Retracted systematic reviews continued to be frequently cited: a citation analysis.

Background And Objectives: To survey the citations of retracted non-Cochrane systematic reviews (SRs) in scientific literature.

Methods: We searched the Web of Science and Google Scholar from their inception to 30 April 2020 to find the citations of 153 previously identified retracted non-Cochrane SRs. We calculated the numbers of citations before and after retraction separately.

Grape Seed Proanthocyanidins Inhibit Migration and Invasion of Bladder Cancer Cells by Reversing EMT through Suppression of TGF- Signaling Pathway.

Bladder cancer (BC) is the most common cancer of the urinary system. Despite advances in diagnosis and therapy, the prognosis is still poor because of recurrence and metastasis. Epithelial-mesenchymal transition (EMT) is considered to play an important role in the invasion and metastasis of BC.

More consideration is needed for retracted non-Cochrane systematic reviews in medicine: a systematic review.

Objective: To analyze the retraction status and reasons of non-Cochrane systematic reviews (SRs) in medicine.

Study Design And Setting: MEDLINE, Embase, Retraction Watch Database and Google Scholar were systematically searched to find all retracted non-Cochrane SRs.

Results: Of 159 non-Cochrane SRs in medicine retracted between 2004 and 2020, more than 70% were led by authors from China and affiliated with hospitals.

New synthetic route for RGD tripeptide.

A new route was employed to synthesize RGD. First, Gly-Asp dipeptide was synthesized by a novel chemical method in two steps, including chloroacetylation of L-aspartic acid and ammonolysis of chloroacetyl L-aspartic acid. Second, Nalpha-Z- L-Arginine was reacted with Gly-Asp to synthesize RGD by the N-carboxyanhydride method.

Synthesis of tetrapeptide Bz-RGDS-NH2 by a combination of chemical and enzymatic methods.

The tetrapeptide Bz-Arg-Gly-Asp-Ser-NH(2) (Bz-RGDS-NH(2)) was successfully synthesized by a combination of chemical and enzymatic methods in this study. Firstly, the precursor tripeptide Gly-Asp-Ser-NH(2) (GDS-NH(2)) was synthesized by a novel chemical method in four steps including chloroacetylation of l-aspartic acid, synthesis of chloroacetyl l-aspartic acid anhydride, the synthesis of ClCH(2)COAsp-SerOMe and ammonolysis of ClCH(2)COAsp-SerOMe. Secondly, lipase (PPL) was used to catalyze the formation of Bz-RGDS-NH(2) in aqueous water-miscible organic cosolvent systems using Bz-Arg-OEt as the acyl donor and GDS-NH(2) as the nucleophile.

Alcalase-catalyzed, kinetically controlled synthesis of a precursor dipeptide of RGDS in organic solvents.

The protease-catalyzed, kinetically controlled synthesis of a precursor dipeptide of RGDS, Z-Asp-Ser-NH2 in organic solvents was studied. Alcalase, an industrial alkaline protease, was used to catalyze the synthesis of the target dipeptide in water-organic cosolvents systems with Z-Asp-OMe as the acyl donor and Ser-NH2 as the nucleophile. Acetonitrile was selected as the organic solvent from acetonitrile, ethanol, methanol, DMF, DMSO, ethyl acetate, 2-methyl-2-propanol, and chloroform tested under the experimental conditions.

Synthesis of a precursor dipeptide of RGDS (Arg-Gly-Asp-Ser) catalysed by the industrial protease alcalase.

Synthesis of Bz-Arg-Gly-NH(2) (N-benzoylargininylglycinamide) [a precursor dipeptide of RGDS (Arg-Gly-Asp-Ser)] catalysed by protease in water/organic co-solvent systems was studied. Starting substrates were N-benzoyl-L-arginine ethyl ester hydrochloride (acyl donor) and glycinamide (nucleophile). Acetonitrile was selected as the organic solvent.

Chemo-enzymatic synthesis of tripeptide RGD diamide in organic solvents.

The tripeptide BzArgGlyAsp(NH(2))(2) was synthesized by a combination of chemical and enzymatic methods in this study. First of all, GlyAsp(NH(2))(2) was synthesized by a novel chemical method in three steps including chloroacetylation of L-aspartic acid, esterification of chloroacetyl L-aspartic acid and ammonolysis of chloroacetyl L-aspartic acid diethyl ester. Secondly, kinetically controlled synthesis of BzArgGlyAsp(NH(2))(2) catalyzed by trypsin in organic solvent was conducted.