
  Fructose-1,6-bisphosphate Aldolase Preferentially Associates to Olyceraldehyde-3-phosphate Dehydrogenase In a Mixture of Cytosolic Proteins as Revealed by Fluorescence Energy-transfer Measurements
  Biochemistry International 20, 487-94
116.   Ovádi J, Tompa P, Vértessy B, Orosz F, Keleti T and Welch GR (1989) [2920010]
  Transient-time analysis of substrate-channelling in interacting enzyme systems.
  Biochem J 257, 187-90
117.   Tompa P, Batke J and Ovádi J (1987) [3569522]
  How to determine the efficiency of intermediate transfer in an interacting enzyme system?
  FEBS Lett 214, 244-8
118.   Tompa P, Batke J, Ovadi J, Welch GR and Srere PA (1987) [3571248]
  Quantitation of the interaction between citrate synthase and malate dehydrogenase.
  J Biol Chem 262, 6089-92
119.   Tompa P, Bar J and Batke J (1986) [-100005338]
  Interaction of Enzymes Involved In Triosephosphate Metabolism - Comparison of Yeast And Rabbit Muscle Cytoplasmic Systems
  Eur J Biochem 159, 117-24
120.   Tompa P, Hong PT and Vas M (1986) [3948871]
  The phosphate group of 3-phosphoglycerate accounts for conformational changes occurring on binding to 3-phosphoglycerate kinase. Enzyme inhibition and thiol reactivity studies.
  Eur J Biochem 154, 643-9

Books or book chapters

1.   Kovács D and Tompa P (2010)
  Chaperone Activity of Intrinsically Disordered Proteins
  Handbook of Molecular Chaperones: Roles, Structures and Mechanisms , Ch.14
2.   Tompa P (2004)
  The functional benefits of protein disorder.
  The Role of Chemistry in the Evolution of Molecular Medicine , 361-362
3.   Friedrich P, Tompa P, Jekely G, Farkas A and Schad E (2001)
  Calpains in cellular signalling.
  Protein modules in cellular signalling. 318, 363-373
4.   Friedrich P, Tompa P and Jekely G (1999)
  Calpains in drosophila and mammals: Structure and implications in neuronal function.
  Calpain: Pharmacology and Toxicology of Calcium-dependent protease. , 429-440
5.   Friedrich P, Tompa P and Jekely G (1999)
  Calpains in drosophila and mammals: Structure and implications in neural function.
  Calpain: Pharmacology and Toxicology of Calcium-dependent protease. , 429-440