scholarly journals Retraction notice to “Influence of hygrothermal effect on dynamic buckling of composite slender column” [Compos. Struct. 267 (2021) 113852]

2021 ◽  
Vol 267 ◽  
pp. 114070
Author(s):  
Hong Tang ◽  
Hong-Liang Dai ◽  
Yang Yang
Keyword(s):  
Dynamic Buckling ◽  
Hygrothermal Effect ◽  
Retraction Notice ◽  
Slender Column

RETRACTION NOTICE

2020 ◽  
Vol 06 (02) ◽  
pp. 130-130
Author(s):  
Isha Patel
Keyword(s):  
Retraction Notice

Target-Templated de novo Design of Macrocyclic D-/L-Peptides: Inhibitors of the PD-1/PD-L1 Interaction

2020 ◽  
Author(s):  
Salvador Guardiola ◽  
Monica Varese ◽  
Xavier Roig ◽  
Jesús Garcia ◽  
Ernest Giralt
Keyword(s):  
Protein Interactions ◽  
Cyclic Peptides ◽  
General Framework ◽  
Large Scale ◽  
De Novo ◽  
Inhibitory Effect ◽  
Original Text ◽  
Protein Protein Interactions ◽  
Retraction Notice ◽  
Pharmaceutical Properties

<p>NOTE: This preprint has been retracted by consensus from all authors. See the retraction notice in place above; the original text can be found under "Version 1", accessible from the version selector above.</p><p><br></p><p>------------------------------------------------------------------------</p><p><br></p><p>Peptides, together with antibodies, are among the most potent biochemical tools to modulate challenging protein-protein interactions. However, current structure-based methods are largely limited to natural peptides and are not suitable for designing target-specific binders with improved pharmaceutical properties, such as macrocyclic peptides. Here we report a general framework that leverages the computational power of Rosetta for large-scale backbone sampling and energy scoring, followed by side-chain composition, to design heterochiral cyclic peptides that bind to a protein surface of interest. To showcase the applicability of our approach, we identified two peptides (PD-<i>i</i>3 and PD-<i>i</i>6) that target PD-1, a key immune checkpoint, and work as protein ligand decoys. A comprehensive biophysical evaluation confirmed their binding mechanism to PD-1 and their inhibitory effect on the PD-1/PD-L1 interaction. Finally, elucidation of their solution structures by NMR served as validation of our <i>de novo </i>design approach. We anticipate that our results will provide a general framework for designing target-specific drug-like peptides.<i></i></p>

A Target-Based Method for Designing Heterochiral Cyclic Peptide Binders: De Novo Inhibitors of the PD-1/PD-L1 Interaction

2020 ◽  
Author(s):  
Salvador Guardiola ◽  
Monica Varese ◽  
Xavier Roig ◽  
Jesús Garcia ◽  
Ernest Giralt
Keyword(s):  
Protein Interactions ◽  
Cyclic Peptides ◽  
General Framework ◽  
Large Scale ◽  
Cyclic Peptide ◽  
De Novo ◽  
Inhibitory Effect ◽  
Original Text ◽  
Retraction Notice ◽  
Pharmaceutical Properties

<p>NOTE: This preprint has been retracted by consensus from all authors. See the retraction notice in place above; the original text can be found under "Version 1", accessible from the version selector above.</p><p><br></p><p>------------------------------------------------------------------------</p><p><br></p><p>Peptides, together with antibodies, are among the most potent biochemical tools to modulate challenging protein-protein interactions. However, current structure-based methods are largely limited to natural peptides and are not suitable for designing target-specific binders with improved pharmaceutical properties, such as macrocyclic peptides. Here we report a general framework that leverages the computational power of Rosetta for large-scale backbone sampling and energy scoring, followed by side-chain composition, to design heterochiral cyclic peptides that bind to a protein surface of interest. To showcase the applicability of our approach, we identified two peptides (PD-<i>i</i>3 and PD-<i>i</i>6) that target PD-1, a key immune checkpoint, and work as protein ligand decoys. A comprehensive biophysical evaluation confirmed their binding mechanism to PD-1 and their inhibitory effect on the PD-1/PD-L1 interaction. Finally, elucidation of their solution structures by NMR served as validation of our <i>de novo </i>design approach. We anticipate that our results will provide a general framework for designing target-specific drug-like peptides.<i></i></p>

Target-Templated de novo Design of Macrocyclic D-/L-Peptides: Inhibitors of the PD-1/PD-L1 Interaction

2020 ◽  
Author(s):  
Salvador Guardiola ◽  
Monica Varese ◽  
Xavier Roig ◽  
Jesús Garcia ◽  
Ernest Giralt
Keyword(s):  
Protein Interactions ◽  
Cyclic Peptides ◽  
General Framework ◽  
Large Scale ◽  
De Novo ◽  
Inhibitory Effect ◽  
Original Text ◽  
Protein Protein Interactions ◽  
Retraction Notice ◽  
Pharmaceutical Properties

<p>NOTE: This preprint has been retracted by consensus from all authors. See the retraction notice in place above; the original text can be found under "Version 1", accessible from the version selector above.</p><p><br></p><p>------------------------------------------------------------------------</p><p><br></p><p>Peptides, together with antibodies, are among the most potent biochemical tools to modulate challenging protein-protein interactions. However, current structure-based methods are largely limited to natural peptides and are not suitable for designing target-specific binders with improved pharmaceutical properties, such as macrocyclic peptides. Here we report a general framework that leverages the computational power of Rosetta for large-scale backbone sampling and energy scoring, followed by side-chain composition, to design heterochiral cyclic peptides that bind to a protein surface of interest. To showcase the applicability of our approach, we identified two peptides (PD-<i>i</i>3 and PD-<i>i</i>6) that target PD-1, a key immune checkpoint, and work as protein ligand decoys. A comprehensive biophysical evaluation confirmed their binding mechanism to PD-1 and their inhibitory effect on the PD-1/PD-L1 interaction. Finally, elucidation of their solution structures by NMR served as validation of our <i>de novo </i>design approach. We anticipate that our results will provide a general framework for designing target-specific drug-like peptides.<i></i></p>

Retraction Notice: Improved Level Set Segmentation Algorithm Based on Kernel Fuzzy Particles Swarm Optimization (KFPSO) Clustering for MRI Images

2018 ◽  
Vol 14 ◽  
Author(s):  
G. Elaiyaraja
Keyword(s):  
Medical Imaging ◽  
Level Set ◽  
Current Medical ◽  
Segmentation Algorithm ◽  
Scientific Publishing ◽  
Swarm Optimization ◽  
Original Source ◽  
Level Set Segmentation ◽  
Copyright Violation ◽  
Retraction Notice

The article entitled “Improved Level Set Segmentation Algorithm Based on Kernel Fuzzy Particles Swarm Optimization (KFPSO) Clustering for MRI Images”, by G. Elaiyaraja, P. Epsiba, N. Kumaratharan and G. Suresh, has been retracted. Kindly see Bentham Science Policy on Article retraction at the link given below: (https://www.benthamscience.com/journals/current-medical-imaging/author-guidelines/). This article has been retracted on the request of the Editor. The authors have plagiarized a paper that had already been published in the journal Current Medical Imaging (CMIM) (Formerly: Current Medical Imaging Reviews) 14(3), Page: 389-400. http://www.eurekaselect.com/149444. It is a pre-requisite for authors to declare explicitly that their work is original and has not been published elsewhere. Authors are advised to properly cite the original source to avoid plagiarism and copyright violation. As such this article represents a severe abuse of the scientific publishing system. Bentham Science Publishers takes a very strong view on this matter and apologizes to the readers of the journal for any inconvenience this may cause.

Retraction Notice: A Kind of Effective Method to Improve the Conversion Efficiency of the Solar Cell

2017 ◽  
Vol 10 (1) ◽  
pp. 35-35
Author(s):  
Xing-Fang Jiang ◽  
Xiang-Min Kong ◽  
Xin-Lu Li ◽  
Hong Jiang ◽  
Dong-Dong Chen
Keyword(s):  
Solar Cell ◽  
Conversion Efficiency ◽  
Retraction Notice
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