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1.

001-es BibID:BIBFORM038449
Első szerző:Batista, Cesar V. F.
Cím:Two novel toxins from the Amazonian scorpion Tityus cambridgei that block Kv1.3 and Shaker B K(+)-channels with distinctly different affinities / Cesar V. F. Batista, Froylan Gómez-Lagunas, Ricardo C. Rodriguez de la Vega, Péter Hajdu, György Panyi, Rezső Gáspár, Lourival D. Possani
Dátum:2002
ISSN:1570-9639
Megjegyzések:Two novel toxic peptides (Tc30 and Tc32) were isolated and characterized from the venom of the Brazilian scorpion Tityus cambridgei. The first have 37 and the second 35 amino acid residues, with molecular masses of 3,871.8 and 3,521.5, respectively. Both contain three disulfide bridges but share only 27% identity. They are relatively potent inhibitors of K(+)-currents in human T lymphocytes with K(d) values of 10 nM for Tc32 and 16 nM for Tc30, but they are less potent or quite poor blockers of Shaker B K(+)-channels, with respective K(d) values of 74 nM and 4.7 microM. Tc30 has a lysine in position 27 and a tyrosine at position 36 identical to those of charybdotoxin. These two positions conform the dyad considered essential for activity. On the contrary, Tc32 has a serine in the position equivalent to lysine 27 of charybdotoxin and does not contain any aromatic amino acid. Due to its unique primary sequence and to its distinctive preference for K(+)-channels of T lymphocytes, it was classified as the first example of a new subfamily of K(+)-channel-specific peptides (alpha-KT x 18.1). Tc30 is a member of the Tityus toxin II-9 subfamily and was given the number alpha-KT x 4.4.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1601 : 2 (2002), p. 123-131. -
További szerzők:Gómez-Lagunas, Froylan Rodriguez de la Vega, Ricardo C. Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos
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2.

001-es BibID:BIBFORM055232
035-os BibID:Article ID: e24157
Első szerző:Dunker, A. Keith
Cím:What's in a name? : Why these proteins are intrinsically disordered / A. Keith Dunker, M. Madan Babu, Elisar Barbar, Martin Blackledge, Sarah E. Bondos, Zsuzsanna Dosztányi, H. Jane Dyson, Julie Forman-Kay, Monika Fuxreiter, Jörg Gsponer, Kyou-Hoon Han, David T. Jones, Sonia Longhi, Steven J. Metallo, Ken Nishikawa, Ruth Nussinov, Zoran Obradovic, Rohit V. Pappu, Burkhard Rost, Philipp Selenko, Vinod Subramaniam, Joel L. Sussman, Peter Tompa, Vladimir N. Uversky
Dátum:2013
ISSN:2169-0693 2169-0707
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény hazai lapban
Megjelenés:Intrinsically Disordered Proteins. - 1 : 1 (2013), [5] p. -
További szerzők:Babu, M. Madan Barbar, Elisar Blackledge, Martin Bondos, Sarah E. Dosztányi Zsuzsanna Dyson, H. Jane Forman-Kay, Julie Fuxreiter Mónika (1969-) (kutató vegyész) Gsponer, Joerg Han, Kyou-Hoon Jones, David T. W. Longhi, Sonia Metallo, Steven J. Nishikawa, Ken Nussinov, Ruth Obradovic, Zoran Pappu, Rohit V. Rost, Burkhard Selenko, Philipp Subramaniam, Vinod Sussman, Joel L. Tompa Péter Uversky, Vladimir N.
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3.

001-es BibID:BIBFORM114859
035-os BibID:(cikkazonosító)140952 (scopus)85170288156
Első szerző:Elnahriry, Khaled A.
Cím:Structural and functional characterisation of Tst2, a novel TRPV1 inhibitory peptide from the Australian sea anemone Telmatactis stephensoni / Elnahriry Khaled A., Wai Dorothy C. C., Ashwood Lauren M., Naseem Muhammad Umair, Szanto Tibor G., Guo Shaodong, Panyi Gyorgy, Prentis Peter J., Norton Raymond S.
Dátum:2024
ISSN:1570-9639
Megjegyzések:Sea anemone venoms are complex mixtures of biologically active compounds, including disulfide-rich peptides, some of which have found applications as research tools, and others as therapeutic leads. Our recent transcriptomic and proteomic studies of the Australian sea anemone Telmatactis stephensoni identified a transcript for a peptide designated Tst2. Tst2 is a 38-residue peptide showing sequence similarity to peptide toxins known to interact with a range of ion channels (NaV, TRPV1, KV and CaV). Recombinant Tst2 (rTst2, which contains an additional Gly at the N-terminus) was produced by periplasmic expression in Escherichia coli, enabling the production of both unlabelled and uniformly 13C,15N?labelled peptide for functional assays and structural studies. The LC-MS profile of the recombinant Tst2 showed a pure peak with molecular mass 6 Da less than that of the reduced form of the peptide, indicating the successful formation of three disulfide bonds from its six cysteine residues. The solution structure of rTst2 was determined using multidimensional NMR spectroscopy and revealed that rTst2 adopts an inhibitor cystine knot (ICK) structure. rTst2 was screened using various functional assays, including patch?clamp electrophysiological and cytotoxicity assays. rTst2 was inactive against voltagegated sodium channels (NaV) and the human voltage-gated proton (hHv1) channel. rTst2 also did not possess cytotoxic activity when assessed against Drosophila melanogaster flies. However, the recombinant peptide at 100 nM showed >50% inhibition of the transient receptor potential subfamily V member 1 (TRPV1) and slight (~10%) inhibition of transient receptor potential subfamily A member 1 (TRPA1). Tst2 is thus a novel ICK inhibitor of the TRPV1 channel.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Sea anemone
Disulfide-rich peptides
Recombinant expression
NMR spectroscopy
ICK scaffold
TRPV1 channel
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1872 : 1 (2024), p. 1-13. -
További szerzők:Wai, Dorothy C. C. Ashwood, Lauren M. Naseem, Muhammad Umair (1993-) (biofizikus, molekuláris biológus) Szántó Gábor Tibor (1980-) (vegyész) Guo, Shaodong Panyi György (1966-) (biofizikus) Prentis, Peter Norton, Raymond S.
Pályázati támogatás:K143071
OTKA
Stipendium Hungaricum Scholarship from the Tempus Public Foundation
Egyéb
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4.

001-es BibID:BIBFORM003891
Első szerző:Gyémánt Gyöngyi (vegyész)
Cím:Evidence for pentagalloyl glucose binding to human salivary α-amylase through aromatic amino acid residues / Gyöngyi Gyémánt, Ágnes Zajácz, Bálint Bécsi, Chandran Ragunath, Narayanan Ramasubbu, Ferenc Erdődi, Gyula Batta, Lili Kandra
Dátum:2009
ISSN:1570-9639
Megjegyzések:We demonstrate here that pentagalloyl glucose (PGG), a main component of gallotannins, was an effective inhibitor of HSA and it exerted similar inhibitory potency to Aleppo tannin used in this study. The inhibition of HSA by PGG was found to be non-competitive and inhibitory constants of KEI = 2.6 ?M and KESI = 3.9 ?M were determined from Lineweaver-Burk secondary plots. PGG as a model compound for gallotannins was selected to study the inhibitory mechanism and to characterize the interaction of HSA with this type of molecules. Surface plasmon resonance (SPR) binding experiments confirmed the direct interaction of HSA and PGG, and it also established similar binding of Aleppo tannin to HSA. Saturation transfer difference (STD) experiment by NMR clearly demonstrated the aromatic rings of PGG may be involved in the interaction suggesting a possible stacking with the aromatic side chains of HSA. The role of aromatic amino acids of HSA in PGG binding was reinforced by kinetic studies with the W58L and Y151M mutants of HSA: the replacement of the active site aromatic amino acids with aliphatic ones decreased the PGG inhibition dramatically, which justified the importance of these residues in the interaction.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Molekulatudomány
pentagalloyl glucose
human salivary alpha-amylase inhibition
surface plasmon resonance
saturation transfer difference
NMR
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1794 : 2 (2009), p. 291-296. -
További szerzők:Zajácz Ágnes Bécsi Bálint (1981-) (vegyészmérnök) Ragunath, Chandran Ramasubbu, Narayanan Erdődi Ferenc (1953-) (biokémikus) Batta Gyula (1953-) (molekula-szerkezet kutató) Kandra Lili (1943-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.2-08/1-2008-0019
TÁMOP
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5.

001-es BibID:BIBFORM003913
Első szerző:Mádi András (biológus)
Cím:Mass spectrometric proteome analysis suggests anaerobic shift in metabolism of Dauer larvae of Caenorhabditis elegans / András Mádi, Stefan Mikkat, Cornelia Koy, Bruno Ringel, Hans-Jürgen Thiesen, Michael O. Glocker
Dátum:2008
ISSN:1570-9639
Megjegyzések:The Dauer larva is a non-feeding alternative larval stage of some nematodes specialized for long-term survival and dispersal. In this study we compared proteome maps obtained from Dauer larvae with those from the corresponding third larval stage (L3) of the feeding life cycle of C. elegans wild-type strain N2. We demonstrate at the protein level that altered metabolism may participate in longevity determination of Dauers. We detected huge amounts of alcohol dehydrogenase (CE12212) and aldehyde dehydrogenase (CE29809) in Dauer animals, indicating highly active fermentative pathways. Inorganic pyrophosphatase (CE05448) that enables to metabolize pyrophosphate as a high-energy source was over-expressed in Dauers. An interesting differentially expressed protein was phosphatidylethanolamine-binding protein (CE38516) that was found in high abundance in samples from Dauer larvae. Protein synthesis may be lowered in Dauer animals by the reduced expression of splicing factor rsp-3 (CE31089) and methionyl-tRNA synthase (CE34219). We observed significantly lower amounts of the pepsin-like aspartyl protease 1 (CE21681) in non-feeding Dauers, which is in agreement with reduced nutrient digestion. Finally, the hypothetical protein R08E5.2 (CE33294) was present in high abundance in L3 animals.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Metabolism
Fractionated protein extraction
Proteomics
MALDI ToF MS
C. elegans
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1784 : 11 (2008), p. 1763-1770. -
További szerzők:Mikkat, Stefan Koy, Cornelia Ringel, Bruno Thiesen, Hans-Jürgen Glocker, Michael O.
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6.

001-es BibID:BIBFORM040670
Első szerző:Mahalingam, Bhuvaneshwari
Cím:Combining mutations in HIV-1 protease to understand mechanisms of resistance / Mahalingam Bhuvaneshwari, Boross Peter, Wang Yuan-Fang, Louis John M., Fischer Christopher C., Tozser Jozsef, Harrison Robert W., Weber Irene T.
Dátum:2002
ISSN:0887-3585
Megjegyzések:HIV-1 develops resistance to protease inhibitors predominantly by selecting mutations in the protease gene. Studies of resistant mutants of HIV-1 protease with single amino acid substitutions have shown a range of independent effects on specificity, inhibition, and stability. Four double mutants, K45I/L90M, K45I/V82S, D30N/V82S, and N88D/L90M were selected for analysis on the basis of observations of increased or decreased stability or enzymatic activity for the respective single mutants. The double mutants were assayed for catalysis, inhibition, and stability. Crystal structures were analyzed for the double mutants at resolutions of 2.2-1.2 A to determine the associated molecular changes. Sequence-dependent changes in protease-inhibitor interactions were observed in the crystal structures. Mutations D30N, K45I, and V82S showed altered interactions with inhibitor residues at P2/P2', P3/P3'/P4/P4', and P1/P1', respectively. One of the conformations of Met90 in K45I/L90M has an unfavorably close contact with the carbonyl oxygen of Asp25, as observed previously in the L90M single mutant. The observed catalytic efficiency and inhibition for the double mutants depended on the specific substrate or inhibitor. In particular, large variation in cleavage of p6(pol)-PR substrate was observed, which is likely to result in defects in the maturation of the protease from the Gag-Pol precursor and hence viral replication. Three of the double mutants showed values for stability that were intermediate between the values observed for the respective single mutants. D30N/V82S mutant showed lower stability than either of the two individual mutations, which is possibly due to concerted changes in the central P2-P2' and S2-S2' sites. The complex effects of combining mutations are discussed.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Proteins-Structure Function And Bioinformatics. - 48 : 1 (2002), p. 107-116. -
További szerzők:Boross Péter (1972-) (biokémikus, vegyész) Wang, Yuan-Fang Louis, John M. Fischer, Christopher C. Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Harrison, Robert W. Weber, Irene T.
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7.

001-es BibID:BIBFORM116513
035-os BibID:(Scopus)85173464630 (WOS)001077676500001
Első szerző:Sanches, Karoline
Cím:Structure-function relationships in domain peptides : from the sea anemone / Sanches Karoline, Ashwood Lauren M., Olushola-Siedoks Abisola Ave-Maria, Wai Dorothy C. C., Rahman Arfatur, Shakeel Kashmala, Naseem Muhammad Umair, Panyi Gyorgy, Prentis Peter J., Norton Raymond S.
Dátum:2024
ISSN:0887-3585
Megjegyzések:Diverse structural scaffolds have been described in peptides from sea anemones, with the ShKT domain being a common scaffold first identified in ShK toxin from Stichodactyla helianthus. ShK is a potent blocker of voltage-gated potassium channels (KV1.x), and an analog, ShK-186 (dalazatide), has completed Phase 1 clinical trials in plaque psoriasis. The ShKT domain has been found in numerous other species, but only a tiny fraction of ShKT domains has been characterized functionally. Despite adopting the canonical ShK fold, some ShKT peptides from sea anemones inhibit KV1.x, while others do not. Mutagenesis studies have shown that a Lys-Tyr (KY) dyad plays a key role in KV1.x blockade, although a cationic residue followed by a hydrophobic residue may also suffice. Nevertheless, ShKT peptides displaying an ShK-like fold and containing a KY dyad do not necessarily block potassium channels, so additional criteria are needed to determine whether new ShKT peptides might show activity against potassium channels. In this study, we used a combination of NMR and molecular dynamics (MD) simulations to assess the potential activity of a new ShKT peptide. We determined the structure of ShKT-Ts1, from the sea anemone Telmatactis stephensoni, examined its tissue localization, and investigated its activity against a range of ion channels. As ShKT-Ts1 showed no activity against KV1.x channels, we used MD simulations to investigate whether solvent exposure of the dyad residues may be informative in rationalizing and potentially predicting the ability of ShKT peptides to block KV1.x channels. We show that either a buried dyad that does not become exposed during MD simulations, or a partially exposed dyad that becomes buried during MD simulations, correlates with weak or absent activity against KV1.x channels. Therefore, structure determination coupled with MD simulations, may be used to predict whether new sequences belonging to the ShKT family may act as potassium channel blockers.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
molecular dynamics
NMR
peptide
potassium channel
sea anemone
ShKT domain
structure determination
Megjelenés:Proteins-Structure Function And Bioinformatics. - 92 : 2 (2023), p. 192-205. -
További szerzők:Ashwood, Lauren M. Olushola-Siedoks, Abisola Ave-Maria Wai, Dorothy C. C. Rahman, Arfatur Shakeel, Kashmala Naseem, Muhammad Umair (1993-) (biofizikus, molekuláris biológus) Panyi György (1966-) (biofizikus) Prentis, Peter Norton, Raymond S.
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8.

001-es BibID:BIBFORM012809
Első szerző:Shemirani, Amir-Houshang (kutató orvos, laboratórium szakorvos)
Cím:The combined effect of fibrin formation and factor XIII A subunit Val34Leu polymorphism on the activation of factor XIII in whole plasma / Amir H. Shemirani, Gizella Haramura, Zsuzsa Bagoly, László Muszbek
Dátum:2006
ISSN:1570-9639
Megjegyzések:The first step in the activation of blood coagulation factor XIII (FXIII) is the proteolytic cleavage of the potentially active A subunit (FXIII-A) by thrombin at Arg37-Gly38. Both fibrin formation and FXIII-AVal34Leu polymorphism influence the rate of proteolytic activation of purified factor XIII, however their relative importance and interaction in determining the time of onset and the rate of FXIII activation in whole plasma have not yet been explored. In the present study it was shown that in plasma, fibrin formation preceded the truncation of FXIII-A by thrombin, the activation process took place exclusively on the surface of newly formed fibrin and activated FXIII remained associated with the fibrin clot. The time of fibrin formation closely correlated with the time of FXIII activation, while there was no significant relationship between the time of FXIII activation and FXIII-AVal34Leu genotype. However, in the case of Leu34 variant the lag phase between fibrin formation and FXIII-A truncation was significantly shorter than in the case of Val34 variant. The results suggest that in whole plasma the onset of FXIII activation is determined by fibrin formation, while the rate of activation is modulated by Val34Leu polymorphism.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Factor XIII Val34Leu polymorphism
Fibrinogen
Fibrin polymerization
Thrombin
Transglutaminase
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1764 : 8 (2006), p. 1420-1423. -
További szerzők:Haramura Gizella (1957-) (vezető analitikus) Bagoly Zsuzsa (1978-) (orvos) Muszbek László (1942-) (haematológus, kutató orvos)
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9.

001-es BibID:BIBFORM001504
Első szerző:Tie, Yunfeng
Cím:Atomic resolution crystal structures of HIV-1 protease and mutants V82A and I84V with saquinavir / Tie Y., Kovalevsky A. Y., Boross P., Wang Y. F., Ghosh A. K., Tozser J., Harrison R. W., Weber I. T.
Dátum:2007
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Proteins 67 : 1 (2007), p. 232-242. -
További szerzők:Kovalevsky, Andrey Yu Boross Péter (1972-) (biokémikus, vegyész) Wang, Yuan-Fang Ghosh, Arun K. Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Harrison, Robert W. Weber, Irene T.
Internet cím:elektronikus változat
DOI
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10.

001-es BibID:BIBFORM082447
Első szerző:Tüű-Szabó Boldizsár
Cím:Altered dynamics may drift pathological fibrillization in membraneless organelles / B. Tüű-Szabó, G. Hoffka, N. Duro, M. Fuxreiter
Dátum:2019
ISSN:1570-9639
Megjegyzések:Protein phase transition can generate non-membrane bound cellular compartments, which can convert from liquid-like to solid-like states. While the molecular driving forces of phase separation have been largely understood, much less is known about the mechanisms of material-state conversion. We apply a recently developed algorithm to describe the weak interaction network of multivalent motifs, and simulate the effect of pathological mutations. We demonstrate that linker dynamics is critical to the material-state of biomolecular condensates. We show that linker flexibility/mobility is a major regulator of the weak, heterogeneous meshwork of multivalent motifs, which promotes phase transition and maintains a liquid-like state. Decreasing linker dynamics increases the propensity of amyloid-like fragments via hampering the motif-exchange and reorganization of the weak interaction network. In contrast, increasing linker mobility may compensate rigidifying mutations, suggesting that the meshwork of weak, variable interactions may provide a rescue mechanism from aggregation. Motif affinity, on the other hand, has a moderate impact on fibrillization. Here we demonstrate that the fuzzy framework provides an efficient approach to handle the intricate organization of membraneless organelles, and could also be applicable to screen for pathological effects of mutations.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Matematikai és természettudományok - Kémiai tudományok
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1867 : 10 (2019), p. 988-998. -
További szerzők:Hoffka Gyula (1992-) (vegyész) Duró Norbert (1990-) (biotechnológus) Fuxreiter Mónika (1969-) (kutató vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
MTA-DE Lendület
MTA
Fehérjedinamikai Kutatócsoport
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