Bibliografías temáticas / Arginine anchor motif

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Literatura académica sobre el tema "Arginine anchor motif"

Autor: Grafiati
Publicado: 21 de diciembre de 2024
Última modificación: 31 de julio de 2025

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Artículos de revistas sobre el tema "Arginine anchor motif"

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Banroques, Josette, Olivier Cordin, Monique Doère, Patrick Linder, and N. Kyle Tanner. "A Conserved Phenylalanine of Motif IV in Superfamily 2 Helicases Is Required for Cooperative, ATP-Dependent Binding of RNA Substrates in DEAD-Box Proteins." Molecular and Cellular Biology 28, no. 10 (2008): 3359–71. http://dx.doi.org/10.1128/mcb.01555-07.

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ABSTRACT We have identified a highly conserved phenylalanine in motif IV of the DEAD-box helicases that is important for their enzymatic activities. In vivo analyses of essential proteins in yeast showed that mutants of this residue had severe growth phenotypes. Most of the mutants also were temperature sensitive, which suggested that the mutations altered the conformational stability. Intragenic suppressors of the F405L mutation in yeast Ded1 mapped close to regions of the protein involved in ATP or RNA binding in DEAD-box crystal structures, which implicated a defect at this level. In vitro
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2

Tang, Shuiquan, and Elizabeth A. Edwards. "Identification of Dehalobacter reductive dehalogenases that catalyse dechlorination of chloroform, 1,1,1-trichloroethane and 1,1-dichloroethane." Philosophical Transactions of the Royal Society B: Biological Sciences 368, no. 1616 (2013): 20120318. http://dx.doi.org/10.1098/rstb.2012.0318.

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Two novel reductive dehalogenases (RDases) that are highly similar to each other but catalyse distinct dechlorination reactions were identified from Dehalobacter -containing mixed cultures. These two RDases were partially purified from crude protein extracts of anaerobic dechlorinating enrichment cultures using blue native polyacrylamide gel electrophoresis. Gel slices were assayed for dechlorinating activity, and associated proteins were identified using liquid chromatography tandem mass spectrometry with the metagenome of the parent culture as the reference database. The two RDases identifie
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3

James, Eddie A., Antonis K. Moustakas, John Bui, George K. Papadopoulos, and William W. Kwok. "DR1001 presents ‘altered-self’ peptides by accepting citrulline in its binding pockets (49.20)." Journal of Immunology 182, no. 1_Supplement (2009): 49.20. http://dx.doi.org/10.4049/jimmunol.182.supp.49.20.

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Abstract HLA-DRB1*1001 (DR1001) is associated with rheumatoid arthritis, containing the shared epitope (residues 70-74) within its third hypervariable region. It has been suggested that shared epitope alleles bias T cell selection and amplification, perhaps favoring the recognition of common self-peptides. However, the binding motif of DR1001 and its epitopes remain relatively uncharacterized. One recent paper inferred a binding motif for DR1001 by aligning the sequences of eluted peptides, but only two epitopes were available to validate these findings. The objective of this study was to asse
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4

Wentzel, Alexander, Andreas Christmann, Thorsten Adams, and Harald Kolmar. "Display of Passenger Proteins on the Surface ofEscherichia coli K-12 by the Enterohemorrhagic E. coli Intimin EaeA." Journal of Bacteriology 183, no. 24 (2001): 7273–84. http://dx.doi.org/10.1128/jb.183.24.7273-7284.2001.

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ABSTRACT Intimins are members of a family of bacterial adhesins from pathogenic Escherichia coli which specifically interact with diverse eukaryotic cell surface receptors. The EaeA intimin from enterohemorrhagic E. coli O157:H7 contains an N-terminal transporter domain, which resides in the bacterial outer membrane and promotes the translocation of four C-terminally attached passenger domains across the bacterial cell envelope. We investigated whether truncated EaeA intimin lacking two carboxy-terminal domains could be used as a translocator for heterologous passenger proteins. We found that
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5

Safrit, J. T., A. Y. Lee, C. A. Andrews, and R. A. Koup. "A region of the third variable loop of HIV-1 gp120 is recognized by HLA-B7-restricted CTLs from two acute seroconversion patients." Journal of Immunology 153, no. 8 (1994): 3822–30. http://dx.doi.org/10.4049/jimmunol.153.8.3822.

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Abstract HIV-1 envelope-specific CTL clones were isolated from the peripheral blood of two patients from within weeks of seroconversion. These clones were CD8+ and restricted by the HLA-B7 molecule. The minimum epitope recognized by the clones was determined to be the 30-amino acid (aa) sequence RPNNNTRKSI within the third variable (V3) loop of the envelope glycoprotein gp120. The aa sequence of this epitope is consistent with the motif found in naturally processed peptides eluted from HLA-B7 molecules. This region of the V3 loop is reasonably well conserved among clade B and some nonclade B i
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6

Yue, Ling, Liang Shang, and Eric Hunter. "Truncation of the Membrane-Spanning Domain of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Defines Elements Required for Fusion, Incorporation, and Infectivity." Journal of Virology 83, no. 22 (2009): 11588–98. http://dx.doi.org/10.1128/jvi.00914-09.

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ABSTRACT The membrane-spanning domain (MSD) of the envelope (Env) glycoprotein from human (HIV) and simian immunodeficiency viruses plays a key role in anchoring the Env complex into the viral membrane but also contributes to its biological function in fusion and virus entry. In HIV type 1 (HIV-1), it has been predicted to span 27 amino acids, from lysine residue 681 to arginine 707, and encompasses an internal arginine at residue 694. By examining a series of C-terminal-truncation mutants of the HIV-1 gp41 glycoprotein that substituted termination codons for amino acids 682 to 708, we show th
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7

Ali, Hashim, David Noyvert, Jacqueline Hankinson, Gemma Lindsey, Aleksei Lulla, and Valeria Lulla. "The astrovirus N-terminal nonstructural protein anchors replication complexes to the perinuclear ER membranes." PLOS Pathogens 20, no. 7 (2024): e1011959. http://dx.doi.org/10.1371/journal.ppat.1011959.

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An essential aspect of positive-sense RNA virus replication is anchoring the replication complex (RC) to cellular membranes. Positive-sense RNA viruses employ diverse strategies, including co-translational membrane targeting through signal peptides and co-opting cellular membrane trafficking components. Often, N-terminal nonstructural proteins play a crucial role in linking the RC to membranes, facilitating the early association of the replication machinery. Astroviruses utilize a polyprotein strategy to synthesize nonstructural proteins, relying on subsequent processing to form replication-co
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8

Wang, Li, Kangjing Chen, and Zhucheng Chen. "Structural basis of ALC1/CHD1L autoinhibition and the mechanism of activation by the nucleosome." Nature Communications 12, no. 1 (2021). http://dx.doi.org/10.1038/s41467-021-24320-4.

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AbstractChromatin remodeler ALC1 (amplification in liver cancer 1) is crucial for repairing damaged DNA. It is autoinhibited and activated by nucleosomal epitopes. However, the mechanisms by which ALC1 is regulated remain unclear. Here we report the crystal structure of human ALC1 and the cryoEM structure bound to the nucleosome. The structure shows the macro domain of ALC1 binds to lobe 2 of the ATPase motor, sequestering two elements for nucleosome recognition, explaining the autoinhibition mechanism of the enzyme. The H4 tail competes with the macro domain for lobe 2-binding, explaining the
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9

Hsu, Sheng-Chieh, Ching-Yu Lin, Yen-Yi Lin, Colin C. Collins, Chia-Lin Chen, and Hsing-Jien Kung. "TEAD4 as an Oncogene and a Mitochondrial Modulator." Frontiers in Cell and Developmental Biology 10 (May 5, 2022). http://dx.doi.org/10.3389/fcell.2022.890419.

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TEAD4 (TEA Domain Transcription Factor 4) is well recognized as the DNA-anchor protein of YAP transcription complex, which is modulated by Hippo, a highly conserved pathway in Metazoa that controls organ size through regulating cell proliferation and apoptosis. To acquire full transcriptional activity, TEAD4 requires co-activator, YAP (Yes-associated protein) or its homolog TAZ (transcriptional coactivator with PDZ-binding motif) the signaling hub that relays the extracellular stimuli to the transcription of target genes. Growing evidence suggests that TEAD4 also exerts its function in a YAP-i
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10

Gallego-Parrilla, José Jesús, Emmanuele Severi, Govind Chandra, and Tracy Palmer. "Identification of novel tail-anchored membrane proteins integrated by the bacterial twin-arginine translocase." Microbiology 170, no. 2 (2024). http://dx.doi.org/10.1099/mic.0.001431.

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The twin-arginine protein transport (Tat) system exports folded proteins across the cytoplasmic membranes of prokaryotes and the energy transducing-membranes of plant thylakoids and mitochondria. Proteins are targeted to the Tat machinery by N-terminal signal peptides with a conserved twin-arginine motif, and some substrates are exported as heterodimers where the signal peptide is present on one of the partner proteins. A subset of Tat substrates is found in the membrane. Tat-dependent membrane proteins usually have large globular domains and a single transmembrane helix present at the N- or C
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Tesis sobre el tema "Arginine anchor motif"

1

Martin, Franck. "Structural and functional studies of chromatin remodeling complex mamalian SWI / SNF." Electronic Thesis or Diss., Strasbourg, 2024. http://www.theses.fr/2024STRAJ044.

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La chromatine est une structure dynamique régulée par différents mécanismes épigénétiques parmi lesquels le remodelage de la chromatine dépendant de l’ATP comme le SWI/SNF. Leur importance est telle que les mutations des protéines de remodelage de la chromatine sont fortement associées à plusieurs maladies dont le cancer. Par exemple les protéines BCL7, qui sont de nouvelles sous unité centrales récemment identifié du complexe SWI/SNF des mammifère, sont associées à différents types de cancers comme dans le Diffuse Large B-cell Lymphoma (DLBCL). Les informations sur les protéines BCL7 sont à c
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