Photo effect on the CD1d-binding ability of azobenzene-attached analogues of α-GalCer

2020 ◽  
Vol 30 (5) ◽  
pp. 126960 ◽  
Author(s):  
Takashi Kanamori ◽  
Tomoki Numata ◽  
Satoshi Kuwabara ◽  
Yasuyuki Ishii ◽  
Hiroshi Watarai ◽  
...  
Keyword(s):  
Binding Ability ◽  
Photo Effect

Treponema, Iron and Neurodegeneration

2018 ◽  
Vol 15 (8) ◽  
pp. 716-722 ◽  
Author(s):  
A. Jolivet-Gougeon ◽  
M. Bonnaure-Mallet
Keyword(s):  
Iron Metabolism ◽  
Plasma Proteins ◽  
Iron Homeostasis ◽  
Neurological Diseases ◽  
Host Cells ◽  
Loss Of Function ◽  
Binding Ability ◽  
Iron Binding Proteins ◽  
Oxidative Species ◽  
Iron Reductase

Spirochetes are suspected to be linked to the genesis of neurological diseases, including neurosyphillis or neurodegeneration (ND). Impaired iron homeostasis has been implicated in loss of function in several enzymes requiring iron as a cofactor, formation of toxic oxidative species, inflammation and elevated production of beta-amyloid proteins. This review proposes to discuss the link that may exist between the involvement of Treponema spp. in the genesis or worsening of ND, and iron dyshomeostasis. Proteins secreted by Treponema can act directly on iron metabolism, with hemin binding ability (HbpA and HbpB) and iron reductase able to reduce the central ferric iron of hemin, iron-containing proteins (rubredoxin, neelaredoxin, desulfoferrodoxin metalloproteins, bacterioferritins etc). Treponema can also interact with cellular compounds, especially plasma proteins involved in iron metabolism, contributing to the virulence of the syphilis spirochetes (e.g. treponemal motility and survival). Fibronectin, transferrin and lactoferrin were also shown to be receptors for treponemal adherence to host cells and extracellular matrix. Association between Treponema and iron binding proteins results in iron accumulation and sequestration by Treponema from host macromolecules during systemic and mucosal infections.

scholarly journals Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure.

1994 ◽  
Vol 14 (11) ◽  
pp. 7557-7568 ◽  
Author(s):  
J Zuo ◽  
R Baler ◽  
G Dahl ◽  
R Voellmy
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Heat Shock ◽  
Dna Binding ◽  
Hydrophobic Interactions ◽  
Coiled Coil ◽  
Heat Shock Transcription Factor ◽  
Single Amino Acid ◽  
Binding Ability ◽  
Heat Shock Element

Heat stress regulation of human heat shock genes is mediated by human heat shock transcription factor hHSF1, which contains three 4-3 hydrophobic repeats (LZ1 to LZ3). In unstressed human cells (37 degrees C), hHSF1 appears to be in an inactive, monomeric state that may be maintained through intramolecular interactions stabilized by transient interaction with hsp70. Heat stress (39 to 42 degrees C) disrupts these interactions, and hHSF1 homotrimerizes and acquires heat shock element DNA-binding ability. hHSF1 expressed in Xenopus oocytes also assumes a monomeric, non-DNA-binding state and is converted to a trimeric, DNA-binding form upon exposure of the oocytes to heat shock (35 to 37 degrees C in this organism). Because endogenous HSF DNA-binding activity is low and anti-hHSF1 antibody does not recognize Xenopus HSF, we employed this system for mapping regions in hHSF1 that are required for the maintenance of the monomeric state. The results of mutagenesis analyses strongly suggest that the inactive hHSF1 monomer is stabilized by hydrophobic interactions involving all three leucine zippers which may form a triple-stranded coiled coil. Trimerization may enable the DNA-binding function of hHSF1 by facilitating cooperative binding of monomeric DNA-binding domains to the heat shock element motif. This view is supported by observations that several different LexA DNA-binding domain-hHSF1 chimeras bind to a LexA-binding site in a heat-regulated fashion, that single amino acid replacements disrupting the integrity of hydrophobic repeats render these chimeras constitutively trimeric and DNA binding, and that LexA itself binds stably to DNA only as a dimer but not as a monomer in our assays.

scholarly journals Disruption of key NADH-binding pocket residues of the Mycobacterium tuberculosis InhA affects DD-CoA binding ability

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Daniel J. Shaw ◽  
Kirsty Robb ◽  
Beatrice V. Vetter ◽  
Madeline Tong ◽  
Virginie Molle ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Binding Pocket ◽  
Binding Ability

scholarly journals Deferoxamine B: A Natural, Excellent and Versatile Metal Chelator

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3255
Author(s):  
Denise Bellotti ◽  
Maurizio Remelli
Keyword(s):  
Metal Ions ◽  
Metal Binding ◽  
Chelation Therapy ◽  
Iron Chelation ◽  
Binding Ability ◽  
Complex Formation Equilibria ◽  
Metal Chelator ◽  
The Past ◽  
Formation Equilibria ◽  
Terminal Amino

Deferoxamine B is an outstanding molecule which has been widely studied in the past decade for its ability to bind iron and many other metal ions. The versatility of this metal chelator makes it suitable for a number of medicinal and analytical applications, from the well-known iron chelation therapy to the most recent use in sensor devices. The three bidentate hydroxamic functional groups of deferoxamine B are the centerpiece of its metal binding ability, which allows the formation of stable complexes with many transition, lanthanoid and actinoid metal ions. In addition to the ferric ion, in fact, more than 20 different metal complexes of deferoxamine b have been characterized in terms of their chemical speciation in solution. In addition, the availability of a terminal amino group, most often not involved in complexation, opens the way to deferoxamine B modification and functionalization. This review aims to collect and summarize the available data concerning the complex-formation equilibria in solutions of deferoxamine B with different metal ions. A general overview of the progress of its applications over the past decade is also discussed, including the treatment of iron overload-associated diseases, its clinical use against cancer and neurodegenerative disorders and its role as a diagnostic tool.

In Vitro PAH-Binding Ability of Lactobacillus brevis TD4

2021 ◽  
pp. 1-17
Author(s):  
Mojtaba Yousefi ◽  
Nasim Khorshidian ◽  
Hedayat Hosseini
Keyword(s):  
Lactobacillus Brevis ◽  
Binding Ability

scholarly journals Nuclear m6A reader YTHDC1 regulates the scaffold function of LINE1 RNA in mouse ESCs and early embryos

2021 ◽  
Author(s):  
Chuan Chen ◽  
Wenqiang Liu ◽  
Jiayin Guo ◽  
Yuanyuan Liu ◽  
Xuelian Liu ◽  
...  
Keyword(s):  
Inner Cell Mass ◽  
Cell Mass ◽  
Embryonic Stem ◽  
Rrna Synthesis ◽  
Binding Ability ◽  
Transcriptome Regulation ◽  
Early Embryos ◽  
Intrinsic Mechanism ◽  
Regulatory Rnas

AbstractN6-methyladenosine (m6A) on chromosome-associated regulatory RNAs (carRNAs), including repeat RNAs, plays important roles in tuning the chromatin state and transcription, but the intrinsic mechanism remains unclear. Here, we report that YTHDC1 plays indispensable roles in the self-renewal and differentiation potency of mouse embryonic stem cells (ESCs), which highly depends on the m6A-binding ability. Ythdc1 is required for sufficient rRNA synthesis and repression of the 2-cell (2C) transcriptional program in ESCs, which recapitulates the transcriptome regulation by the LINE1 scaffold. Detailed analyses revealed that YTHDC1 recognizes m6A on LINE1 RNAs in the nucleus and regulates the formation of the LINE1-NCL partnership and the chromatin recruitment of KAP1. Moreover, the establishment of H3K9me3 on 2C-related retrotransposons is interrupted in Ythdc1-depleted ESCs and inner cell mass (ICM) cells, which consequently increases the transcriptional activities. Our study reveals a role of m6A in regulating the RNA scaffold, providing a new model for the RNA-chromatin cross-talk.

scholarly journals Effects of cobalt-histidine absorbent on aerobic denitrification by Paracoccus versutus LYM

AMB Express ◽  
2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Chaoyue Sun ◽  
Yu Zhang ◽  
Zhenping Qu ◽  
Jiti Zhou
Keyword(s):  
Nitrate Reduction ◽  
Nitrite Reduction ◽  
Aerobic Denitrification ◽  
Chemical Absorption ◽  
Binding Ability ◽  
Biological Reduction ◽  
Distinct Effect ◽  
The Future

AbstractTo overcome the problem that ferrous complexes are easily oxidized by O2 and then lose NO binding ability in the chemical absorption-biological reduction (CABR) process, cobalt(II)-histidine [Co(II)His] was proposed as an alternative. To evaluate the applicability of Co(II)His, the effects of CoHis absorbent on the aerobic denitrification by Paracoccus versutus LYM were investigated. Results indicated that His significantly promoted nitrite reduction. The inhibition effects of CoHis absorbent could be substantially alleviated by increasing the initial His/Co2+ to 4 or higher. CoHis with concentrations of 4, 8, 12, 16 and 20 mM presented no distinct effect on nitrite reduction, but slightly inhibited the reduction of nitrate, resulting in longer lag of nitrate reduction, and obviously promoted the growth of strain LYM. In the presence of 5, 10, 15 and 20 mM CoHis absorbent, the main denitrification product was N2 (not less than 95.0%). This study is of significance in verifying the applicability of Co(II)His in the CABR process, and provides a referable CoHis absorbent concentration as 20 mM with an initial His/Co2+ of 4 for the future experiments.

scholarly journals Novel Cell Permeable Polymers of N-Substituted L-2,3-Diaminopropionic Acid (DAPEGs) and Cellular Consequences of Their Interactions with Nucleic Acids

2021 ◽  
Vol 22 (5) ◽  
pp. 2571
Author(s):  
Anita Romanowska ◽  
Katarzyna Węgrzyn ◽  
Katarzyna Bury ◽  
Emilia Sikorska ◽  
Aleksandra Gnatek ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Plasmid Dna ◽  
Main Chain ◽  
Cell Permeability ◽  
Binding Ability ◽  
Transfection Efficacy ◽  
Polycationic Polymers ◽  
Diaminopropionic Acid ◽  
Dsdna Binding ◽  
Micromolar Range

The present study aimed to synthesize novel polycationic polymers composed of N-substituted L-2,3-diaminopropionic acid residues (DAPEGs) and investigate their cell permeability, cytotoxicity, and DNA-binding ability. The most efficient cell membrane-penetrating compounds (O2Oc-Dap(GO2)n-O2Oc-NH2, where n = 4, 6, and 8) showed dsDNA binding with a binding constant in the micromolar range (0.3, 3.4, and 0.19 µM, respectively) and were not cytotoxic to HB2 and MDA-MB-231 cells. Selected compounds used in the transfection of a GFP plasmid showed high transfection efficacy and minimal cytotoxicity. Their interaction with plasmid DNA and the increasing length of the main chain of tested compounds strongly influenced the organization and shape of the flower-like nanostructures formed, which were unique for 5/6-FAM-O2Oc-[Dap(GO2)]8-O2Oc-NH2 and typical for large proteins.

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