Disease relevance of WRB

• Additionally, we have accurately located a previously described gene, the WRB gene, between the markers ACTL5-D21S268 within this Down Syndrome Region-2 [1].
• Binding of the 5' terminal sequence of virion RNA (vRNA) to the polymerase activates a tryptophan-rich, cap-binding sequence on the PB2 subunit [2].
• A tryptophan-rich repeat motif that is highly conserved between these proteins, as well as in the reverse transcriptase from simian immunodeficiency virus, has been postulated to be involved in hydrophobic subunit interactions [3].
• A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity [4].
• Among the isolated phage clones, we found that tryptophan-rich peptide sequences appeared repetitively in successive cycles of phage library panning [5].

High impact information on WRB

• Since deblocking was done with piperidine and the peptide was removed from the resin by treatment with ethanolamine, this synthetic protocol prevented oxidation of the indole rings of this tryptophan-rich peptide and reduced truncations produced by acid hydrolysis [6].
• The subjects slept at the laboratory for 2 separate nights so that morning performance could be evaluated after an evening diet containing either tryptophan-rich alpha-lactalbumin or tryptophan-low placebo protein [7].
• These results demonstrate the crucial role of a tryptophan-rich motif in gp41 during a post-CD4-binding step of glycoprotein-mediated fusion [4].
• All these proteins contain several tryptophan-rich repeats designated DWS motifs and internal repeat sequences [8].
• The former encodes a 107-kDa protein containing tryptophan-rich repeats, which may serve to anchor the protein within the cell wall [9].

Chemical compound and disease context of WRB

• The membrane-proximal tryptophan-rich region of the HIV transmembrane glycoprotein, gp41, plays an important role in the membrane fusion reaction [10].
• The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles [10].
• Transmission electron microscopy of S. aureus and Staphylococcus epidermidis treated with CP29 (a 26-amino-acid alpha-helical peptide), CP11CN (a 13-amino-acid, proline- and tryptophan-rich peptide), and Bac2A-NH(2) (a linearized version of the 12-amino-acid loop peptide bactenecin) showed variability in effects on bacterial structure [11].
• Although toxicity of phthalate esters through accumulation of QA remains to be investigated, they may be detrimental by acting as metabolic disrupters when intake of a tryptophan-rich diet and exposure to phthalate esters occur coincidentally [12].

Biological context of WRB

• This paper presents an aquatic food web biomagnification model that simulates inorganic mercury (Hg(II)) and MeHg accumulation in fish tissue and estimates WRB-specific biomagnification factors for resident fish species of concern to stakeholders [13].
• Antimicrobial activity of arginine- and tryptophan-rich hexapeptides: the effects of aromatic clusters, D-amino acid substitution and cyclization [14].
• A multiple alignment of the tryptophan-rich regions of the CcsA-, CcmC- and CcmF-like sequences in the genome databases indicates that they represent three different families [15].
• These antibodies are directed against a tryptophan-rich conserved sequence inside the major parasite surface glycoprotein [16].
• A tryptophan-rich motif, which has been proposed to represent a heme binding site in bacterial cytochrome biogenesis proteins (CcmC and CcmF), is functionally important in plastid CcsA [15].

Anatomical context of WRB

• Here we describe the identification and characterization of a new gene, WRB, that maps to 21q22.3 between ACTL5 and HMG 14 and appears to be widely expressed in adult and fetal tissues [17].
• Interferon induction of human tryptophanyl-tRNA synthetase safeguards the synthesis of tryptophan-rich immune-system proteins: a hypothesis [18].
• The fungicidal effect and mechanism of a tryptophan-rich 13-mer peptide, indolicidin derived from granules of bovine neutrophils, were investigated [19].
• Our physiological tests indicate, that the orange pigmentation of the serosa induced by the ovicide results from a disturbance of the tryptophan/ommochrome pathway serving the excretion of potentially toxic metabolites of tryptophan-rich proteins [20].
• Two have cleared their jaundice but have biochemical evidence of hepatitis and hepatomegaly, four have congenital heart disease 5/6 posterior embryotoxon, 2/6 butterfly vertebrae, 4/6 hyperlipidaemia and 4/6 failure to thrive [21].

Associations of WRB with chemical compounds

• In the Willamette River Basin (WRB, Oregon, USA), health advisories currently limit consumption of fish that have accumulated methylmercury (MeHg) to levels posing a potential health risk for humans [13].
• The distance between these two species was found to be less than 20 A. These results have been interpreted to indicate that propranolol, when bound to the beta-adrenergic receptor, is situated such that its naphthyl moiety is inserted into a tryptophan-rich hydrophobic pocket of the receptor [22].
• (i) At the higher temperature, insertion of tryptophan-rich peptides increased the partitioning to the Pluronic phase [23].
• Antimicrobial activity of short arginine- and tryptophan-rich peptides [24].
• A method is presented by which prealbumin (thyroxine-binding prealbumin; tryptophan-rich prealbumin) may be purified to homogeneity from human serum [25].

Other interactions of WRB

• Present experiments were performed on unusually tryptophan-rich protein, bacterial penicillin acylase (28 Trp per dimer of 82 kDa) and were aimed to extend these observations [26].

Analytical, diagnostic and therapeutic context of WRB

• Wheat-germ lectin affinity chromatography yielded membrane-enriched fractions of RBS, RL and whole rat brain (WRB) [27].
• We report here on an in situ atomic force microscopy study of the interaction of indolicidin, a tryptophan-rich antimicrobial peptide, with phase-segregated zwitterionic DOPC/DSPC supported planar bilayers [28].
• Solvent-dependent structure of two tryptophan-rich antimicrobial peptides and their analogs studied by FTIR and CD spectroscopy [29].

References