Postdoctoral Position available

An independent, motivated individual with a strong interest in neurodegenerative disease and substantial research experience in either cell biology and/or biochemistry is sought for an established laboratory at the University of Maryland School of Medicine in Baltimore. The Lindberg laboratory has received funding to establish the mechanism of action of the neuronally-expressed secretory chaperone proSAAS with regard to its known effects in improving cellular outcomes in neurodegenerative disease (Parkinson’s, ALS, and Alzheimer’s). Current projects involve both animal work as well as structure-function analyses of in vitro interactions. Please visit for more information.
If interested, please email a current CV, a brief cover letter concerning your past research as well as career plans, and the email addresses and phone numbers of three references to Dr. Iris Lindberg at

Technical Research Associate

Our Neurobiology laboratory at UMB seeks a full- OR part-time research technician to carry out mostly biochemical and cell biological bench research activities in the general area of neurodegeneration (Alzheimer’s, Parkinson’s and ALS). The ideal candidate will be a new or recent college graduate (BA or BS in a science-related field is required; grade point should be 3.0 or above) who has prior college or summer wet lab research experience. The best fit for this position might be a person taking a year or two off prior to graduate or professional school. The person will be responsible for handling routine laboratory activities (ordering, plasmid purification, cell culture maintenance) but will mostly perform original research activities under the direction of a postdoctoral fellow and/or the lab head. Techniques involved will include, but are likely not limited to, cell culture, immunohistochemistry, protein purification, and spectrophotometric plate assays. We are looking for a helpful, curious, and motivated individual with a deep interest in basic scientific research; an opportunity for publication exists. Please see this lab website for further information on laboratory research interests. If your credentials match the above, please send your resume and the names and contact information of two or three references to Dr. Iris Lindberg at ilindberg at som dot umaryland dot edu. UMB is an EE/AA employer.

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:

Secreted Chaperones in Neurodegeneration
(2020) Chaplot, K., Jarvela, TS and Lindberg, I.
Frontiers in Aging Neuroscience, August 2020 PMID: 33192447

Increased expression and retention of the secretory chaperone proSAAS following cell stress.
(2020)Shakya,M., Yildirim, T., and Lindberg, I. 25(6):943 PMID: 32691307

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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