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10.1111/j.1476-5381.2011.01374.x 152 PalyginO.LaloU.VerkhratskyA.PankratovY

In this work, we unravel the structural foundation underlying human NMT1 activity at the ribosome using high-resolution cryo-electron microscopy of native and reconstituted ribosome-nascent chain complexes (RNCs)

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It was originally discovered by researchers at Tulane Medical School who were looking for a way to stimulate growth hormone production via the growth hormone secretagogue receptor (GHS-R) without simultaneously increasing other hormonesas often observed in exogenous growth hormone (GH) therapy [1]