Institution
Hungarian Academy of Sciences
Government•Budapest, Hungary•
About: Hungarian Academy of Sciences is a government organization based out in Budapest, Hungary. It is known for research contribution in the topics: Catalysis & Population. The organization has 21510 authors who have published 56712 publications receiving 1612286 citations. The organization is also known as: Magyar Tudományos Akadémia & MTA.
Topics: Catalysis, Population, Adsorption, Neutron, Ionization
Papers published on a yearly basis
Papers
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1,986 citations
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TL;DR: The IUPred server presents a novel algorithm for predicting such regions from amino acid sequences by estimating their total pairwise interresidue interaction energy, based on the assumption that IUP sequences do not fold due to their inability to form sufficient stabilizing inter Residue interactions.
Abstract: Summary: Intrinsically unstructured/disordered proteins and domains (IUPs) lack a well-defined three-dimensional structure under native conditions. The IUPred server presents a novel algorithm for predicting such regions from amino acid sequences by estimating their total pairwise interresidue interaction energy, based on the assumption that IUP sequences do not fold due to their inability to form sufficient stabilizing interresidue interactions. Optional to the prediction are built-in parameter sets optimized for predicting short or long disordered regions and structured domains.
Availability: The IUPred server is available for academic users at http://iupred.enzim.hu
Contact: [email protected]
1,954 citations
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University of Maryland, College Park1, Queen's University2, Cornell University3, University of Minnesota4, Nanyang Technological University5, McKinsey & Company6, Koç University7, Jacobs University Bremen8, University of Minho9, The Chinese University of Hong Kong10, Indian Institute of Management Ahmedabad11, Pontifical Catholic University of Peru12, University of Valencia13, Johannes Kepler University of Linz14, Victoria University of Wellington15, Hungarian Academy of Sciences16, National and Kapodistrian University of Athens17, La Trobe University18, University of Melbourne19, Sungkyunkwan University20, ESSEC Business School21, University of San Diego22, Katholieke Universiteit Leuven23, University of Patras24, Human Sciences Research Council25, ODESSA26, University of Tartu27, Norwegian School of Economics28, University of Koblenz and Landau29, University of Sussex30, University of Sindh31, Gakushuin University32, University of Groningen33, University of Tokyo34
TL;DR: The differences across cultures in the enforcement of conformity may reflect their specific histories and advances knowledge that can foster cross-cultural understanding in a world of increasing global interdependence and has implications for modeling cultural change.
Abstract: With data from 33 nations, we illustrate the differences between cultures that are tight (have many strong norms and a low tolerance of deviant behavior) versus loose (have weak social norms and a high tolerance of deviant behavior). Tightness-looseness is part of a complex, loosely integrated multilevel system that comprises distal ecological and historical threats (e.g., high population density, resource scarcity, a history of territorial conflict, and disease and environmental threats), broad versus narrow socialization in societal institutions (e.g., autocracy, media regulations), the strength of everyday recurring situations, and micro-level psychological affordances (e.g., prevention self-guides, high regulatory strength, need for structure). This research advances knowledge that can foster cross-cultural understanding in a world of increasing global interdependence and has implications for modeling cultural change.
1,895 citations
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TL;DR: The user is allowed to submit additional information about segment localization to enhance the prediction power, which improves the prediction accuracy as well as helps the interpretation of experimental results, i.e. in epitope insertion experiments.
Abstract: Summary: The HMMTOP transmembrane topology prediction server predicts both the localization of helical transmembrane segments and the topology of transmembrane proteins. Recently, several improvements have been introduced to the original method. Now, the user is allowed to submit additional information about segment localization to enhance the prediction power. This option improves the prediction accuracy as well as helps the interpretation of experimental results, i.e. in epitope insertion experiments. Availability: HMMTOP 2.0 is freely available to noncommercial users at http://www.enzim.hu/hmmtop. Source code is also available upon request to academic users.
1,866 citations
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TL;DR: This chapter is dedicated to describing citrate synthase, which can be followed by measuring the appearance of the free SH group of the released CoASH through three methods discussed in the chapter.
Abstract: Publisher Summary This chapter is dedicated to describing citrate synthase. The assay of citrate synthase is performed by coupling it to the transacetylase reaction. The disappearance of acetyl phosphate is followed by a hydroxamate method and the formation of citrate by the pentabromoacetone method. The malate dehydrogenase catalyzed reaction is used to generate the oxaloacetate for the citrate synthase reaction. Another method for assaying citrate synthase uses 14 C-acetyl-CoA and measures its incorporation in 14 C-citrate, which is isolated as a silver salt. Citrate synthase can be followed by measuring the appearance of the free SH group of the released CoASH; three such methods are discussed in the chapter. One method is to measure the oxidation of the CoASH by dichlorophenol- indophenol, which is accompanied by a decrease in absorbancy at 578 mμ. Another method measures the CoASH polarographically. The third method measures SH by the use of 5, 5’-dithiobis-(2-nitrobenzoate) (DTNB) (Ellman's reagent).
1,848 citations
Authors
Showing all 21526 results
Name | H-index | Papers | Citations |
---|---|---|---|
Jasvinder A. Singh | 176 | 2382 | 223370 |
Alexander S. Szalay | 166 | 936 | 145745 |
Ashok Kumar | 151 | 5654 | 164086 |
György Buzsáki | 150 | 446 | 96433 |
Daniel Bloch | 145 | 1819 | 119556 |
Brajesh C Choudhary | 143 | 1618 | 108058 |
Geoffrey Burnstock | 141 | 1488 | 99525 |
Suman Bala Beri | 137 | 1608 | 104798 |
Vipin Bhatnagar | 137 | 1756 | 104163 |
Paul Slovic | 136 | 506 | 126658 |
Manjit Kaur | 135 | 1540 | 97378 |
Gabor Istvan Veres | 135 | 1349 | 96104 |
Dimitri Bourilkov | 134 | 1489 | 96884 |
Georges Azuelos | 134 | 1294 | 90690 |
Michael Tytgat | 134 | 1449 | 94133 |