scholarly journals Parra and the Journal of Scientific Exploration

2021 ◽  
Vol 35 (3) ◽  
pp. 642-645
Author(s):  
Stephen Braude
Keyword(s):  
Scientific Exploration ◽  
Retraction Notice ◽  
Own Name ◽  
Provided Examples

Michael Nahm’s report in this issue of the JSE deftly presents many of the scholarly offenses perpetrated by Alejandro Parra. Some of those not mentioned had to do with Parra’s submissions to the JSE, and I feel it’s important to add those to the record. JSE published a retraction notice earlier this year (Volume 35, Issue 1) and provided examples of Parra’s plagiarism. Moreover, the Journal rejected another paper in which we found substantial plagiarism. But Parra’s boldest effort was his submission, under his own name, of a paper by an Argentinian author, Anna Conforte—in fact, a paper Parra published in his own newsletter. But Parra never indicated that the paper was written by someone else. Several people independently and carefully compared the English submission to the original Spanish. All agreed that Parra apparently simply auto-translated the paper to clumsy English and presented it as his own work.

RETRACTION NOTICE

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

X-Ray Free Electron Laser Facility for Next Generation of Scientific Exploration and Discovery

2011 ◽  
Vol 131 (2) ◽  
pp. 68-71
Author(s):  
Etsuo FUJIWARA ◽  
Eiichi ANAYAMA ◽  
Yuichiro KATSUTA ◽  
Toshiki IZUTANI ◽  
Daichi OKUHARA ◽  
...  
Keyword(s):  
Free Electron ◽  
Free Electron Laser ◽  
Next Generation ◽  
X Ray ◽  
Scientific Exploration ◽  
Laser Facility

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NOTE: This preprint has been retracted by consensus from all authors.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>

Paleontology and stratigraphy of Middle Eocene rock units in the southern Green River and Uinta Basins, Wyoming and Utah

2017 ◽  
Vol 4 ◽  
pp. 1-53 ◽  
Author(s):  
Paul Murphey ◽  
K.E. Townsend ◽  
Anthony Friscia ◽  
James Westgate ◽  
Emmett Evanoff ◽  
...  
Keyword(s):  
Current Knowledge ◽  
Middle Eocene ◽  
Green River Basin ◽  
Green River ◽  
Scientific Exploration ◽  
History Of ◽  
Climatic History ◽  
Field Excursion ◽  
Land Mammal ◽  
Bridger Formation

The Bridger Formation is restricted to the Green River Basin in southwest Wyoming, and the Uinta and Duchesne River Formations are located in the Uinta Basin in Utah. These three rock units and their diverse fossil assemblages are of great scientific importance and historic interest to vertebrate paleontologists. Notably, they are also the stratotypes from oldest to youngest for the three middle Eocene North American Land Mammal Ages—the Bridgerian, Uintan, and Duchesnean. The fossils and sediments of these formations provide a critically important record of biotic, environmental, and climatic history spanning approximately 10 million years (49 to 39 Ma). This article provides a detailed field excursion through portions of the Green River and Uinta Basins that focuses on locations of geologic, paleontologic, and historical interest. In support of the field excursion, we also provide a review of current knowledge of these formations with emphasis on lithostratigraphy, biochronology, depositional, and paleoenvironmental history, and the history of scientific exploration.

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.

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