| Year |
Citation |
Score |
| 2012 |
Kókai E, Páldy FS, Somogyi K, Chougule A, Pál M, Kerekes É, Deák P, Friedrich P, Dombrádi V, Ãdám G. CalpB modulates border cell migration in Drosophila egg chambers. Bmc Developmental Biology. 12: 20. PMID 22827336 DOI: 10.1186/1471-213X-12-20 |
0.302 |
|
| 2011 |
Bozóky Z, Róna G, Klement É, Medzihradszky KF, Merényi G, Vértessy BG, Friedrich P. Calpain-catalyzed proteolysis of human dUTPase specifically removes the nuclear localization signal peptide. Plos One. 6: e19546. PMID 21625588 DOI: 10.1371/Journal.Pone.0019546 |
0.39 |
|
| 2009 |
Kovács L, Alexa A, Klement E, Kókai E, Tantos A, Gógl G, Sperka T, Medzihradszky KF, Tözsér J, Dombrádi V, Friedrich P. Regulation of calpain B from Drosophila melanogaster by phosphorylation. The Febs Journal. 276: 4959-72. PMID 19694808 DOI: 10.1111/J.1742-4658.2009.07198.X |
0.792 |
|
| 2009 |
Toke O, Bánóczi Z, Tárkányi G, Friedrich P, Hudecz F. Folding transitions in calpain activator peptides studied by solution NMR spectroscopy. Journal of Peptide Science : An Official Publication of the European Peptide Society. 15: 404-10. PMID 19378261 DOI: 10.1002/Psc.1131 |
0.38 |
|
| 2009 |
Tantos A, Friedrich P, Tompa P. Cold stability of intrinsically disordered proteins. Febs Letters. 583: 465-9. PMID 19121309 DOI: 10.1016/J.Febslet.2008.12.054 |
0.766 |
|
| 2009 |
Bozoky Z, Alexa A, Dancsok J, Gogl G, Klement E, Medzihradszky KF, Friedrich P. Identifying calpain substrates in intact S2 cells of Drosophila. Archives of Biochemistry and Biophysics. 481: 219-25. PMID 19038228 DOI: 10.1016/J.Abb.2008.11.011 |
0.382 |
|
| 2008 |
Világi I, Kiss DS, Farkas A, Borbély S, Tárnok K, Halasy K, Bánóczi Z, Hudecz F, Friedrich P. Synthetic calpain activator boosts neuronal excitability without extra Ca2+. Molecular and Cellular Neurosciences. 38: 629-36. PMID 18599308 DOI: 10.1016/J.Mcn.2008.05.012 |
0.352 |
|
| 2008 |
Bánóczi Z, Alexa A, Farkas A, Friedrich P, Hudecz F. Novel cell-penetrating calpain substrate. Bioconjugate Chemistry. 19: 1375-81. PMID 18529021 DOI: 10.1021/Bc800021Y |
0.35 |
|
| 2008 |
Kiss R, Bozoky Z, Kovács D, Róna G, Friedrich P, Dvortsák P, Weisemann R, Weisemann R, Tompa P, Perczel A. Calcium-induced tripartite binding of intrinsically disordered calpastatin to its cognate enzyme, calpain. Febs Letters. 582: 2149-54. PMID 18519038 DOI: 10.1016/J.Febslet.2008.05.032 |
0.647 |
|
| 2008 |
Kiss R, Bozoky Z, Kovács D, Róna G, Friedrich P, Dvortsák P, Weisemann R, Tompa P, Perczel A. Corrigendum to “Calcium‐induced tripartite binding of intrinsically disordered calpastatin to its cognate enzyme, calpain” [FEBS Lett. 582 (2008) 2149–2154] Febs Letters. 582: 2816-2816. DOI: 10.1016/J.Febslet.2008.06.032 |
0.619 |
|
| 2007 |
Banóczi Z, Tantos A, Farkas A, Tompa P, Friedrich P, Hudecz F. Synthesis of cell-penetrating conjugates of calpain activator peptides. Bioconjugate Chemistry. 18: 130-7. PMID 17226965 DOI: 10.1021/Bc0601976 |
0.773 |
|
| 2006 |
Kókai E, Tantos A, Vissi E, Szöor B, Tompa P, Gausz J, Alphey L, Friedrich P, Dombrádi V. CG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y. Archives of Biochemistry and Biophysics. 451: 59-67. PMID 16631104 DOI: 10.1016/J.Abb.2006.03.020 |
0.78 |
|
| 2006 |
Csizmók V, Szollosi E, Friedrich P, Tompa P. A novel two-dimensional electrophoresis technique for the identification of intrinsically unstructured proteins. Molecular & Cellular Proteomics : McP. 5: 265-73. PMID 16223749 DOI: 10.1074/Mcp.M500181-Mcp200 |
0.74 |
|
| 2005 |
Friedrich P, Bozóky Z. Digestive versus regulatory proteases: on calpain action in vivo. Biological Chemistry. 386: 609-12. PMID 16207081 DOI: 10.1515/Bc.2005.071 |
0.425 |
|
| 2005 |
Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P. Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. Biochemistry. 44: 3955-64. PMID 15751971 DOI: 10.1021/Bi047817F |
0.752 |
|
| 2005 |
Bokor M, Csizmók V, Kovács D, Bánki P, Friedrich P, Tompa P, Tompa K. NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins. Biophysical Journal. 88: 2030-7. PMID 15613629 DOI: 10.1529/Biophysj.104.051912 |
0.742 |
|
| 2005 |
Bozóky Z, Alexa A, Tompa P, Friedrich P. Multiple interactions of the 'transducer' govern its function in calpain activation by Ca2+. The Biochemical Journal. 388: 741-4. PMID 15569003 DOI: 10.1042/Bj20041935 |
0.765 |
|
| 2004 |
Friedrich P. The intriguing Ca2+ requirement of calpain activation. Biochemical and Biophysical Research Communications. 323: 1131-3. PMID 15451413 DOI: 10.1016/J.Bbrc.2004.08.194 |
0.381 |
|
| 2004 |
Farkas B, Tantos A, Schlett K, Világi I, Friedrich P. Ischemia-induced increase in long-term potentiation is warded off by specific calpain inhibitor PD150606. Brain Research. 1024: 150-8. PMID 15451377 DOI: 10.1016/J.Brainres.2004.07.059 |
0.76 |
|
| 2004 |
Friedrich P, Tompa P, Farkas A. The calpain-system of Drosophila melanogaster: coming of age. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 26: 1088-96. PMID 15382138 DOI: 10.1002/Bies.20106 |
0.762 |
|
| 2004 |
Farkas A, Nardai G, Csermely P, Tompa P, Friedrich P. DUK114, the Drosophila orthologue of bovine brain calpain activator protein, is a molecular chaperone. The Biochemical Journal. 383: 165-70. PMID 15250825 DOI: 10.1042/Bj20040668 |
0.748 |
|
| 2004 |
Fuxreiter M, Simon I, Friedrich P, Tompa P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. Journal of Molecular Biology. 338: 1015-26. PMID 15111064 DOI: 10.1016/J.Jmb.2004.03.017 |
0.739 |
|
| 2004 |
Friedrich P, Papp H, Halasy K, Farkas A, Farkas B, Tompa P, Kása P. Differential distribution of calpain small subunit 1 and 2 in rat brain. The European Journal of Neuroscience. 19: 1819-25. PMID 15078555 DOI: 10.1111/J.1460-9568.2004.03313.X |
0.736 |
|
| 2004 |
Jánossy J, Ubezio P, Apáti A, Magócsi M, Tompa P, Friedrich P. Calpain as a multi-site regulator of cell cycle. Biochemical Pharmacology. 67: 1513-21. PMID 15041468 DOI: 10.1016/J.Bcp.2003.12.021 |
0.732 |
|
| 2004 |
Tompa P, Buzder-Lantos P, Tantos A, Farkas A, Szilágyi A, Bánóczi Z, Hudecz F, Friedrich P. On the sequential determinants of calpain cleavage. The Journal of Biological Chemistry. 279: 20775-85. PMID 14988399 DOI: 10.1074/Jbc.M313873200 |
0.769 |
|
| 2004 |
Alexa A, Bozóky Z, Farkas A, Tompa P, Friedrich P. Contribution of distinct structural elements to activation of calpain by Ca2+ ions. The Journal of Biological Chemistry. 279: 20118-26. PMID 14976200 DOI: 10.1074/Jbc.M311969200 |
0.761 |
|
| 2004 |
Farkas A, Tompa P, Schád E, Sinka R, Jékely G, Friedrich P. Autolytic activation and localization in Schneider cells (S2) of calpain B from Drosophila. The Biochemical Journal. 378: 299-305. PMID 14614768 DOI: 10.1042/Bj20031310 |
0.764 |
|
| 2003 |
Mucsi Z, Hudecz F, Hollósi M, Tompa P, Friedrich P. Binding-induced folding transitions in calpastatin subdomains A and C. Protein Science : a Publication of the Protein Society. 12: 2327-36. PMID 14500891 DOI: 10.1110/Ps.03138803 |
0.758 |
|
| 2003 |
Farkas A, Tompa P, Friedrich P. Revisiting ubiquity and tissue specificity of human calpains. Biological Chemistry. 384: 945-9. PMID 12887062 DOI: 10.1515/Bc.2003.106 |
0.727 |
|
| 2003 |
Spadoni C, Farkas A, Sinka R, Tompa P, Friedrich P. Molecular cloning and RNA expression of a novel Drosophila calpain, Calpain C. Biochemical and Biophysical Research Communications. 303: 343-9. PMID 12646209 DOI: 10.1016/S0006-291X(03)00350-4 |
0.754 |
|
| 2002 |
Alexa A, Schmidt G, Tompa P, Ogueta S, Vázquez J, Kulcsár P, Kovács J, Dombrádi V, Friedrich P. 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. 41: 12427-35. PMID 12369833 DOI: 10.1021/Bi025916S |
0.641 |
|
| 2002 |
Tompa P, Tusnády GE, Friedrich P, Simon I. The role of dimerization in prion replication. Biophysical Journal. 82: 1711-8. PMID 11916832 DOI: 10.1016/S0006-3495(02)75523-9 |
0.723 |
|
| 2002 |
Schád E, Farkas A, Jékely G, Tompa P, Friedrich P. A novel human small subunit of calpains. The Biochemical Journal. 362: 383-8. PMID 11853546 DOI: 10.1042/0264-6021:3620383 |
0.774 |
|
| 2002 |
Tompa P, Mucsi Z, Orosz G, Friedrich P. Calpastatin subdomains A and C are activators of calpain. The Journal of Biological Chemistry. 277: 9022-6. PMID 11809743 DOI: 10.1074/Jbc.C100700200 |
0.763 |
|
| 2001 |
Tompa P, Töth-Boconádi R, Friedrich P. Frequency decoding of fast calcium oscillations by calpain. Cell Calcium. 29: 161-70. PMID 11162853 DOI: 10.1054/ceca.2000.0179 |
0.595 |
|
| 2001 |
Tompa P, Emori Y, Sorimachi H, Suzuki K, Friedrich P. Domain III of calpain is a ca2+-regulated phospholipid-binding domain. Biochemical and Biophysical Research Communications. 280: 1333-9. PMID 11162675 DOI: 10.1006/Bbrc.2001.4279 |
0.644 |
|
| 2000 |
Wronski R, Tompa P, Hutter-Paier B, Crailsheim K, Friedrich P, Windisch M. Inhibitory effect of a brain derived peptide preparation on the Ca++-dependent protease, calpain. Journal of Neural Transmission (Vienna, Austria : 1996). 107: 145-57. PMID 10847556 DOI: 10.1007/s007020050013 |
0.653 |
|
| 2000 |
Tompa P, Schád E, Friedrich P. A sensitive and continuous fluorometric activity assay using a natural substrate. Microtubule-associated protein 2. Methods in Molecular Biology (Clifton, N.J.). 144: 137-41. PMID 10818758 DOI: 10.1385/1-59259-050-0:137 |
0.648 |
|
| 2000 |
Tompa P, Friedrich P. Kinetic analysis of human mu-calpain autolysis. Methods in Molecular Biology (Clifton, N.J.). 144: 129-36. PMID 10818757 DOI: 10.1385/1-59259-050-0:129 |
0.584 |
|
| 2000 |
Jékely G, Pintér M, Friedrich P. Drosophila calpains. Purification of a calpain-like enzyme from fruit flies, and expression in Escherichia coli. Methods in Molecular Biology (Clifton, N.J.). 144: 67-74. PMID 10818749 DOI: 10.1385/1-59259-050-0:67 |
0.317 |
|
| 1999 |
Jékely G, Friedrich P. Characterization of two recombinant Drosophila calpains. CALPA and a novel homolog, CALPB. The Journal of Biological Chemistry. 274: 23893-900. PMID 10446155 DOI: 10.1074/Jbc.274.34.23893 |
0.43 |
|
| 1998 |
Tompa P, Friedrich P. Prion proteins as memory molecules: an hypothesis. Neuroscience. 86: 1037-43. PMID 9697111 DOI: 10.1016/S0306-4522(98)00148-1 |
0.602 |
|
| 1998 |
Pintér M, Jékely G, Szepesi RJ, Farkas A, Theopold U, Meyer HE, Lindholm D, Nässel DR, Hultmark D, Friedrich P. TER94, a Drosophila homolog of the membrane fusion protein CDC48/p97, is accumulated in nonproliferating cells: in the reproductive organs and in the brain of the imago. Insect Biochemistry and Molecular Biology. 28: 91-8. PMID 9639875 DOI: 10.1016/S0965-1748(97)00095-7 |
0.306 |
|
| 1998 |
Tompa P, Friedrich P. Synaptic metaplasticity and the local charge effect in postsynaptic densities. Trends in Neurosciences. 21: 97-102. PMID 9530914 DOI: 10.1016/S0166-2236(97)01176-4 |
0.611 |
|
| 1996 |
Tompa P, Baki A, Schád E, Friedrich P. The calpain cascade. Mu-calpain activates m-calpain. The Journal of Biological Chemistry. 271: 33161-4. PMID 8969168 DOI: 10.1074/Jbc.271.52.33161 |
0.641 |
|
| 1996 |
Sánchez C, Tompa P, Szücs K, Friedrich P, Avila J. Phosphorylation and dephosphorylation in the proline-rich C-terminal domain of microtubule-associated protein 2. European Journal of Biochemistry / Febs. 241: 765-71. PMID 8944764 DOI: 10.1111/J.1432-1033.1996.00765.X |
0.636 |
|
| 1996 |
Baki A, Tompa P, Alexa A, Molnár O, Friedrich P. Autolysis parallels activation of mu-calpain. The Biochemical Journal. 318: 897-901. PMID 8836135 DOI: 10.1042/Bj3180897 |
0.655 |
|
| 1996 |
Alexa A, Tompa P, Baki A, Vereb G, Friedrich P. Mutual protection of microtubule-associated protein 2 (MAP2) and cyclic AMP-dependent protein kinase II against mu-calpain. Journal of Neuroscience Research. 44: 438-45. PMID 8776665 DOI: 10.1002/(Sici)1097-4547(19960601)44:5<438::Aid-Jnr4>3.0.Co;2-G |
0.639 |
|
| 1995 |
Tompa P, Schád E, Baki A, Alexa A, Batke J, Friedrich P. An ultrasensitive, continuous fluorometric assay for calpain activity. Analytical Biochemistry. 228: 287-93. PMID 8572308 DOI: 10.1006/Abio.1995.1352 |
0.649 |
|
| 1994 |
Szücs K, Ledesma MD, Dombrádi V, Gergely P, Avila J, Friedrich P. Dephosphorylation of tau protein from Alzheimer's disease patients. Neuroscience Letters. 165: 175-8. PMID 7517023 DOI: 10.1016/0304-3940(94)90738-2 |
0.325 |
|
| 1993 |
Ulloa L, Dombrádi V, DÃaz-Nido J, Szücs K, Gergely P, Friedrich P, Avila J. Dephosphorylation of distinct sites on microtubule-associated protein MAP1B by protein phosphatases 1, 2A and 2B. Febs Letters. 330: 85-9. PMID 7690334 DOI: 10.1016/0014-5793(93)80925-K |
0.329 |
|
| 1992 |
Pintér M, Stierandova A, Friedrich P. Purification and characterization of a Ca(2+)-activated thiol protease from Drosophila melanogaster. Biochemistry. 31: 8201-6. PMID 1525160 DOI: 10.1021/Bi00150A012 |
0.391 |
|
| 1992 |
Friedrich P, Aszadi A. Calcium-dependent proteolysis and isopeptide bond formation: Calpains and transglutaminases Pure and Applied Chemistry. 64: 1093-1097. DOI: 10.1351/Pac199264081093 |
0.387 |
|
| 1991 |
Friedrich P, Aszódi A. MAP2: a sensitive cross-linker and adjustable spacer in dendritic architecture. Febs Letters. 295: 5-9. PMID 1765166 DOI: 10.1016/0014-5793(91)81371-E |
0.3 |
|
| 1991 |
Aszódi A, Müller U, Friedrich P, Spatz HC. Signal convergence on protein kinase A as a molecular correlate of learning. Proceedings of the National Academy of Sciences of the United States of America. 88: 5832-6. PMID 1648232 DOI: 10.1073/Pnas.88.13.5832 |
0.34 |
|
| 1989 |
Friedrich P, Aszódi A. Cyclic AMP turnover and signal amplification. The Biochemical Journal. 257: 621-3. PMID 16744553 DOI: 10.1042/Bj2570621B |
0.544 |
|
| 1989 |
Dévay P, Pintér M, Kiss I, Faragó A, Friedrich P. Protein kinase C in larval brain of wild-type and dunce memory-mutant Drosophila. Journal of Neurogenetics. 5: 119-26. PMID 2500506 DOI: 10.3109/01677068909066202 |
0.36 |
|
| 1988 |
Risnik VV, Adám G, Gusev NB, Friedrich P. Casein kinases I and II bound to pig brain microtubules. Cellular and Molecular Neurobiology. 8: 315-24. PMID 3224359 DOI: 10.1007/Bf00711173 |
0.301 |
|
| 1988 |
Pintér M, Friedrich P. The calcium-dependent proteolytic system calpain-calpastatin in Drosophila melanogaster. The Biochemical Journal. 253: 467-73. PMID 2845920 DOI: 10.1042/Bj2530467 |
0.386 |
|
| 1988 |
Adám G, Friedrich P. Microtubule-associated cyclic AMP-dependent protein kinase in Drosophila melanogaster. Journal of Neurochemistry. 51: 1014-22. PMID 2843603 DOI: 10.1111/J.1471-4159.1988.Tb03062.X |
0.373 |
|
| 1987 |
Friedrich P, Hajdu J. An overview of supramolecular enzyme organization. Biochemical Society Transactions. 15: 973-7. PMID 3691951 DOI: 10.1042/Bst0150973 |
0.496 |
|
| 1987 |
Dombrádi V, Gergely P, Bot G, Friedrich P. Purification of the catalytic subunit of protein phosphatase-1 from Drosophila melanogaster. Biochemical and Biophysical Research Communications. 144: 1175-81. PMID 3034274 DOI: 10.1016/0006-291X(87)91435-5 |
0.337 |
|
| 1987 |
Dévay P, Friedrich P. Cyclic AMP-induced phosphorylation of 27.5-kDa protein(s) in larval brains of normal and memory-mutant Drosophila melanogaster. Journal of Neurogenetics. 4: 275-84. PMID 2831325 DOI: 10.3109/01677068709102348 |
0.315 |
|
| 1987 |
Dombrádi V, Friedrich P, Bot G. Protein phosphatases type 1 and type 2 in Drosophila melanogaster Comparative Biochemistry and Physiology -- Part B: Biochemistry And. 87: 857-861. DOI: 10.1016/0305-0491(87)90402-0 |
0.356 |
|
| 1987 |
Dombrádi V, Risnik V, Erdödi F, Bot G, Friedrich P. Regulation of phosphorylase kinase in Drosophila melanogaster Insect Biochemistry. 17: 579-585. DOI: 10.1016/0020-1790(87)90057-6 |
0.32 |
|
| 1986 |
Kareva VV, Dobrovol'sky AB, Baratova LA, Friedrich P, Gusev NB. Ca2+-induced structural change in the Ca2+/Mg2+ domain of troponin C detected by crosslinking. Biochimica Et Biophysica Acta. 869: 322-9. PMID 3947641 DOI: 10.1016/0167-4838(86)90072-5 |
0.334 |
|
| 1986 |
Dombrádi V, Matkó J, Kiss Z, Kiss L, Friedrich P, Bot G. Structural and functional properties of Drosophila melanogaster phosphorylase: comparison with the rabbit skeletal muscle enzyme. Comparative Biochemistry and Physiology. B, Comparative Biochemistry. 84: 537-43. PMID 3093145 DOI: 10.1016/0305-0491(86)90119-7 |
0.354 |
|
| 1986 |
Dombrádi V, Dévay P, Friedrich P, Bot G. Regulation of glycogen phosphorylase in Drosophila melanogaster by reversible phosphorylation-dephosphorylation Insect Biochemistry. 16: 557-565. DOI: 10.1016/0020-1790(86)90033-8 |
0.37 |
|
| 1985 |
Dombrádi V, Hajdu J, Friedrich P, Bot G. Purification and characterization of glycogen phosphorylase from Drosophila melanogaster Insect Biochemistry. 15: 403-410. DOI: 10.1016/0020-1790(85)90032-0 |
0.533 |
|
| 1984 |
Dobrovol'sky AB, Gusev NB, Friedrich P. Crosslinking of troponin complex with 1,3-difluoro-4,6-dinitrobenzene. Identification of the crosslink formed between troponin C and troponin I in the absence of Ca2+. Biochimica Et Biophysica Acta. 789: 144-51. PMID 6477927 DOI: 10.1016/0167-4838(84)90198-5 |
0.316 |
|
| 1984 |
Dévay P, Solti M, Kiss I, Dombrádi, Friedrich P. Differences in protein phosphorylation in vivo and in vitro between wild type and dunce mutant strains of Drosophila melanogaster. The International Journal of Biochemistry. 16: 1401-8. PMID 6442236 DOI: 10.1016/0020-711X(84)90248-9 |
0.302 |
|
| 1983 |
Solti M, Dévay P, Kiss I, Londesborough J, Friedrich P. Cyclic nucleotide phosphodiesterases in larval brain of wild type and dunce mutant strains of Drosophila melanogaster: isoenzyme pattern and activation by Ca2+/calmodulin. Biochemical and Biophysical Research Communications. 111: 652-8. PMID 6301474 DOI: 10.1016/0006-291X(83)90356-X |
0.331 |
|
| 1982 |
Dombrádi V, Tóth B, Bot G, Hajdu J, Friedrich P. Interaction of ligands in phosphorylase A as monitored by crosslinking and enzymatic modifications: synergism of glucose and caffeine manifested in the exposure of N-terminal segment. The International Journal of Biochemistry. 14: 277-84. PMID 7067907 DOI: 10.1016/0020-711X(82)90088-X |
0.491 |
|
| 1981 |
Vas M, Lakatos S, Hajdu J, Friedrich P. Kinetic behaviour and oligomeric state of 3-phosphoglyceroyl-D-glyceraldehyde-3-phosphate dehydrogenase. Biochimie. 63: 89-96. PMID 7225461 |
0.481 |
|
| 1981 |
Dombrádi V, Tóth B, Bot G, Hajdu J, Friedrich P. SYNERGISM IN EXPOSURE OF N-TERMINAL SEGMENT IN GLYCOGEN PHOSPHORYLASE a Biochemical Society Transactions. 9: 158P-158P. DOI: 10.1042/Bst009158Pd |
0.462 |
|
| 1980 |
Dombrádi V, Hajdu J, Bot G, Friedrich P. Structural changes in glycogen phosphorylase as revealed by cross-linking with bifunctional diimidates: phospho-dephospho hybrid and phosphorylase a. Biochemistry. 19: 2295-9. PMID 7387975 DOI: 10.1021/Bi00552A002 |
0.54 |
|
| 1980 |
Gusev NB, Friedrich P. Ca2+-induced conformational changes in the troponin complex detected by crosslinking. Biochimica Et Biophysica Acta. 626: 106-16. PMID 6779874 DOI: 10.1016/0005-2795(80)90202-0 |
0.335 |
|
| 1979 |
Gusev NB, Hajdu J, Friedrich P. Motility of the N-terminal tail of phosphorylase b as revealed by crosslinking. Biochemical and Biophysical Research Communications. 90: 70-7. PMID 496993 DOI: 10.1016/0006-291X(79)91591-2 |
0.524 |
|
| 1979 |
Friedrich P. On the physiological significance of positive and negative cooperativity in enzymes. Journal of Theoretical Biology. 81: 527-32. PMID 231712 DOI: 10.1016/0022-5193(79)90050-X |
0.318 |
|
| 1979 |
Hajdu J, Dombrádi V, Bot G, Friedrich P. Structural changes in glycogen phosphorlase as revealed by cross-linking with bifunctional diimidates: phosphorylase b. Biochemistry. 18: 4037-41. PMID 226120 DOI: 10.1021/Bi00585A030 |
0.488 |
|
| 1979 |
Solti M, Friedrich P. The 'enzyme-probe' method for characterizing metabolite pools. The use of NAD-glycohydrolase in human erythrocyte sonicate as a model system. European Journal of Biochemistry / Febs. 95: 551-9. PMID 221219 DOI: 10.1111/J.1432-1033.1979.Tb12996.X |
0.322 |
|
| 1976 |
Solti M, Friedrich P. Partial reversible inactivation of enzymes due to binding to the human erythrocyte membrane. Molecular and Cellular Biochemistry. 10: 145-52. PMID 1264075 DOI: 10.1007/Bf01731685 |
0.324 |
|
| 1976 |
Hajdu J, Bartha F, Friedrich P. Crosslinking with bifunctional reagents as a means for studying the symmetry of oligomeric proteins. European Journal of Biochemistry / Febs. 68: 373-83. PMID 987906 DOI: 10.1111/J.1432-1033.1976.Tb10824.X |
0.537 |
|
| 1975 |
Hajdu J, Solti M, Friedrich P. Cross-linking and coupling of rabbit muscle aldolase and glyceraldehyde-3-phosphate dehydrogenase by glutaraldehyde. Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae. 10: 7-16. PMID 807079 |
0.481 |
|
| 1975 |
Hajdu J, Friedrich P. Reaction of glutaraldehyde with NH2 compounds. A spectrophotometric method for the determination of glutaraldehyde concentration. Analytical Biochemistry. 65: 273-80. PMID 236693 DOI: 10.1016/0003-2697(75)90510-2 |
0.463 |
|
| 1973 |
Földi J, Szabolcsi G, Friedrich P. Interaction of glycolytic enzymes: increase of the apparent molecular weight of aldolase in rabbit muscle extract. Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae. 8: 263-5. PMID 4784605 |
0.687 |
|
| 1970 |
Szajáni B, Sajgó M, Biszku E, Friedrich P, Szabolcsi G. Identification of a cysteinyl residue involved in the activity of rabbit muscle aldolase. European Journal of Biochemistry / Febs. 15: 171-8. PMID 5489834 DOI: 10.1111/J.1432-1033.1970.Tb00992.X |
0.743 |
|
| 1969 |
Szajáni B, Friedrich P, Szabolcsi G. Inhibition of rabbit skeletal muscle aldolase by an alkylating agent. Acta Biochimica Et Biophysica; Academiae Scientiarum Hungaricae. 4: 265-72. PMID 5367475 |
0.666 |
|
| 1964 |
FRIEDRICH P, POLGAR L, SZABOLCSI G. THE EXISTENCE OF A HISTIDINE RESIDUE ESSENTIAL FOR GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE ACTION. Acta Physiologica Academiae Scientiarum Hungaricae. 25: 217-28. PMID 14239413 |
0.707 |
|
| 1964 |
Friedrich P, Polgár L, Szabolcsi G. Effect of photo-oxidation on glyceraldehyde-3-phosphate Dehydrogenase Nature. 202: 1214-1215. DOI: 10.1038/2021214A0 |
0.712 |
|
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