TY - JOUR AU - Suthar, Sharad Kumar AU - Rauscher, Anna Ágnes AU - Winternitz, Máté AU - Gyimesi, Máté AU - Málnási Csizmadia, András TI - Chiral HPLC separation of enantiomeric blebbistatin derivatives and racemization analysis in vertebrate tissues. JF - JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS J2 - J PHARMACEUT BIOMED ANAL VL - 204 PY - 2021 SN - 0731-7085 DO - 10.1016/j.jpba.2021.114246 UR - https://m2.mtmt.hu/api/publication/32111416 ID - 32111416 N1 - Funding Agency and Grant Number: Hungarian National Research Development and Innovation OfficeNational Research, Development & Innovation Office (NRDIO) - Hungary [NVKP 16-1-2016-0051, 2019-1.1.1-PIACI-KFI-2019-00488]; Szint+Excellence Program-ELTE TTK Funding text: The research was supported by the Hungarian National Research Development and Innovation Office grant No. NVKP 16-1-2016-0051 and 2019-1.1.1-PIACI-KFI-2019-00488. The authors also acknowledge the financial support by Szint+Excellence Program-ELTE TTK. AB - Simple and consistent chiral HPLC methods for the efficient separation of enantiomeric blebbistatin derivatives, namely parent compound blebbistatin and derivatives 4-nitroblebbistatin, 4-aminoblebbistatin, 4-dimethylaminoblebbistatin, and 4-t-butylblebbistatin were developed using cellulose tris(3,5-dimethylphenylcarbamate) as a stationary phase (Lux cellulose-1 column). Blebbistatin, 4-aminoblebbistatin, and 4-dimethylaminoblebbistatin racemates were well-separated in normal-phase HPLC conditions while 4-nitroblebbistatin and 4-t-butylblebbistatin were effectively separated in both normal- and reversed-phase HPLC conditions. Furthermore, the order of elution of enantiopure compounds was found to be independent of mobile phase compositions and conditions used, and solely depends on the interaction between the enantiomer and the chiral stationary phase. We found that despite the chiral center being present far from the D-ring in the blebbistatin structure, the D-ring substitutions prominently affect the chiral separation. Ex vivo racemization studies of the most popular blebbistatin derivative (S)-(-)-4-aminoblebbistatin in rat blood and brain tissues revealed that the compound does not convert into the inactive enantiomer. This confirms that (S)-(-)-4-aminoblebbistatin is a useful tool compound in cellular and molecular biology studies without the risks of racemization and degradation effects. LA - English DB - MTMT ER - TY - JOUR AU - M Tóth, Erika AU - Toumi, Marwene AU - Farkas, Rózsa AU - Takáts, Kornél AU - Somodi, Csenge AU - Ács, Éva TI - Insight into the hidden bacterial diversity of Lake Balaton, Hungary JF - BIOLOGIA FUTURA J2 - BIOL FUTURA VL - 71 PY - 2020 IS - 4 SP - 383 EP - 391 PG - 9 SN - 2676-8615 DO - 10.1007/s42977-020-00040-6 UR - https://m2.mtmt.hu/api/publication/31599696 ID - 31599696 N1 - A publikáció a Nemzeti Közszolgálati Egyetem 2020. évi Tématerületi Kiválóság Program keretében, a Fenntartható biztonság és társadalmi környezet elnevezésű projekt támogatásával valósult meg, az Innovációs és Technológiai Minisztérium Nemzeti Kutatási, Fejlesztési és Innovációs Alapból nyújtott támogatásával, a Nemzeti Kutatási, Fejlesztési és Innovációs Hivatal által kibocsátott támogatói okirat alapján. AB - In the present study, the prokaryotic community structure of the water of Lake Balaton was investigated at the littoral region of three different points (Tihany, Balatonmariafurdo and Keszthely) by cultivation independent methods [next-generation sequencing (NGS), specific PCRs and microscopy cell counting] to check the hidden microbial diversity of the lake. The taxon-specific PCRs did not show pathogenic bacteria but at Keszthely and Mariafurdo sites extended spectrum beta-lactamase-producing microorganisms could be detected. The bacterial as well as archaeal diversity of the water was high even when many taxa are still uncultivable. Based on NGS, the bacterial communities were dominated by Proteobacteria, Bacteroidetes and Actinobacteria, while the most frequent Archaea belonged to Woesearchaeia (Nanoarchaeota). The ratio of the detected taxa differed among the samples. Three different types of phototrophic groups appeared: Cyanobacteria (oxygenic phototrophic organisms), Chloroflexi (anaerobic, organotrophic bacteria) and the aerobic, anoxic photoheterotrophic group (AAPs). Members of Firmicutes appeared only with low abundance, and Enterobacteriales (order within Proteobacteria) were present also only in low numbers in all samples. LA - English DB - MTMT ER - TY - JOUR AU - Pénzes, Máté AU - Túrós, Demeter AU - Máthé, Domokos AU - Szigeti, Krisztián AU - Hegedűs, Nikolett AU - Rauscher, Anna Ágnes AU - Tóth, Péter József AU - Ivic, Ivan AU - Padmanabhan, Parasuraman AU - Pál, Gabriella AU - Dobolyi, Árpád AU - Gyimesi, Máté AU - Málnási Csizmadia, András TI - Direct myosin-2 inhibition enhances cerebral perfusion resulting in functional improvement after ischemic stroke JF - THERANOSTICS J2 - THERANOSTICS VL - 10 PY - 2020 IS - 12 SP - 5341 EP - 5356 PG - 16 SN - 1838-7640 DO - 10.7150/thno.42077 UR - https://m2.mtmt.hu/api/publication/31179505 ID - 31179505 N1 - * Megosztott szerzőség LA - English DB - MTMT ER - TY - JOUR AU - Lukács, Péter AU - Földi, Mátyás Csaba AU - Valanszki, L AU - Casanova, E AU - Biri-Kovács, Beáta AU - Nyitray, László AU - Málnási Csizmadia, András AU - Mike, Árpád TI - Non-blocking modulation contributes to sodium channel inhibition by a covalently attached photoreactive riluzole analog JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 8 PY - 2018 PG - 11 SN - 2045-2322 DO - 10.1038/s41598-018-26444-y UR - https://m2.mtmt.hu/api/publication/3397475 ID - 3397475 N1 - MTA-ELTE NAP B Opto-Neuropharmacology Group Hungary, Budapest, Hungary Department of Physiology, Center of Physiology and Pharmacology and Comprehensive Cancer Center (CCC), Medical University of Vienna, Vienna, Austria Ludwig Boltzmann Institute for Cancer Research (LBI-CR), Vienna, Austria Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary MTA-ELTE Molecular Biophysics Research Group, Eötvös Loránd University, Budapest, Hungary Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Martonvásár, Hungary Cited By :1 Export Date: 31 July 2019 Correspondence Address: Mike, A.; MTA-ELTE NAP B Opto-Neuropharmacology Group HungaryHungary; email: arpadmike1@gmail.com Funding details: Office of Research, Innovation and Economic Development, California State Polytechnic University, Pomona, VKSZ_14–1–2015–0052 Funding details: KTIA-NAP-13–2–2014–002 Funding text 1: This work was supported by the Hungarian Brain Research Program (KTIA-NAP-13–2–2014–002), and The National Research, Development and Innovation Office (VKSZ_14–1–2015–0052). Plasmid DNA for NaV1.4 channel were kindly provided by Hannes Todt. MTA-ELTE NAP B Opto-Neuropharmacology Group Hungary, Budapest, Hungary Department of Physiology, Center of Physiology and Pharmacology and Comprehensive Cancer Center (CCC), Medical University of Vienna, Vienna, Austria Ludwig Boltzmann Institute for Cancer Research (LBI-CR), Vienna, Austria Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary MTA-ELTE Molecular Biophysics Research Group, Eötvös Loránd University, Budapest, Hungary Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Martonvásár, Hungary Cited By :1 Export Date: 10 August 2019 Correspondence Address: Mike, A.; MTA-ELTE NAP B Opto-Neuropharmacology Group HungaryHungary; email: arpadmike1@gmail.com Funding details: Office of Research, Innovation and Economic Development, California State Polytechnic University, Pomona, VKSZ_14–1–2015–0052 Funding details: KTIA-NAP-13–2–2014–002 Funding text 1: This work was supported by the Hungarian Brain Research Program (KTIA-NAP-13–2–2014–002), and The National Research, Development and Innovation Office (VKSZ_14–1–2015–0052). Plasmid DNA for NaV1.4 channel were kindly provided by Hannes Todt. MTA-ELTE NAP B Opto-Neuropharmacology Group Hungary, Budapest, Hungary Department of Physiology, Center of Physiology and Pharmacology and Comprehensive Cancer Center (CCC), Medical University of Vienna, Vienna, Austria Ludwig Boltzmann Institute for Cancer Research (LBI-CR), Vienna, Austria Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary MTA-ELTE Molecular Biophysics Research Group, Eötvös Loránd University, Budapest, Hungary Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Martonvásár, Hungary Cited By :1 Export Date: 18 September 2019 Correspondence Address: Mike, A.; MTA-ELTE NAP B Opto-Neuropharmacology Group HungaryHungary; email: arpadmike1@gmail.com MTA-ELTE NAP B Opto-Neuropharmacology Group Hungary, Budapest, Hungary Department of Physiology, Center of Physiology and Pharmacology and Comprehensive Cancer Center (CCC), Medical University of Vienna, Vienna, Austria Ludwig Boltzmann Institute for Cancer Research (LBI-CR), Vienna, Austria Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary MTA-ELTE Molecular Biophysics Research Group, Eötvös Loránd University, Budapest, Hungary Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Martonvásár, Hungary Cited By :2 Export Date: 11 February 2020 Correspondence Address: Mike, A.; MTA-ELTE NAP B Opto-Neuropharmacology Group HungaryHungary; email: arpadmike1@gmail.com MTA-ELTE NAP B Opto-Neuropharmacology Group Hungary, Budapest, Hungary Department of Physiology, Center of Physiology and Pharmacology and Comprehensive Cancer Center (CCC), Medical University of Vienna, Vienna, Austria Ludwig Boltzmann Institute for Cancer Research (LBI-CR), Vienna, Austria Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary MTA-ELTE Molecular Biophysics Research Group, Eötvös Loránd University, Budapest, Hungary Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Martonvásár, Hungary Cited By :2 Export Date: 17 April 2020 Correspondence Address: Mike, A.; MTA-ELTE NAP B Opto-Neuropharmacology Group HungaryHungary; email: arpadmike1@gmail.com Chemicals/CAS: azide, 12596-60-0, 14343-69-2; riluzole, 1744-22-5; Azides; Muscle Proteins; Riluzole; Scn4a protein, rat; Sodium Channel Blockers; Sodium Channels Funding details: VKSZ_14–1–2015–0052 Funding details: KTIA-NAP-13–2–2014–002 Funding text 1: This work was supported by the Hungarian Brain Research Program (KTIA-NAP-13–2–2014–002), and The National Research, Development and Innovation Office (VKSZ_14–1–2015–0052). Plasmid DNA for NaV1.4 channel were kindly provided by Hannes Todt. MTA-ELTE NAP B Opto-Neuropharmacology Group Hungary, Budapest, Hungary Department of Physiology, Center of Physiology and Pharmacology and Comprehensive Cancer Center (CCC), Medical University of Vienna, Vienna, Austria Ludwig Boltzmann Institute for Cancer Research (LBI-CR), Vienna, Austria Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary MTA-ELTE Molecular Biophysics Research Group, Eötvös Loránd University, Budapest, Hungary Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Martonvásár, Hungary Cited By :4 Export Date: 20 March 2021 Correspondence Address: Mike, A.; MTA-ELTE NAP B Opto-Neuropharmacology Group HungaryHungary; email: arpadmike1@gmail.com Chemicals/CAS: azide, 12596-60-0, 14343-69-2; riluzole, 1744-22-5; Azides; Muscle Proteins; Riluzole; Scn4a protein, rat; Sodium Channel Blockers; Sodium Channels Funding details: KTIA-NAP-13–2–2014–002 Funding details: VKSZ_14–1–2015–0052 Funding text 1: This work was supported by the Hungarian Brain Research Program (KTIA-NAP-13–2–2014–002), and The National Research, Development and Innovation Office (VKSZ_14–1–2015–0052). Plasmid DNA for NaV1.4 channel were kindly provided by Hannes Todt. AB - Sodium channel inhibitor drugs decrease pathological hyperactivity in various diseases including pain syndromes, myotonia, arrhythmias, nerve injuries and epilepsies. Inhibiting pathological but not physiological activity, however, is a major challenge in drug development. Sodium channel inhibitors exert their effects by a dual action: they obstruct ion flow ("block"), and they alter the energetics of channel opening and closing ("modulation"). Ideal drugs would be modulators without blocking effect, because modulation is inherently activity-dependent, therefore selective for pathological hyperactivity. Can block and modulation be separated? It has been difficult to tell, because the effect of modulation is obscured by conformation-dependent association/dissociation of the drug. To eliminate dynamic association/dissociation, we used a photoreactive riluzole analog which could be covalently bound to the channel; and found, unexpectedly, that drug-bound channels could still conduct ions, although with modulated gating. The finding that non-blocking modulation is possible, may open a novel avenue for drug development because non-blocking modulators could be more specific in treating hyperactivity-linked diseases. LA - English DB - MTMT ER - TY - JOUR AU - Rauscher, Anna A AU - Kumar, Sharad AU - Várkuti, Boglárka AU - Képiró, Miklós AU - Horvath, Adam I AU - Végner, László AU - Hegyi, György AU - Borhegyi, Zsolt AU - Varga, Máté AU - Lenkei, Zsolt AU - Málnási Csizmadia, András TI - Highly Soluble, Non-Phototoxic, Non-Fluorescent, Photostable Blebbistatin Derivatives JF - BIOPHYSICAL JOURNAL J2 - BIOPHYS J VL - 112 PY - 2017 IS - 3 SP - 266A EP - 267A SN - 0006-3495 UR - https://m2.mtmt.hu/api/publication/3247385 ID - 3247385 LA - English DB - MTMT ER - TY - JOUR AU - Poór, Miklós AU - Kunsági-Máté, Sándor AU - Bálint, Mónika Enikő AU - Hetényi, Csaba AU - Gerner, Zsófia AU - Lemli, Beáta TI - Interaction of mycotoxin zearalenone with human serum albumin JF - JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY J2 - J PHOTOCH PHOTOBIO B VL - 170 PY - 2017 SP - 16 EP - 24 PG - 9 SN - 1011-1344 DO - 10.1016/j.jphotobiol.2017.03.016 UR - https://m2.mtmt.hu/api/publication/3203729 ID - 3203729 N1 - Cited By :46 Export Date: 24 October 2023 CODEN: JPPBE Correspondence Address: Poór, M.; Department of Pharmacology and Toxicology, Szigeti út 12, Hungary; email: poor.miklos@pte.hu LA - English DB - MTMT ER - TY - JOUR AU - Herman, Bianka Edina AU - Szabó, Johanna AU - Bacsa, Ildikó AU - Wölfling, János AU - Schneider, Gyula AU - Bálint, Mónika Enikő AU - Hetényi, Csaba AU - Mernyák, Erzsébet AU - Szécsi, Mihály TI - Comparative investigation of the in vitro inhibitory potencies of 13-epimeric estrones and D-secoestrones towards 17β-hydroxysteroid dehydrogenase type 1 JF - JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY J2 - J ENZYM INHIB MED CH VL - 31 PY - 2016 IS - Suppl. 3 SP - 61 EP - 69 PG - 9 SN - 1475-6366 DO - 10.1080/14756366.2016.1204610 UR - https://m2.mtmt.hu/api/publication/3097533 ID - 3097533 N1 - MTA-ELTE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Budapest, Hungary AB - The inhibitory effects of 13-epimeric estrones, D-secooxime and D-secoalcohol estrone compounds on human placental 17β-hydroxysteroid dehydrogenase type 1 isozyme (17β-HSD1) were investigated. The transformation of estrone to 17β-estradiol was studied by an in vitro radiosubstrate incubation method. 13α-Estrone inhibited the enzyme activity effectively with an IC50 value of 1.2 μM, which indicates that enzyme affinity is similar to that of the natural estrone substrate. The 13β derivatives and the compounds bearing a 3-hydroxy group generally exerted stronger inhibition than the 13α and 3-ether counterparts. The 3-hydroxy-13β-D-secoalcohol and the 3-hydroxy-13α-D-secooxime displayed an outstanding cofactor dependence, i.e. more efficient inhibition in the presence of NADH than NADPH. The 3-hydroxy-13β-D-secooxime has an IC50 value of 0.070 μM and is one of the most effective 17β-HSD1 inhibitors reported to date in the literature. © 2016 Informa UK Limited, trading as Taylor & Francis Group. LA - English DB - MTMT ER - TY - JOUR AU - Várkuti, Boglárka AU - Képiró, Miklós AU - Horváth, Ádám István AU - Végner, László AU - Ráti, S AU - Zsigmond, Áron AU - Hegyi, György AU - Lenkei, Z AU - Varga, Máté AU - Málnási Csizmadia, András TI - A highly soluble, non-phototoxic, non-fluorescent blebbistatin derivative. JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 6 PY - 2016 PG - 10 SN - 2045-2322 DO - 10.1038/srep26141 UR - https://m2.mtmt.hu/api/publication/3074596 ID - 3074596 N1 - Department of Biochemistry, Institute of Biology, Eötvös Loránd University, Budapest, H-1117, Hungary Printnet Ltd., Veresegyház, H-2212, Hungary Department of Genetics, Institute of Biology, Eötvös Loránd University, Budapest, H-1117, Hungary Brain Plasticity Unit, ESPCI-Paris-Tech, CNRS UMR8249, Paris, France MTA-ELTE Molecular Biophysics Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, H-1117, Hungary Optopharma Ltd., Budapest, H-1015, Hungary Cited By :13 Export Date: 8 January 2019 Correspondence Address: Málnási-Csizmadia, A.; Department of Biochemistry, Institute of Biology, Eötvös Loránd UniversityHungary; email: malnalab@yahoo.com Department of Biochemistry, Institute of Biology, Eötvös Loránd University, Budapest, H-1117, Hungary Printnet Ltd., Veresegyház, H-2212, Hungary Department of Genetics, Institute of Biology, Eötvös Loránd University, Budapest, H-1117, Hungary Brain Plasticity Unit, ESPCI-Paris-Tech, CNRS UMR8249, Paris, France MTA-ELTE Molecular Biophysics Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, H-1117, Hungary Optopharma Ltd., Budapest, H-1015, Hungary Cited By :15 Export Date: 16 September 2019 Correspondence Address: Málnási-Csizmadia, A.; Department of Biochemistry, Institute of Biology, Eötvös Loránd UniversityHungary; email: malnalab@yahoo.com Department of Biochemistry, Institute of Biology, Eötvös Loránd University, Budapest, H-1117, Hungary Printnet Ltd., Veresegyház, H-2212, Hungary Department of Genetics, Institute of Biology, Eötvös Loránd University, Budapest, H-1117, Hungary Brain Plasticity Unit, ESPCI-Paris-Tech, CNRS UMR8249, Paris, France MTA-ELTE Molecular Biophysics Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, H-1117, Hungary Optopharma Ltd., Budapest, H-1015, Hungary Cited By :16 Export Date: 27 November 2019 Correspondence Address: Málnási-Csizmadia, A.; Department of Biochemistry, Institute of Biology, Eötvös Loránd UniversityHungary; email: malnalab@yahoo.com LA - English DB - MTMT ER - TY - JOUR AU - Jeszenői, Norbert AU - Bálint, Mónika Enikő AU - Horváth, István AU - van der Spoel, D AU - Hetényi, Csaba TI - Exploration of Interfacial Hydration Networks of Target-Ligand Complexes. JF - JOURNAL OF CHEMICAL INFORMATION AND MODELING J2 - J CHEM INF MODEL VL - 56 ET - 0 PY - 2016 IS - 1 SP - 148 EP - 158 PG - 11 SN - 1549-9596 DO - 10.1021/acs.jcim.5b00638 UR - https://m2.mtmt.hu/api/publication/2998137 ID - 2998137 N1 - Department of Genetics, Eötvös Loránd University, Pázmány Péter sétány 1/C, Budapest, 1117, Hungary MTA NAP-B Molecular Neuroendocrinology Group, Institute of Physiology, Szentágothai Research Center, Center for Neuroscience, University of Pécs, Szigeti út 12, Pécs, 7624, Hungary Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/C, Budapest, 1117, Hungary Chemistry Doctoral School, University of Szeged, Dugonics tér 13, Szeged, 6720, Hungary Uppsala Center for Computational Chemistry, Science for Life Laboratory, Department of Cell and Molecular Biology, University of Uppsala, Box 596, Uppsala, SE-75124, Sweden MTA-ELTE Molecular Biophysics Research Group, Hungarian Academy of Sciences, Pázmány sétány 1/C, Budapest, 1117, Hungary Cited By :25 Export Date: 24 October 2023 CODEN: JCISD Correspondence Address: Hetényi, C.; MTA-ELTE Molecular Biophysics Research Group, Pázmány sétány 1/C, Hungary; email: csabahete@yahoo.com AB - Interfacial hydration strongly influences interactions between biomolecules. For example, drug-target complexes are often stabilized by hydration networks formed between hydrophilic residues and water molecules at the interface. Exhaustive exploration of hydration networks is challenging for experimental as well as theoretical methods due to high mobility of participating water molecules. In the present study, we introduced a tool for determination of the complete, void-free hydration structures of molecular interfaces. The tool was applied to 31 complexes including histone proteins, a HIV-1 protease, a G-protein-signaling modulator, and peptide ligands of various lengths. The complexes contained 344 experimentally determined water positions used for validation, and excellent agreement with these was obtained. High-level cooperation between interfacial water molecules was detected by a new approach based on the decomposition of hydration networks into static and dynamic network regions (subnets). Besides providing hydration structures at the atomic level, our results uncovered hitherto hidden networking fundaments of integrity and stability of complex biomolecular interfaces filling an important gap in the toolkit of drug design and structural biochemistry. The presence of continuous, static regions of the interfacial hydration network was found necessary also for stable complexes of histone proteins participating in chromatin assembly and epigenetic regulation. LA - English DB - MTMT ER - TY - JOUR AU - Gráf, László AU - Molnár, Tamás AU - Kardos, József AU - Gáspári, Zoltán AU - Katona, Gergely TI - The role of structural flexibility and stability in the interaction of serine proteases with their inhibitors JF - CURRENT PROTEIN AND PEPTIDE SCIENCE J2 - CURR PROTEIN PEPT SCI VL - 16 PY - 2015 IS - 6 SP - 521 EP - 531 PG - 11 SN - 1389-2037 DO - 10.2174/1389203716666150429123733 UR - https://m2.mtmt.hu/api/publication/2923894 ID - 2923894 N1 - Megjegyzés-25226546 Hiányzó Jelleg: 'JOUR\n\nArticle' Admin megjegyzés-25226546 tblcategory: (Category) ('JOUR\n\nArticle') #Jelleg Cited By :1 Export Date: 12 July 2019 CODEN: CPPSC Correspondence Address: Gráf, L.; Department of Biochemistry, Eötvös Loránd University, P.O. Box: 1117, Hungary; email: graf@elte.hu Cited By :2 Export Date: 12 September 2019 CODEN: CPPSC Correspondence Address: Gráf, L.; Department of Biochemistry, Eötvös Loránd University, P.O. Box: 1117, Hungary; email: graf@elte.hu Cited By :2 Export Date: 2 October 2019 CODEN: CPPSC Correspondence Address: Gráf, L.; Department of Biochemistry, Eötvös Loránd University, P.O. Box: 1117, Hungary; email: graf@elte.hu Cited By :2 Export Date: 17 December 2019 CODEN: CPPSC Correspondence Address: Gráf, L.; Department of Biochemistry, Eötvös Loránd University, P.O. Box: 1117, Hungary; email: graf@elte.hu Funding Agency and Grant Number: Hungarian National Research Fund (OTKA)Orszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [104198] Funding text: Support from the Hungarian National Research Fund (OTKA grant 104198) is acknowledged. We would like to thank George Kunos and John Markley for reviewing our manuscript. AB - Serine proteases and their natural inhibitors have long been served as excellent models for studying (primary, secondary and tertiary) structure - activity relationships of biologically interacting proteins. As protein flexibility has been accepted as a “fourth dimension” of the protein structure, its contribution to the binding process has gained much interest. In this article we review extreme cases of serine protease interactions with canonical serine protease inhibitors that provide unique insights into the dynamics of protein- protein interactions. The major conclusions of our review article are: a) taxon-specific inhibitory effects of two highly homologous protease inhibitors from Schistocerca gregaria (SGCI and SGTI), as investigated by H/D exchange experiments and NMR spectroscopy, are due to their differential flexibilities, b) stabilities of some protease and inhibitor complexes, the wide-spread and increased flexibility of some segments in the protein-protein complexes, as studied by X-ray crystallography and NMR-spectroscopy, appear to be proportional to the physical stability of the complex. © 2015 Bentham Science Publishers. LA - English DB - MTMT ER -