Sirtuins (SIRTs) are nicotinamide adenine dinucleotide (NAD + )-dependent protein deacetylases, which regulate important biological processes ranging from apoptosis, age-associated pathophysiologies, adipocyte and muscle differentiation, and energy expenditure to gluconeogenesis. Very recently, sirtuin 5 (SIRT5) has received considerable attention due to that it was found to have weak deacetylase activity but strong desuccinylase, demalonylase and deglutarylase activities, and it was also found to be associated with several human diseases such as cancer, Alzheimer's disease, and Parkinson's disease. In this review, we for the first time summarized the structure characteristics, known peptide and small-molecule inhibitors of SIRT5, extracted some clues from current available information and introduced some feasible, practical in silico methods, which might be useful in further efforts to develop new SIRT5 inhibitors.Sirtuin, SIRT5 inhibitor, crystal structure, small-molecule inhibitors, computer-aided drug design Citation:Yang, L., Ma, X., He, Y., Yuan, C., Chen, Q., Li, G., and Chen, X. (2017). Sirtuin 5: a review of structure, known inhibitors and clues for developing new inhibitors. Sci China Life Sci 60, 249-256.

Diabetes mellitus is the most serious and prevalent metabolic disorders worldwide, complications of which can decrease significantly the quality of life and contribute to premature death. Resistance to insulin is a predominant pathophysiological factor of Type 2 diabetes (T2D). Protein tyrosine phosphatase 1B (PTP1B) is an important negative factor of insulin signal and a potent therapeutic target in T2D patients. This review highlights recent advances (2012-2015) in research related to the role of PTP1B in signal transduction processes implicated in pathophysiology of T2D, and novel PTP1B inhibitors with an emphasis on their chemical structures and modes of action.

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This review highlights the recent advances in research related to the role of IDO in immune escape in cancer and novel small-molecule IDO inhibitors with an emphasis on their chemical structures and modes of action.

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Sirt5 is a potential new drug target for the treatment of cancer, Alzheimer's disease, and Parkinson's disease. Given that norharmane is an important chemical synthon for some biologically important compounds and 9‐substituted norharmane derivatives containing a negatively charged carboxyl group may accord with the characteristic of potential Sirt5 inhibitors, a series of novel 9‐substituted norharmane derivatives were synthesized. The chemical structures and purities of all the target compounds were characterized by 1H NMR, 13C NMR, MS, and HPLC. By in vitro SIRT5 inhibitory assays, three compounds (1a, 3a, and 3b) show over 30% inhibition ratios at concentration of 100 µM, and the most active compound 3b has 35% and 52% inhibition ratios at 30 µM and 100 µM, respectively. Docking analysis showed that compound 3b is likely to fit very well on the substrate binding site of Sirt5, and hence, we believe that compound 3b can serve as a lead compound for further efforts to develop specific Sirt5 inhibitors.

Correction for 'IDO as a drug target for cancer immunotherapy: recent developments in IDO inhibitors discovery' by Shan Qian et al., RSC Adv., 2016, 6, 7575-7581. In Fig. 2 of the original manuscript, the structures given for Indoximod and Epacadostat were incorrect. In addition, the structure labelled "GDC-0919" was labelled incorrectly; the correct label is "GDC-0919 analogue". The corrected Fig. 2 is shown below.In Section 3 of the manuscript, "Therapeutic strategies and challenges of IDO inhibitors in cancer immunotherapy", an incorrect IC 50 value was given for Epacadostat, and a citation to ref. 17 of the original manuscript was omitted. The corrected text should read:"Epacadostat (INCB024360) was obtained following a high throughput screening (HTS) of Incyte's corporate collection (IC 50 ¼ 0.072 mM). 17,18 "In Section 4 of the manuscript, "Structure-based IDO inhibitors design", a citation to ref. 26 of the original manuscript was omitted. The corrected text should read:"Based on the co-crystal structure of IDO with PIM, Roerhrig et al. 26 and Huang et al. 30 discovered independently that 1H-1,2,3-triazole might be a new key pharmacophore of potent IDO inhibitors."Additionally, the following discussion should be added to the end of Section 4, and the reference cited as ref. 1 of this correction should be added:"As Roehrig et al. were concentrating on developing 4-aryl triazoles as potent IDO inhibitors, they used computational structurebased methods to design more triazole-based IDO inhibitors with low molecular weight and high efficiency. The most potent compound has an IC 50 value in the nanomolar range both in the enzymatic and in the cellular assays. 1