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Antibodies targeting the neuraminidase active site inhibit influenza H3N2 viruses with an S245N glycosylation site
Antibodies targeting the neuraminidase active site inhibit influenza H3N2 viruses with an S245N glycosylation site
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Antibodies targeting the neuraminidase active site inhibit influenza H3N2 viruses with an S245N glycosylation site

Stadlbauer, Daniel ; McMahon, Meagan ; Turner, Hannah L ; Zhu, Xueyong ; Wan, Hongquan ; Carreño, Juan Manuel ; O'Dell, George ; Strohmeier, Shirin ; Khalil, Zain ; Luksza, Marta ; van Bakel, Harm ; Simon, Viviana ; Ellebedy, Ali H ; Wilson, Ian A ; Ward, Andrew B ; Krammer, Florian

Nature communications, 2022-12, Vol.13 (1), p.7864-8, Article 7864 [Periódico revisado por pares]

England: Nature Publishing Group

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AmiP from hyperthermophilic Thermus parvatiensis prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase
AmiP from hyperthermophilic Thermus parvatiensis prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase
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AmiP from hyperthermophilic Thermus parvatiensis prophage is a thermoactive and ultrathermostable peptidoglycan lytic amidase

Jasilionis, Andrius ; Plotka, Magdalena ; Wang, Lei ; Dorawa, Sebastian ; Lange, Joanna ; Watzlawick, Hildegard ; van den Bergh, Tom ; Vroling, Bas ; Altenbuchner, Josef ; Kaczorowska, Anna‐Karina ; Pohl, Ehmke ; Kaczorowski, Tadeusz ; Nordberg Karlsson, Eva ; Freitag‐Pohl, Stefanie

Protein science, 2023-03, Vol.32 (3), p.e4585-n/a [Periódico revisado por pares]

Hoboken, USA: John Wiley & Sons, Inc

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3
The endocannabinoid hydrolase FAAH is an allosteric enzyme
The endocannabinoid hydrolase FAAH is an allosteric enzyme
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The endocannabinoid hydrolase FAAH is an allosteric enzyme

Dainese, Enrico ; Oddi, Sergio ; Simonetti, Monica ; Sabatucci, Annalaura ; Angelucci, Clotilde B ; Ballone, Alice ; Dufrusine, Beatrice ; Fezza, Filomena ; De Fabritiis, Gianni ; Maccarrone, Mauro

Scientific reports, 2020-02, Vol.10 (1), p.2292, Article 2292 [Periódico revisado por pares]

England: Nature Publishing Group

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4
High‐performance variants of plant diacylglycerol acyltransferase 1 generated by directed evolution provide insights into structure function
High‐performance variants of plant diacylglycerol acyltransferase 1 generated by directed evolution provide insights into structure function
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High‐performance variants of plant diacylglycerol acyltransferase 1 generated by directed evolution provide insights into structure function

Chen, Guanqun ; Xu, Yang ; Siloto, Rodrigo M. P. ; Caldo, Kristian Mark P. ; Vanhercke, Thomas ; Tahchy, Anna El ; Niesner, Nathalie ; Chen, Yongyan ; Mietkiewska, Elzbieta ; Weselake, Randall J.

The Plant journal : for cell and molecular biology, 2017-10, Vol.92 (2), p.167-177 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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5
Expression and purification of recombinant extracellular sulfatase HSulf-2 allows deciphering of enzyme sub-domain coordinated role for the binding and 6-O-desulfation of heparan sulfate
Expression and purification of recombinant extracellular sulfatase HSulf-2 allows deciphering of enzyme sub-domain coordinated role for the binding and 6-O-desulfation of heparan sulfate
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Expression and purification of recombinant extracellular sulfatase HSulf-2 allows deciphering of enzyme sub-domain coordinated role for the binding and 6-O-desulfation of heparan sulfate

Seffouh, Amal ; El Masri, Rana ; Makshakova, Olga ; Gout, Evelyne ; Hassoun, Zahra el Oula ; Andrieu, Jean-pierre ; Lortat-Jacob, Hugues ; Vivès, Romain R.

Cellular and molecular life sciences : CMLS, 2019-05, Vol.76 (9), p.1807-1819 [Periódico revisado por pares]

Cham: Springer International Publishing

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6
Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme
Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme
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Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme

McCord, Lauren A. ; Liang, Wenguang G. ; Dowdell, Evan ; Kalas, Vasilios ; Hoey, Robert J. ; Koide, Akiko ; Koide, Shohei ; Tang, Wei-Jen

Proceedings of the National Academy of Sciences - PNAS, 2013-08, Vol.110 (34), p.13827-13832 [Periódico revisado por pares]

United States: National Academy of Sciences

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7
Ubiquitin vinyl methyl ester binding orients the misaligned active site of the ubiquitin hydrolase UCHL1 into productive conformation
Ubiquitin vinyl methyl ester binding orients the misaligned active site of the ubiquitin hydrolase UCHL1 into productive conformation
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Ubiquitin vinyl methyl ester binding orients the misaligned active site of the ubiquitin hydrolase UCHL1 into productive conformation

Boudreaux, David A ; Maiti, Tushar K ; Davies, Christopher W ; Das, Chittaranjan

Proceedings of the National Academy of Sciences - PNAS, 2010-05, Vol.107 (20), p.9117-9122 [Periódico revisado por pares]

United States: National Academy of Sciences

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8
Functional Studies of [FeFe] Hydrogenase Maturation in an Escherichia coli Biosynthetic System
Functional Studies of [FeFe] Hydrogenase Maturation in an Escherichia coli Biosynthetic System
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Functional Studies of [FeFe] Hydrogenase Maturation in an Escherichia coli Biosynthetic System

KING, Paul W ; POSEWITZ, Matthew C ; GHIRARDI, Maria L ; SEIBERT, Michael

Journal of Bacteriology, 2006-03, Vol.188 (6), p.2163-2172 [Periódico revisado por pares]

Washington, DC: American Society for Microbiology

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9
Identification of Human Leukotriene A4 Hydrolase Inhibitors Using Structure-Based Pharmacophore Modeling and Molecular Docking
Identification of Human Leukotriene A4 Hydrolase Inhibitors Using Structure-Based Pharmacophore Modeling and Molecular Docking
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Identification of Human Leukotriene A4 Hydrolase Inhibitors Using Structure-Based Pharmacophore Modeling and Molecular Docking

Audat, Suaad A ; Al-Shar'i, Nizar A ; Al-Oudat, Buthina A ; Bryant-Friedrich, Amanda ; Bedi, Mel F ; Zayed, Aref L ; Al-Balas, Qosay A

Molecules (Basel, Switzerland), 2020-06, Vol.25 (12), p.2871 [Periódico revisado por pares]

Switzerland: MDPI AG

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10
The crystal structure of the malic enzyme from Candidatus Phytoplasma reveals the minimal structural determinants for a malic enzyme
The crystal structure of the malic enzyme from Candidatus Phytoplasma reveals the minimal structural determinants for a malic enzyme
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The crystal structure of the malic enzyme from Candidatus Phytoplasma reveals the minimal structural determinants for a malic enzyme

Alvarez, C. E. ; Trajtenberg, F. ; Larrieux, N. ; Saigo, M. ; Golic, A. ; Andreo, C. S. ; Hogenhout, S. A. ; Mussi, M. A. ; Drincovich, M. F. ; Buschiazzo, A.

Acta crystallographica. Section D, Biological crystallography., 2018-04, Vol.74 (4), p.332-340 [Periódico revisado por pares]

5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography

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