Most newly synthesized proteins destined for the secretory pathway contain a signal peptide (SP) that triggers cotranslational translocation into the endoplasmic reticulum (ER). However, how small polypeptides undergo ER translocation is not fully understood. In this issue of JBC, Guo et al. describe a mechanism for posttranslational translocation of small secretory proteins featuring a positive charge within the SP N-terminal region. Defects in this element disrupt proper secretion and explain the effects of genetic mutations associated with one type of diabetes.
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Background Although pneumonia is a leading cause of death in New York City (NYC), limited data exist about the settings in which pneumonia ...
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Summary We tested whether prophylactic droperidol and ondansetron, in combination with a moderate dose of dexamethasone, were equally effe...
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by Demin Li, Carol Bentley, Jenna Yates, Maryam Salimi, Jenny Greig, Sarah Wiblin, Tasneem Hassanali, Alison H. Banham Therapeutic monoclon...
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Abstract Dermoscopy has demonstrated clinical benefits in improving early melanoma diagnosis and reducing unnecessary biopsies. Despite th...
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by Sarah K. Sharman, Bianca N. Islam, Yali Hou, Margaux Usry, Allison Bridges, Nagendra Singh, Subbaramiah Sridhar, Satish Rao, Darren D. Br...
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