P Tompa

Summary

Affiliation: Hungarian Academy of Sciences
Country: Hungary

Publications

  1. pmc The relationship between proteome size, structural disorder and organism complexity
    Eva Schad
    Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Karolina ut 29, Budapest, Hungary
    Genome Biol 12:R120. 2011
  2. pmc Structural disorder promotes assembly of protein complexes
    Hedi Hegyi
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    BMC Struct Biol 7:65. 2007
  3. doi request reprint Intrinsically disordered chaperones in plants and animals
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina ut 29, H 1113 Budapest, Hungary
    Biochem Cell Biol 88:167-74. 2010
  4. ncbi request reprint Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Trends Biochem Sci 33:2-8. 2008
  5. ncbi request reprint Structural disorder throws new light on moonlighting
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 29 Karolina Street, 1113 Budapest, Hungary
    Trends Biochem Sci 30:484-9. 2005
  6. doi request reprint Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins
    P Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    FEBS J 276:5406-15. 2009
  7. ncbi request reprint The interplay between structure and function in intrinsically unstructured proteins
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, H 1518 Budapest, Hungary
    FEBS Lett 579:3346-54. 2005
  8. ncbi request reprint The role of structural disorder in the function of RNA and protein chaperones
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518 Budapest, P O Box 7, Hungary
    FASEB J 18:1169-75. 2004
  9. doi request reprint Close encounters of the third kind: disordered domains and the interactions of proteins
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Bioessays 31:328-35. 2009
  10. ncbi request reprint Intrinsically unstructured proteins evolve by repeat expansion
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518 Budapest, PO Box 7, Hungary
    Bioessays 25:847-55. 2003

Collaborators

Detail Information

Publications65

  1. pmc The relationship between proteome size, structural disorder and organism complexity
    Eva Schad
    Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Karolina ut 29, Budapest, Hungary
    Genome Biol 12:R120. 2011
    ..As intrinsic protein disorder has been linked with complex responses to environmental stimuli and communication between cells, an additional possibility is that structural disorder may effectively increase the complexity of species...
  2. pmc Structural disorder promotes assembly of protein complexes
    Hedi Hegyi
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    BMC Struct Biol 7:65. 2007
    ..The recent high-throughput analyses of protein-protein interactions and protein complexes in the cell generated data that enable to address this issue by bioinformatic means...
  3. doi request reprint Intrinsically disordered chaperones in plants and animals
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina ut 29, H 1113 Budapest, Hungary
    Biochem Cell Biol 88:167-74. 2010
    ..Using these details, we chart out how far the field has progressed only to emphasize the long road ahead before chaperone function can be firmly established as part of the physiological mechanistic arsenal of the emerging group of IDPs...
  4. ncbi request reprint Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Trends Biochem Sci 33:2-8. 2008
    ..Given the crucial role of protein disorder in protein-protein interactions and in regulatory processes, we envision that fuzziness will become integral to understanding the interactome...
  5. ncbi request reprint Structural disorder throws new light on moonlighting
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 29 Karolina Street, 1113 Budapest, Hungary
    Trends Biochem Sci 30:484-9. 2005
    ..Owing to the apparent functional benefits, we expect to see many more examples of this parsimonious use of protein material in complex metabolic networks...
  6. doi request reprint Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins
    P Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    FEBS J 276:5406-15. 2009
    ..e. disorder in the bound state that may serve different functions, such as the accommodation of destabilizing residues and the mediation of secondary interactions between protofibrils...
  7. ncbi request reprint The interplay between structure and function in intrinsically unstructured proteins
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, H 1518 Budapest, Hungary
    FEBS Lett 579:3346-54. 2005
    ..Via all these details, it is demonstrated that in only a couple of years after its conception, the idea of protein disorder has already come of age and transformed our basic concepts of protein structure and function...
  8. ncbi request reprint The role of structural disorder in the function of RNA and protein chaperones
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518 Budapest, P O Box 7, Hungary
    FASEB J 18:1169-75. 2004
    ..7% and 15%, respectively. In keeping with these and other details, a novel "entropy transfer" model is presented to account for the mechanistic role of structural disorder in chaperone function...
  9. doi request reprint Close encounters of the third kind: disordered domains and the interactions of proteins
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Bioessays 31:328-35. 2009
    ..With these points, we argue that these long disordered regions should be recognized as a distinct class of biologically functional protein domains...
  10. ncbi request reprint Intrinsically unstructured proteins evolve by repeat expansion
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518 Budapest, PO Box 7, Hungary
    Bioessays 25:847-55. 2003
    ....
  11. doi request reprint Power law distribution defines structural disorder as a structural element directly linked with function
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, PO Box 7, 1518 Budapest, Hungary
    J Mol Biol 403:346-50. 2010
    ..We interpret this finding by the direct functional involvement of disorder, which distinguishes it from secondary structural elements and endows it with tertiary structural attributes...
  12. pmc Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects
    P Tompa
    Institute of Enzymology, Biological Research Center, and Research Institute for Solid State Physics and Optics, Hungarian Academy of Sciences, H 1518 Budapest, Hungary
    Biophys J 91:2243-9. 2006
    ....
  13. ncbi request reprint Prevalent structural disorder in E. coli and S. cerevisiae proteomes
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    J Proteome Res 5:1996-2000. 2006
    ..Thus, protein disorder is a widespread and functionally important phenomenon, which needs to be characterized in full detail for understanding complex organisms at the molecular level...
  14. ncbi request reprint Intrinsically unstructured proteins
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518, PO Box 7, Budapest, Hungary
    Trends Biochem Sci 27:527-33. 2002
    ..In this review, recent findings are surveyed to illustrate that this novel but rapidly advancing field has reached a point where these proteins can be comprehensively classified on the basis of structure and function...
  15. doi request reprint Unstructural biology coming of age
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Curr Opin Struct Biol 21:419-25. 2011
    ....
  16. ncbi request reprint Calpastatin subdomains A and C are activators of calpain
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H 1518 Budapest, P O Box 7, Hungary
    J Biol Chem 277:9022-6. 2002
    ..Furthermore, these activators open new avenues to cell biological studies of calpain function and eventually may alleviate pathological states caused by calpain malfunction...
  17. ncbi request reprint Frequency decoding of fast calcium oscillations by calpain
    P Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Hungary
    Cell Calcium 29:161-70. 2001
    ..Our results show that calpain is sensitive to the frequency of fast Ca2+ oscillations in vitro, which is of potential physiological significance...
  18. ncbi request reprint Domain III of calpain is a ca2+-regulated phospholipid-binding domain
    P Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, H 1518, Hungary
    Biochem Biophys Res Commun 280:1333-9. 2001
    ..These results suggest that domain III might be the primary lipid binding site of calpain and may play a decisive role in orchestrating Ca2+- and lipid activation of the enzyme...
  19. ncbi request reprint Contribution of distinct structural elements to activation of calpain by Ca2+ ions
    Anita Alexa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, H 1518 Budapest, Hungary
    J Biol Chem 279:20118-26. 2004
    ..A schematic model of this "extended transducer" mechanism is presented...
  20. pmc DUK114, the Drosophila orthologue of bovine brain calpain activator protein, is a molecular chaperone
    Attila Farkas
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Biochem J 383:165-70. 2004
    ..Our work is the first experimental evidence that DUK114, and possibly other members of this family, are molecular chaperones...
  21. ncbi request reprint Local structural disorder imparts plasticity on linear motifs
    Monika Fuxreiter
    Institute of Enzymology, BRC, Hungarian Academy of Sciences, Budapest, Hungary
    Bioinformatics 23:950-6. 2007
    ..These results establish a connection between LMs and molecular recognition elements of intrinsically unstructured proteins (IUPs), which realize a non-conventional mode of partner binding mostly in regulatory functions...
  22. ncbi request reprint Molecular cloning and RNA expression of a novel Drosophila calpain, Calpain C
    Cesare Spadoni
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, Budapest H 1518, Hungary
    Biochem Biophys Res Commun 303:343-9. 2003
    ..Moreover, we analysed Calpain C RNA expression during Drosophila development by RT-PCR and RNA in situ hybridization, which revealed strong expression in the salivary glands...
  23. doi request reprint Hydration water/interfacial water in crystalline lens
    K Tompa
    Research Institute for Solid State Physics and Optics, Hungarian Academy of Sciences, Budapest, POB 49, H 1525, Hungary
    Exp Eye Res 91:76-84. 2010
    ..6 +/- 0.3 J g(-1) K(-1). Thus, in a thermodynamic sense, crystalline protein and its hydrate layer behave as a highly-interconnected single phase...
  24. ncbi request reprint Molecular principles of the interactions of disordered proteins
    Bálint Mészáros
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518, Budapest, Hungary
    J Mol Biol 372:549-61. 2007
    ..e. they use their binding energy for folding. Overall, our findings provide a structural rationale to the prior suggestions that many IUPs are specialized for functions realized by protein-protein interactions...
  25. pmc Intrinsically disordered proteins display no preference for chaperone binding in vivo
    Hedi Hegyi
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    PLoS Comput Biol 4:e1000017. 2008
    ..In support of this conclusion, we show that IDPs that bind chaperones also tend to bind other proteins...
  26. doi request reprint Wide-line NMR and protein hydration
    K Tompa
    Research Institute for Solid State Physics and Optics, Hungarian Academy of Sciences, Budapest, Hungary
    Methods Mol Biol 895:167-96. 2012
    ..Finally, we wrap up the chapter with the results on two proteins (a globular and an intrinsically disordered)...
  27. pmc Distinct hydration properties of wild-type and familial point mutant A53T of α-synuclein associated with Parkinson's disease
    E Hazy
    Institute of Enzymology, Hungarian Academy of Sciences, Budapest, Hungary
    Biophys J 101:2260-6. 2011
    ..These differences disappear in the amyloid state, suggesting basically the same surface topology, irrespective of the initial monomeric state...
  28. ncbi request reprint The calpain cascade. Mu-calpain activates m-calpain
    P Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H 1518 Budapest, Hungary
    J Biol Chem 271:33161-4. 1996
    ..We suggest that these in vitro observations are relevant in vivo and the calpain cascade may play an important role in coordinating the functioning of calpains in living cells...
  29. ncbi request reprint Disorder and sequence repeats in hub proteins and their implications for network evolution
    Zsuzsanna Dosztanyi
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518 Budapest, Hungary
    J Proteome Res 5:2985-95. 2006
    ....
  30. pmc Multiple interactions of the 'transducer' govern its function in calpain activation by Ca2+
    Zoltan Bozoky
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, 1518 Budapest, Hungary
    Biochem J 388:741-4. 2005
    ..The kinetic parameters of these mutant enzymes support a model featuring shrinkage of transducer as a contributor to structural changes involved in calpain activation...
  31. ncbi request reprint Structural disorder serves as a weak signal for intracellular protein degradation
    P Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Proteins 71:903-9. 2008
    ..Protein disorder, nevertheless, plays a key signalling role in many cases...
  32. pmc Intrinsic structural disorder confers cellular viability on oncogenic fusion proteins
    Hedi Hegyi
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    PLoS Comput Biol 5:e1000552. 2009
    ..g. EWS-ATF). Our findings also suggest novel strategies of intervention against the ensuing neoplastic transformations...
  33. ncbi request reprint Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2
    Veronika Csizmok
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Post Office Box 7, H 1518 Budapest, Hungary
    Biochemistry 44:3955-64. 2005
    ..To emphasize the possible importance of this structural trait, we propose that these motifs be called primary contact sites in IUPs...
  34. pmc Malleable machines take shape in eukaryotic transcriptional regulation
    Monika Fuxreiter
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina ut 29, H 1113, H 1518 Budapest, Hungary
    Nat Chem Biol 4:728-37. 2008
    ..All these features expand the capacities of ordered complexes and give rise to efficient regulatory mechanisms...
  35. doi request reprint Janus chaperones: assistance of both RNA- and protein-folding by ribosomal proteins
    Denes Kovacs
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    FEBS Lett 583:88-92. 2009
    ..These observations highlight possible novel aspects of the promiscuous functions of ribosomal proteins outside of the ribosome...
  36. ncbi request reprint Differential distribution of calpain small subunit 1 and 2 in rat brain
    Peter Friedrich
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H 1518 Budapest, PO Box 7, Hungary
    Eur J Neurosci 19:1819-25. 2004
    ..The hypothesis is advanced that these distinct distributions of calpain subunits may be related to the transport of these enzymes in nerve cells...
  37. ncbi request reprint The calpain-system of Drosophila melanogaster: coming of age
    Peter Friedrich
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Bioessays 26:1088-96. 2004
    ..Equipped with all this information, we may now embark on the genetic modification of family members, interpreting mutant phenotypes in terms of the cell biology of calpains...
  38. ncbi request reprint IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    Zsuzsanna Dosztanyi
    Institute of Enzymology, BRC, Hungarian Academy of Sciences, PO Box 7, H 1518 Budapest, Hungary
    Bioinformatics 21:3433-4. 2005
    ..Optional to the prediction are built-in parameter sets optimized for predicting short or long disordered regions and structured domains...
  39. ncbi request reprint Calpain as a multi-site regulator of cell cycle
    Judit Janossy
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Biochem Pharmacol 67:1513-21. 2004
    ..Overall, our analysis suggests that calpain regulates the cell cycle at more points than previously thought...
  40. pmc A novel human small subunit of calpains
    Eva Schad
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H 1518 Budapest, P O Box 7, Hungary
    Biochem J 362:383-8. 2002
    ..The expression of this protein in vivo, as assessed from its appearance in expressed sequence tag clones, is rather limited, making it an example of a tissue-specific, rather than ubiquitous, small subunit...
  41. doi request reprint Protein disorder prevails under crowded conditions
    C S Szasz
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Biochemistry 50:5834-44. 2011
    ..e., these IDPs do remain in a state of rapidly interconverting structural ensemble. Altogether, our results underline that structural disorder is the physiological state of these proteins...
  42. pmc Prion protein: evolution caught en route
    P Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P.O. Box 7, H-1518 Budapest, Hungary
    Proc Natl Acad Sci U S A 98:4431-6. 2001
    ..This scenario may explain why, in a structural sense, the prion protein is still en route toward becoming a foldable globular protein...
  43. ncbi request reprint On the sequential determinants of calpain cleavage
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, H 1518 Budapest, Hungary
    J Biol Chem 279:20775-85. 2004
    ..In the case of micro- and m-calpain, this substrate is kinetically superior to commercially available ones, and it can be used for the in vivo assessment of the activity of these ubiquitous mammalian calpains...
  44. pmc Autolytic activation and localization in Schneider cells (S2) of calpain B from Drosophila
    Attila Farkas
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, Budapest H 1518, Hungary
    Biochem J 378:299-305. 2004
    ..In S2 cells, calpain B was mainly in the cytoplasm and upon a rise in Ca2+ the enzyme adhered to intracellular membranes...
  45. doi request reprint Cold stability of intrinsically disordered proteins
    Agnes Tantos
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina ut 29, H 1113 Budapest, Hungary
    FEBS Lett 583:465-9. 2009
    ..Our results affirm that in contrast with globular proteins IDPs are resistant to cold treatment. The theoretical and functional aspects of this observation are discussed...
  46. pmc Dual coding in alternative reading frames correlates with intrinsic protein disorder
    Erika Kovacs
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina ut 29, H 1113 Budapest, Hungary
    Proc Natl Acad Sci U S A 107:5429-34. 2010
    ..By discussing several examples, we demonstrate that dual coding may be an effective mechanism for the evolutionary appearance of novel intrinsically disordered regions with new functions...
  47. ncbi request reprint The phosphorylation state of threonine-220, a uniquely phosphatase-sensitive protein kinase A site in microtubule-associated protein MAP2c, regulates microtubule binding and stability
    A Alexa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Biochemistry 41:12427-35. 2002
    ..Phosphorylation of this site also affects proteolytic sensitivity of MAP2c, which might represent a further level of control in this system. Thus, the phosphorylation state of T(220) may be a primary determinant of microtubule function...
  48. pmc NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins
    Monika Bokor
    Research Institute for Solid State Physics and Optics, Hungarian Academy of Sciences, Budapest, Hungary
    Biophys J 88:2030-7. 2005
    ..The theoretical treatment and experimental approach presented in this article may have general utility in characterizing proteins that belong to this novel structural class...
  49. ncbi request reprint Towards proteomic approaches for the identification of structural disorder
    Veronika Csizmok
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Curr Protein Pept Sci 8:173-9. 2007
    ..Advantages and drawbacks of the various approaches are outlined in anticipation of future inventions in the field that will hopefully elevate IUP research to the truly proteomic level...
  50. doi request reprint Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities
    Edit Szollosi
    Institute of Enzymology, Hungarian Academy of Sciences, Budapest, Hungary
    J Proteome Res 7:2291-9. 2008
    ..Finally, we also would like to point out the utility of our 2DE/MS technique for discoveringor, as a matter of fact, rediscoveringIDPs even from the complicated proteome of an advanced eukaryote...
  51. ncbi request reprint Phosphorylation-induced transient intrinsic structure in the kinase-inducible domain of CREB facilitates its recognition by the KIX domain of CBP
    Iván Solt
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Proteins 64:749-57. 2006
    ....
  52. doi request reprint Limitations of induced folding in molecular recognition by intrinsically disordered proteins
    Eszter Hazy
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P O Box 7, 1518 Budapest, Hungary
    Chemphyschem 10:1415-9. 2009
    ..It is suggested that a new model describing the structure-function relationship of IDPs has to encompass such structural and functional promiscuity inherent in the disordered state of IDPs...
  53. ncbi request reprint A novel two-dimensional electrophoresis technique for the identification of intrinsically unstructured proteins
    Veronika Csizmok
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H 1518 Budapest, Hungary
    Mol Cell Proteomics 5:265-73. 2006
    ..Overall the reproducibility and ease of performance of this technique may promote the proteomic scale recognition and characterization of protein disorder...
  54. ncbi request reprint Large systematic errors compromise quantitation of intrinsically unstructured proteins
    E Szollosi
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518 Budapest, Hungary
    Anal Biochem 360:321-3. 2007
  55. ncbi request reprint Revisiting ubiquity and tissue specificity of human calpains
    Attila Farkas
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, PO Box 7, H 1518 Budapest, Hungary
    Biol Chem 384:945-9. 2003
    ..Therefore, the categoric classification of 'ubiquitous' vs. 'tissue-specific' calpains is a simplification...
  56. doi request reprint High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1
    Annamária Balázs
    Department of Medical Chemistry, Semmelweis University Medical School, Budapest, Hungary
    FEBS J 276:3744-56. 2009
    ....
  57. doi request reprint The androgen receptor gene polyglycine repeat polymorphism is associated with memory performance in healthy Chinese individuals
    Denes Kovacs
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H 1518 Budapest, Hungary
    Psychoneuroendocrinology 34:947-52. 2009
    ..002 for Immediate and p=0.014 for Delayed Logical Memory), but not in males (p=0.31 and 0.83, respectively). We conclude that functional variation of the androgen receptor gene is able to modulate memory function in women...
  58. ncbi request reprint Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    Monika Fuxreiter
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    J Mol Biol 338:1015-26. 2004
    ..This finding implies that IUPs draw a functional advantage from preformed structural elements, as they enable their facile, kinetically and energetically less demanding, interaction with their physiological partner...
  59. ncbi request reprint Prediction of protein disorder at the domain level
    Zsuzsanna Dosztanyi
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Curr Protein Pept Sci 8:161-71. 2007
    ..The primary focus of our review is the interpretation of prediction results in a way that enables segmentation of proteins to separate ordered domains from disordered regions...
  60. doi request reprint Prediction of protein disorder
    Zsuzsanna Dosztanyi
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Methods Mol Biol 426:103-15. 2008
    ..An emphasis is also given to a somewhat different approach, in which ordered/disordered regions are explicitly delineated to the end of making constructs amenable for structure determination even when disordered regions are present...
  61. pmc Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins
    Denes Kovacs
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary H 1113
    Plant Physiol 147:381-90. 2008
    ..We suggest that these findings provide the rationale for the mechanism of how these proteins avert the adverse effects of dehydration stresses...
  62. pmc The role of dimerization in prion replication
    Peter Tompa
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest
    Biophys J 82:1711-8. 2002
    ..We present a model including these features largely ignored so far and show that it adheres satisfactorily to the observed phenomenology of prion replication...
  63. doi request reprint Structural and dynamic characterization of intrinsically disordered human securin by NMR spectroscopy
    Veronika Csizmok
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Karolina ut 29, H 1113, Hungary
    J Am Chem Soc 130:16873-9. 2008
    ..These results, in combination with bioinformatic and biochemical data on the securin/separase interaction, shed light on the inhibitory action of securin on separase...
  64. pmc Binding-induced folding transitions in calpastatin subdomains A and C
    Zoltan Mucsi
    Department of Organic Chemistry, Eotvos Lorand University, H 1117 Budapest, Hungary
    Protein Sci 12:2327-36. 2003
    ..Taken together, these observations point to significant binding-induced local folding transitions in calpastatin, in a way that ensures highly specific, yet reversible, action of the inhibitor...
  65. pmc DisProt: the Database of Disordered Proteins
    Megan Sickmeier
    Department of Biochemistry and Molecular Biology, Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, Indianapolis, IN 46202, USA
    Nucleic Acids Res 35:D786-93. 2007
    ..In addition to being a unique source of biological information, DisProt opens doors for a plethora of bioinformatics studies. DisProt is openly available at http://www.disprot.org...