Independent, energetic individuals with research experience in either cell biology and/or biochemistry and an interest in secretory systems are invited to apply to our established neurobiology/endocrinology laboratory at the University of Maryland School of Medicine in Baltimore. The laboratory is prediminantly focused on defining the biological roles of two neuroprotective secretory chaperones specific to neurons with regard to blocking protein aggregation in neurodegenerative diseases such as Alzheimer’s and Parkinson’s.

One major funded project involves the study of human prohormone convertase variations (SNPs) in new CRISPR/Cas9 mouse models and endocrine cell lines; in particular, studying SNP effects on hypothalamic cell biology and peptide hormone production and their role in obesity. A second funded project addresses the role of convertase binding proteins that play a role as endogenous secretory chaperones in Alzheimer’s and Parkinson’s diseases.

Please email a current CV, a brief statement of your research interests, and the email addresses and phone numbers of three references, to Dr. Iris Lindberg at A recent Ph.D. as well as at least one first-author paper (in a refereed English-language journal) is required. Possibility of independent funding is highly desirable.

We also currently have rotation openings for graduate students, particularly those interested in neurodegeneration. You will learn basic techniques in the molecular and cell biology of neurons, including construction of CRISPR/Cas9 vectors to knock out selected genes, immunofluorescence, and biochemical assays of protein aggregation.

If you would like to rotate in the lab (you must be currently enrolled in a University of Maryland graduate program), please send an email to Iris Lindberg at A minimal eight week rotation period is required.

Selected Relevant Publications for these two projects:

(Human Obesity SNPs and Mutations)

  • Functional analysis of PCSK2 coding variants: A founder effect in the Old Order Amish population.
    Winters A, Ramos-Molina B, Jarvela TS, Yerges-Armstrong L, Pollin TI, and Lindberg, I. (2017). Diabetes Res Clin Pract. 2017 Jul 3;131:82-90. doi: 10.1016/j.diabres.2017.06.023. [Epub ahead of print]PMID:28719828.
  • Revisiting PC1/3 mutants: dominant-negative effect of endoplasmic reticulum-retained mutants.
    Blanco EH, Ramos-Molina B, Lindberg I.Endocrinology. 2015 J156(10):3625-37. doi: 10.1210/en.2015-1068. Epub 2015 Jul 24.

    Defective transport of the obesity mutant PC1/3 N222D contributes to loss of function.
    Prabhu, Y., Blanco, E.H., Liu, M., Peinado, J.R., Wheeler, M.C., Gekakis, N., Arvan, P., Lindberg, I.(2014) Endocrinology. Jul;155(7):2391-401.PMID:24828610

    Biochemical and cell biological properties of the human prohormone convertase 1/3 Ser357Gly mutation: a PC1/3 hypermorph.
    Blanco, EH, Peinado JR, Martín, MG, and Lindberg, I. (2014) Endocrinology. 2014 Sep;155(9):3434-47 PMID:24932808

    Congenital proprotein convertase 1/3 deficiency causes malabsorptive diarrhea and other endocrinopathies in a pediatric cohort. (2013) Martín MG, Lindberg I, Solorzano-Vargas RS, Wang J, Avitzur Y, Bandsma R, Sokollik C, Lawrence S, Pickett LA, Chen Z, Egritas O, Dalgic B, Albornoz V, de Ridder L, Hulst J, Gok F, Aydoğan A, Al-Hussaini A, Gok DE, Yourshaw M, Wu SV, Cortina G, Stanford S, Georgia S. Gastroenterology.145(1):138-48. PMID:23562752


    The neural chaperone proSAAS blocks α-synuclein fibrillation and neurotoxicity.
    (2016) Jarvela TS, Lam HA, Helwig M, Lorenzen N, Otzen DE, McLean PJ, Maidment NT, Lindberg I.
    Proc Natl Acad Sci U S A. 2016 Aug 9;113(32): PMID:27457957

    Chaperones in Neurodegeneration. (2015) Lindberg I, Shorter J, Wiseman RL, Chiti F, Dickey CA, McLean PJ.J Neurosci. 2015 Oct 14;35(41):13853-9.Review. PMID:26468185

    A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer’s disease. (2014) Hoshino A, Helwig M, Rezaei S, Berridge C, Eriksen JL, Lindberg I. J Neurochem. 2014 Feb;128(3):419-30. PMID:24102330

    The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins. (2013)Helwig M, Hoshino A, Berridge C, Lee SN, Lorenzen N, Otzen DE, Eriksen JL, and Lindberg I. J. Biol. Chem. 11;288(2):1114-24.

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