马里兰大学神经病理学研究博士后职位

日期:2015-01-02
A funded postdoctoral position is currently available in the Lindberg Secretory Biology Laboratory in the Department of Neurobiology and Anatomy at the University of Maryland Medical School in Baltimore Maryland.

A funded postdoctoral position is currently available in the Lindberg Secretory Biology Laboratory in the Department of Neurobiology and Anatomy at the University of Maryland Medical School in Baltimore, Maryland.

Our research focuses on the role of the proprotein convertases and secretory chaperones in both the proteolytic maturation of peptide signaling peptides as well as in certain neuropathologies (Alzheimer’s, Parkinson’s etc).

We are particularly interested in establishing the role of the known secretory chaperone proteins 7B2 and proSAAS in secretory protein homeostasis. Our recent work has revealed unexpected connections between these secretory proteins in neurodegenerative disease. We are also interested in defining the mechanism by which proprotein convertase 1/3 mutations lead to obesity. Our active collaborations with clinicians who have identified patients with PC1/3 mutations allow us to extend our structural biology work to human disease.

We are seeking a highly motivated candidate to join our team who has:

- a Ph.D. and 0-3 years of relevant postdoctoral experience
- a track record of publications in peer-reviewed journals
- validated experience in cell biology or (preferably) structural biochemistry

Experience with Alzheimer model mouse strains is a plus but is not necessary.

Please send your application as a single PDF document containing a cover letter, a concise summary of previous research, a curriculum vitae including a publication list, and phone and email details for at least 3 references to ilindberg@som.umaryland.edu. For further information, please visit our website: thelindberglab.com

Selected Relevant Publications:

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.

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

A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer’s disease.
Hoshino, A., Helwig, M., Rezaei, S., Berridge, C., Eriksen, J.L., and Lindberg, I. (2013) J. Neurochem. 128(3):419-30.

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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