Výsledky vyhledávání - "DSF, differential scanning fluorimetry"

A fragment-based approach to assess the ligandability of ArgB, ArgC, ArgD and ArgF in the L-arginine biosynthetic pathway of Mycobacterium tuberculosis

Autor: William R. Jacobs, Maria A. Pasillas, Ailidh Burgess, Tom L. Blundell, Sangeeta Tiwari, Anthony G. Coyne, James Cory-Wright, Vitor Mendes, Clio Meghir, Víctor Sebastián-Pérez, Sherine E. Thomas, Shaymaa A. Zaidan, Emma Cattermole, Pooja Gupta, Chris Abell

Publikováno v: Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 3491-3506 (2021)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
Computational and Structural Biotechnology Journal
'Computational and Structural Biotechnology Journal ', vol: 19, pages: 3491-3506 (2021)

16 p.-8 fig.-4 tab.
The L-arginine biosynthesis pathway consists of eight enzymes that catalyse the conversion of L-glutamate to L-arginine. Arginine auxotrophs (argB/argF deletion mutants) of Mycobacterium tuberculosis are rapidly sterilised in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::862c280712d00acb38047d21232c7e0d
http://www.sciencedirect.com/science/article/pii/S2001037021002373

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Endogenous modulators of neurotrophin signaling: Landscape of the transient ATP-NGF interactions

Autor: Doriano Lamba, Sonia Covaceuszach, Franci Merzel, Alberto Cassetta, Francesca Paoletti, Simona Golic Grdadolnik, Iza Ogris, Jože Grdadolnik

Publikováno v: Computational and Structural Biotechnology Journal 19 (2021): 2938–2949. doi:10.1016/j.csbj.2021.05.009
info:cnr-pdr/source/autori:Paoletti F.; Merzel F.; Cassetta A.; Ogris I.; Covaceuszach S.; Grdadolnik J.; Lamba D.; Golic Grdadolnik S./titolo:Endogenous modulators of neurotrophin signaling: Landscape of the transient ATP-NGF interactions/doi:10.1016%2Fj.csbj.2021.05.009/rivista:Computational and Structural Biotechnology Journal/anno:2021/pagina_da:2938/pagina_a:2949/intervallo_pagine:2938–2949/volume:19
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 2938-2949 (2021)
Computational and Structural Biotechnology Journal

Graphical abstract
Highlights • High-resolution solution NMR structure of rhNGF has been determined. • Quinary interactions characterize ATP binding to rhNGF. • SPR, ITC and STD-NMR reveal ATP binding to rhNGF with mM affinity. • NMR and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dad8b1ec3a685ab9524b7c239670f5be
https://doi.org/10.1016/j.csbj.2021.05.009

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Framework Mutations of the 10-1074 bnAb Increase Conformational Stability, Manufacturability, and Stability While Preserving Full Neutralization Activity

Autor: Chelsey Bennett, Mcclure Megan J, Georgia D. Tomaras, Michael S. Seaman, Clark Rutilio H, Randal R. Ketchem, J. Alaina Floyd, Kelly E. Seaton, Christine C. Siska, Yan Brodsky, Jeremy M. Shaver, Bryan T. Mayer, Nicole L. Yates, Bruce A. Kerwin, Alison J. Gillespie

Publikováno v: Journal of Pharmaceutical Sciences

The broadly neutralizing anti-HIV antibody, 10-1074, is a highly somatically hypermutated IgG1 being developed for prophylaxis in sub-Saharan Africa. A series of algorithms were applied to identify potentially destabilizing residues in the framework

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::752f2582d80bda3c1169fc5c9a92aaad
http://europepmc.org/articles/PMC6941225

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Molecular basis for diaryldiamine selectivity and competition with tRNA in a type 2 methionyl-tRNA synthetase from a Gram-negative bacterium

Autor: Jackeline de Lima Zanella, Maxuel O. Andrade, Artur T. Cordeiro, Celso Eduardo Benedetti, Gustavo Fernando Mercaldi

Publikováno v: The Journal of Biological Chemistry

Gram-negative bacteria are responsible for a variety of human, animal, and plant diseases. The spread of multidrug-resistant Gram-negative bacteria poses a challenge to disease control and highlights the need for novel antimicrobials. Owing to their

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::acbdd329108a3856fe29326d32428f16
https://pubmed.ncbi.nlm.nih.gov/33857480

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A crystallographic snapshot of SARS-CoV-2 main protease maturation process

Autor: A.C.M. Zeri, Andre S. Godoy, Higor Vinícius Dias Rosa, A. Douangamath, D. Fearon, Marjorie Caroline Liberato Cavalcanti Freire, F. von Delft, G.D. Noske, R.S. Fernandes, A.F.Z. Nascimento, Humberto D'Muniz Pereira, Glaucius Oliva, G.M.A. Lima, A.M. Nakamura, V.O. Gawriljuk

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Journal of Molecular Biology

SARS-CoV-2 is the causative agent of COVID-19. The dimeric form of the viral Mpro is responsible for the cleavage of the viral polyprotein in 11 sites, including its own N and C-terminus. The lack of structural information for intermediary forms of M

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d8be5caf0449ca3ec7e2df71c823a0f

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Long-range allostery mediates cooperative adenine nucleotide binding by the Ski2-like RNA helicase Brr2

Autor: Marina V. Rodnina, K. Vester, Dmitry Burakovskiy, Markus C. Wahl, Pohl Milón, Eva Absmeier, Tahereh Ghane, Petra Imhof, Karine F. Santos

Publikováno v: The Journal of Biological Chemistry
Journal of Biological Chemistry

Brr2 is an essential Ski2-like RNA helicase that exhibits a unique structure among the spliceosomal helicases. Brr2 harbors a catalytically active N-terminal helicase cassette and a structurally similar but enzymatically inactive C-terminal helicase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ebde8382e3bb7f7e295d497fb6fcc56

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Biochemical and structural characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL family

Autor: Jelena Rajkovic, Juan A. Hermoso, José Berenguer, Elisa Beneventi, Mercedes Sánchez-Costa, Aurelio Hidalgo, Jacobo Cruces, María-Isabel González-Siso, Ana Torrado, Ivanna Rivera, Vega Miguel-Ruano, María L. Rúa, Kamila Knapik, Manuel Becerra, José M. Otero

Publikováno v: Investigo. Repositorio Institucional de la Universidade de Vigo
Universidade de Vigo (UVigo)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Biblos-e Archivo. Repositorio Institucional de la UAM
RUC. Repositorio da Universidade da Coruña
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 1214-1232 (2021)
Computational and Structural Biotechnology Journal
RUC: Repositorio da Universidade da Coruña
Universidade da Coruña (UDC)

Graphical abstract
Highlights • A novel thermophilic esterase discovered from hot-spring metagenomic library. • EstD11 shows broad substrate specificity including substrates of industrial interest. • Atomic resolution crystallographic comp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5cb848bc105fe00f6966a667d7b1477
https://linkinghub.elsevier.com/retrieve/pii/S2001037021000519

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Sensitive and Quantitative Detection of MHC-I Displayed Neoepitopes Using a Semiautomated Workflow and TOMAHAQ Mass Spectrometry

Autor: Lélia Delamarre, Christopher M. Rose, Craig Blanchette, Martine Darwish, Romain Bouziat, Jennie R. Lill, Samuel B. Pollock

Publikováno v: Molecular & Cellular Proteomics : MCP

Advances in several key technologies, including MHC peptidomics, have helped fuel our understanding of basic immune regulatory mechanisms and the identification of T cell receptor targets for the development of immunotherapeutics. Isolating and accur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::947ac153e25533f2a43cef70c902c68f
https://pubmed.ncbi.nlm.nih.gov/34129938

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A conserved arginine residue is critical for stabilizing the N2 FeS cluster in mitochondrial complex I

Autor: Wei Song, Judy Hirst, Maxie M. Roessler, Mikhail A. Hameedi, Daniel N. Grba, Katherine H. Richardson, John J. Wright, Andrew J. Y. Jones

Publikováno v: The Journal of Biological Chemistry

Respiratory complex I (NADH:ubiquinone oxidoreductase), the first enzyme of the electron-transport chain, captures the free energy released by NADH oxidation and ubiquinone reduction to translocate protons across an energy-transducing membrane and dr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75611df039fac8bfd38c2d255fa14341
https://pubmed.ncbi.nlm.nih.gov/33640456

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Discriminative SKP2 Interactions with CDK-Cyclin Complexes Support a Cyclin A-Specific Role in p27KIP1 Degradation

Autor: Judith Reeks, James R. Ault, Martyna W. Pastok, Natalie J. Tatum, Svitlana Korolchuk, Mengxi Liu, Martin E.M. Noble, Richard A Heath, Frank Sobott, Bailey C. Montefiore, D.J. Wood, Lan-Zhen Wang, Michele Pagano, Jane A. Endicott, Marco Salamina, Arnaud Baslé, Stefan T. Arold

Publikováno v: Journal of Molecular Biology

Graphical abstract
Highlights • SKP2 engages a site on the N-terminal lobe of cyclin A. • SKP2 recruits a catalytic CDK2-cyclin A to CDK2-cyclin A-CKS1-p27KIP1-SKP1-SKP2. • The SKP2 and p27KIP1 binding sites on cyclin A are divergent but o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9746668e50adfe7324966d3acc066eea
https://pubmed.ncbi.nlm.nih.gov/33422522

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