Výsledky vyhledávání - "Recombinant Proteins/chemistry/genetics/metabolism"

The Third Sodium Binding Site of Na,K-ATPase Is Functionally Linked to Acidic pH-Activated Inward Current

Autor: Jean-Daniel Horisberger, Käthi Geering, Ciming Li

Publikováno v: Journal of Membrane Biology, vol. 213, no. 1, pp. 1-9

Sodium- and potassium-activated adenosine triphosphatases (Na,K-ATPase) is the ubiquitous active transport system that maintains the Na(+) and K(+) gradients across the plasma membrane by exchanging three intracellular Na(+) ions against two extracel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a24eaaf833cecd8886ea5c6f7401890
http://doc.rero.ch/record/319660/files/232_2006_Article_35.pdf

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Insight into the remarkable affinity and selectivity of the aminobenzosuberone scaffold for the M1 aminopeptidases family based on structure analysis

Autor: Peng, G, McEwen, A, Olieric, V, Schmitt, C, Albrecht, S, Cavarelli, Jean, Tarnus, Celine

Publikováno v: Proteins
Proteins, 2017, 85 (8), pp.1413-1421. ⟨10.1002/prot.25301⟩

Aminopeptidases are ubiquitous hydrolases that cleave the N-terminal residues of proteins and oligopeptides. They are broadly distributed throughout all kingdoms of life and have been implicated in a wide variety of physiological processes, including

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::994ef31d4e1a5848d744de518bf2f2ff
https://hal.archives-ouvertes.fr/hal-02161625

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Model for the architecture of caveolae based on a flexible, net-like assembly of Cavin1 and Caveolin discs

Autor: Kay Grünewald, Cedric Leyrat, Pascale Schellenberger, Miriam Carolin Stoeber, Ari Helenius, C. Alistair Siebert

Publikováno v: Proceedings of the National Academy of Sciences, Vol. 113, No 50 (2016) pp. E8069-E8078
'Proceedings of the National Academy of Sciences of the USA ', vol: 113, pages: E8069-E8078 (2016)
Europe PubMed Central

Caveolae are invaginated plasma membrane domains involved in mechanosensing, signaling, endocytosis, and membrane homeostasis. Oligomers of membrane-embedded caveolins and peripherally attached cavins form the caveolar coat whose structure has remain

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff26269255a99a86f789c6ce9c294679
https://doi.org/10.1073/pnas.1616838113

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Sch9 Is a Major Target of TORC1 in Saccharomyces cerevisiae

Autor: Olivier Deloche, Alexandre Soulard, Claudio De Virgilio, James R. Broach, Robbie Loewith, Dorothea Anrather, Howard Riezman, Alexandre Huber, Gustav Ammerer, Michael N. Hall, Soyeon I. Lippman, Valeria Wanke, Jörg Urban, Debdyuti Mukhopadhyay

Publikováno v: Molecular Cell, Vol. 26, No 5 (2007) pp. 663-74

The Target of Rapamycin (TOR) protein is a Ser/Thr kinase that functions in two distinct multiprotein complexes: TORC1 and TORC2. These conserved complexes regulate many different aspects of cell growth in response to intracellular and extracellular

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7842a659903906e994c49760267e190

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Site-directed alkylation and the alternating access model for LacY

Autor: Wenjun Zhang, Isidore Kwaw, H. Ronald Kaback, Pushpa Venkatesan, R L Dunten, Stathis Frillingos, Natalia Ermolova

Publikováno v: Proceedings of the National Academy of Sciences. 104:491-494

In a functional lactose permease mutant from Escherichia coli (LacY) devoid of native Cys residues, almost every residue was replaced individually with Cys and tested for reactivity with the permeant alkylating agent N -ethylmaleimide in right-side-o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::650c7fe87dd30ff82dc9d26045c5221f
https://doi.org/10.1073/pnas.0609968104

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Overlapping binding sites drive allosteric agonism and positive cooperativity in type 4 metabotropic glutamate receptors

Autor: Jesús Giraldo, Jean-Philippe Pin, Amadeu Llebaria, Fanny Malhaire, Pauline Scholler, Cyril Goudet, Xavier Rovira, Patricia González-Bulnes, Jordi Rodrigo

Publikováno v: FASEB Journal
FASEB Journal, Federation of American Society of Experimental Biology, 2015, 29 (1), pp.116--30. ⟨10.1096/fj.14-257287⟩

International audience; Type 4 metabotropic glutamate (mGlu4) receptors are emerging targets for the treatment of various disorders. Accordingly, numerous mGlu4-positive allosteric modulators (PAMs) have been identified, some of which also display ag

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::200889aa0a9b8b9e098b0a511c8504af
https://hal.archives-ouvertes.fr/hal-01943324

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An artificial PPR scaffold for programmable RNA recognition

Autor: Aleksandra Filipovska, Oliver Rackham, Tiongsun Chia, Muhammad Fazril Mohamad Razif, Lional Rajappa, Stéphane Thore, James P. Lingford, Sandrine Claire Coquille

Publikováno v: Nature Communications, Vol. 5 (2014) P. 5729

Pentatricopeptide repeat (PPR) proteins control diverse aspects of RNA metabolism in eukaryotic cells. Although recent computational and structural studies have provided insights into RNA recognition by PPR proteins, their highly insoluble nature and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a89d94ca7401147dde92781d26290630
https://pubmed.ncbi.nlm.nih.gov/25517350

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Crystal structure of an antiviral ankyrin targeting the HIV-1 capsid and molecular modeling of the ankyrin-capsid complex

Autor: Vannajan Sanghiran Lee, Somphot Saoin, Sawitree Nangola, Warachai Praditwongwan, Saw See Hong, Pierre Boulanger, Phimonphan Chuankhayan, Philippe Minard, Chun-Jung Chen, Chatchai Tayapiwatana, Tanchanok Wisitponchai

Publikováno v: JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN
JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN, 2014, 28 (8), pp.869-84. ⟨10.1007/s10822-014-9772-9⟩

International audience; Ankyrins are cellular repeat proteins, which can be genetically modified to randomize amino-acid residues located at defined positions in each repeat unit, and thus create a potential binding surface adaptable to macromolecula

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11c7bff15f4cb9f7fcbc82c237faa300
https://pubmed.ncbi.nlm.nih.gov/24997121

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Death Domain Assembly Mechanism Revealed by Crystal Structure of the Oligomeric PIDDosome Core Complex

Autor: Solange Cuenin, Hyun Ho Park, Jürg Tschopp, Emmanuelle Logette, Thomas Walz, Stefan Raunser, Hao Wu

Publikováno v: Cell, vol. 128, no. 3, pp. 533-46

SummaryProteins of the death domain (DD) superfamily mediate assembly of oligomeric signaling complexes for the activation of caspases and kinases via unknown mechanisms. Here we report the crystal structure of the PIDD DD and RAIDD DD complex, which

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::881aefc92d8fc2a59811f8a7892c7a4e
https://europepmc.org/articles/PMC2908332/

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Inhibition of interleukin 1 receptor/Toll-like receptor signaling through the alternatively spliced, short form of MyD88 is due to its failure to recruit IRAK-4

Autor: Jürg Tschopp, Natalia Olivos, Brian Brissoni, Rudi Beyaert, Sophie Janssens, Kimberly Burns

Publikováno v: The Journal of Experimental Medicine
Journal of Experimental Medicine, vol. 197, no. 2, pp. 263-8

Toll-like receptors (TLRs) and members of the proinflammatory interleukin 1 receptor (IL-1R) family are dependent on the presence of MyD88 for efficient signal transduction. The bipartite nature of MyD88 (N-terminal death domain [DD] and COOH-termina

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::892b88a42b1d95d3eb105ab3d6c2fd49
https://pubmed.ncbi.nlm.nih.gov/12538665

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