Synthesis of DNA-Binding Polyamides: Robust Solid-Phase Methods for Coupling Heterocyclic Aromatic Amino Acids

ChemInform ◽  
2003 ◽  
Vol 34 (30) ◽  
Author(s):  
Peter O. Krutzik ◽  
A. Richard Chamberlin
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Solid Phase ◽  
Aromatic Amino Acids

NonO, a non-POU-domain-containing, octamer-binding protein, is the mammalian homolog of Drosophila nonAdiss

1993 ◽  
Vol 13 (9) ◽  
pp. 5593-5603
Author(s):  
Y S Yang ◽  
J H Hanke ◽  
L Carayannopoulos ◽  
C M Craft ◽  
J D Capra ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Protein Binding ◽  
Aromatic Amino Acids ◽  
Courtship Song ◽  
Dna Binding Domain ◽  
Binding Motifs ◽  
Dna And Rna ◽  
Pou Domain ◽  
A Site

We have cloned the ubiquitous form of an octamer-binding, 60-kDa protein (NonO) that appears to be the mammalian equivalent of the Drosophila visual and courtship song behavior protein, no-on-transient A/dissonance (nonAdiss). A region unprecedently rich in aromatic amino acids containing two ribonuclear protein binding motifs is highly conserved between the two proteins. A ubiquitous form of NonO is present in all adult tissues, whereas lymphocytes and retina express unique forms of NonO mRNA. The ubiquitous form contains a potential helix-turn-helix motif followed by a highly charged region but differs from prototypic octamer-binding factors by lacking the POU DNA-binding domain. In addition to its conventional octamer duplex-binding, NonO binds single-stranded DNA and RNA at a site independent of the duplex site.

scholarly journals NonO, a non-POU-domain-containing, octamer-binding protein, is the mammalian homolog of Drosophila nonAdiss.

1993 ◽  
Vol 13 (9) ◽  
pp. 5593-5603 ◽  
Author(s):  
Y S Yang ◽  
J H Hanke ◽  
L Carayannopoulos ◽  
C M Craft ◽  
J D Capra ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Protein Binding ◽  
Aromatic Amino Acids ◽  
Courtship Song ◽  
Dna Binding Domain ◽  
Binding Motifs ◽  
Dna And Rna ◽  
Pou Domain ◽  
A Site

We have cloned the ubiquitous form of an octamer-binding, 60-kDa protein (NonO) that appears to be the mammalian equivalent of the Drosophila visual and courtship song behavior protein, no-on-transient A/dissonance (nonAdiss). A region unprecedently rich in aromatic amino acids containing two ribonuclear protein binding motifs is highly conserved between the two proteins. A ubiquitous form of NonO is present in all adult tissues, whereas lymphocytes and retina express unique forms of NonO mRNA. The ubiquitous form contains a potential helix-turn-helix motif followed by a highly charged region but differs from prototypic octamer-binding factors by lacking the POU DNA-binding domain. In addition to its conventional octamer duplex-binding, NonO binds single-stranded DNA and RNA at a site independent of the duplex site.

DNA binding ligands with in vivo efficacy in murine models of bacterial infection: optimization of internal aromatic amino acids

2004 ◽  
Vol 14 (9) ◽  
pp. 2067-2072 ◽  
Author(s):  
Roland W. Bürli ◽  
Jacob A. Kaizerman ◽  
Jian-Xin Duan ◽  
Peter Jones ◽  
Kirk W. Johnson ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Bacterial Infection ◽  
Aromatic Amino Acids ◽  
Murine Models ◽  
In Vivo Efficacy

The Efficient Preparation of Radiolabeled Aromatic Amino Acids via Cu-Mediated Radiofluorination using Ni-complexes

2019 ◽  
Author(s):  
A Craig ◽  
N Kolks ◽  
E Urusova ◽  
BD Zlatopolskiy ◽  
B Neumaier
Keyword(s):  
Amino Acids ◽  
Aromatic Amino Acids

Long term dietary intake of aromatic amino acids are associated with leptin gene expression in adipose tissues of non-diabetic adults

2018 ◽  
Author(s):  
Golaleh Asghari ◽  
Emad Yuzbashian ◽  
Maryam Zarkesh ◽  
Parvin Mirmiran ◽  
Mehdi Hedayati ◽  
...  
Keyword(s):  
Gene Expression ◽  
Amino Acids ◽  
Dietary Intake ◽  
Aromatic Amino Acids ◽  
Adipose Tissues

Single Amino Acid Based Self-Assemblies of Cysteine and Methionine

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Neutral Condition ◽  
Single Amino Acid ◽  
Binding Assays ◽  
Human Neuroblastoma ◽  
Cytotoxicity Assays ◽  
First Time

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. To get insights into the structure formation, thioflavin T and Congo red binding assays were done which revealed that aggregates may not have amyloid like characteristics. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. The cytotoxicity assays of cysteine and methionine structures were performed on Human Neuroblastoma IMR-32 cells which suggested that aggregates are not cytotoxic in nature and thus, may not have amyloid like etiology. The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.

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