scholarly journals SUMO-Mimicking Peptides Inhibiting Protein SUMOylation

ChemBioChem ◽  
2014 ◽  
Vol 15 (18) ◽  
pp. 2662-2666 ◽  
Author(s):  
Bo Zhao ◽  
Eric B. Villhauer ◽  
Karan Bhuripanyo ◽  
Hiroaki Kiyokawa ◽  
Hermann Schindelin ◽  
...  
Keyword(s):  
Inhibiting Protein ◽  
Mimicking Peptides ◽  
Protein Sumoylation

scholarly journals Back Cover: SUMO-Mimicking Peptides Inhibiting Protein SUMOylation (ChemBioChem 18/2014)

ChemBioChem ◽  
2014 ◽  
Vol 15 (18) ◽  
pp. 2792-2792
Author(s):  
Bo Zhao ◽  
Eric B. Villhauer ◽  
Karan Bhuripanyo ◽  
Hiroaki Kiyokawa ◽  
Hermann Schindelin ◽  
...  
Keyword(s):  
Back Cover ◽  
Inhibiting Protein ◽  
Mimicking Peptides ◽  
Protein Sumoylation

The effects of rutin and troxerutin on stabilizing SOD1 and inhibiting protein aggregation

2020 ◽  
Vol 34 (6) ◽  
Author(s):  
Xiaoyu Zhuang ◽  
Bing Zhao ◽  
Zhiqiang Liu ◽  
Fengrui Song ◽  
Jianzhong Lu
Keyword(s):  
Protein Aggregation ◽  
Inhibiting Protein

scholarly journals Impact of porous nanomaterials on inhibiting protein aggregation behaviour

RSC Advances ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 3354-3362
Author(s):  
Munmun Bardhan ◽  
Sandip Dolui ◽  
Siddhi Chaudhuri ◽  
Uttam Paul ◽  
Gaurav Bhattacharjee ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Physiological Conditions ◽  
Intrinsically Disordered ◽  
Aggregation Behaviour ◽  
Inhibiting Protein ◽  
Porous Nanomaterials

Aggregation of intrinsically disordered as well as the ordered proteins under certain premises or physiological conditions leads to pathological disorder.

scholarly journals Correction: Rational design of a stapled JAZ9 peptide inhibiting protein–protein interaction of a plant transcription factor

2021 ◽  
Author(s):  
Kaho Suzuki ◽  
Yousuke Takaoka ◽  
Minoru Ueda
Keyword(s):  
Transcription Factor ◽  
Protein Interaction ◽  
Rational Design ◽  
Protein Protein Interaction ◽  
Inhibiting Protein

Correction for ‘Rational design of a stapled JAZ9 peptide inhibiting protein–protein interaction of a plant transcription factor’ by Kaho Suzuki et al., RSC Chem. Biol., 2021, DOI: 10.1039/d0cb00204f.

scholarly journals 1,2,3-Triazoles as Biomimetics in Peptide Science

Molecules ◽  
2021 ◽  
Vol 26 (10) ◽  
pp. 2937
Author(s):  
Naima Agouram ◽  
El Mestafa El Hadrami ◽  
Abdeslem Bentama
Keyword(s):  
Enzymatic Degradation ◽  
Triazole Ring ◽  
Biologically Active ◽  
Amide Bond ◽  
Biologically Relevant ◽  
Amide Bonds ◽  
Natural Peptides ◽  
Mimicking Peptides ◽  
Chemical Mediators

Natural peptides are an important class of chemical mediators, essential for most vital processes. What limits the potential of the use of peptides as drugs is their low bioavailability and enzymatic degradation in vivo. To overcome this limitation, the development of new molecules mimicking peptides is of great importance for the development of new biologically active molecules. Therefore, replacing the amide bond in a peptide with a heterocyclic bioisostere, such as the 1,2,3-triazole ring, can be considered an effective solution for the synthesis of biologically relevant peptidomimetics. These 1,2,3-triazoles may have an interesting biological activity, because they behave as rigid link units, which can mimic the electronic properties of amide bonds and show bioisosteric effects. Additionally, triazole can be used as a linker moiety to link peptides to other functional groups.

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