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  • January 1, 2018
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Featured Post
 
Since MSRI’s inception, Dr. Greenstein has completed the renovation of the MSRI laboratory and has made significant progress in identifying the cause of MS as well as developing a potential treatment. MSRI needs your help to take Dr. Greenstein’s research to the next level. Please consider purchasing an engraved tile to be placed in the MSRI Laboratory. The tile may honor a loved one, friend or the many lives affected by this disabling disease. Help MSRI FIND the cause, STOP the progression, and CURE MS.

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  • February 24, 2019
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Listen Up! Sunday, February 24 at 6 am:

MSRI Board Member Ernie Alvino and former Philadelphia Flyer, Hall of Famer, Brian Propp discuss our March 10 celebrity hockey game on Philadelphia Agenda with Brad Segal.

You can listen on 101.1 FM (B101) FM, 98.1 FM (WOGL) or 96.5 FM (WTDY)

https://wogl.radio.com/media/audio-channel/2019-02-24-philaagenda-ms-research-institute

Thank you for helping to Find, Stop, and Cure MS!

  • December 14, 2018
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December 14, 2018

Dear Supporter,

As we approach the end of the year I would like to thank you for your ongoing support. This has enabled usto continue work at full speed in the laboratory.

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  • August 21, 2018
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The immune system has an inherent contradiction in the way it functions – the major role of the immune system is to fight off the invasion of our bodies by bacteria, fungi, viruses and parasites; but in order to accomplish this, immune cells need to recognize our own tissues so that they can determine what is foreign when we have an infection.

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  • August 20, 2018
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Jeffrey I. Greenstein, M.D.
President, MSRI

August 20, 2018

Dear Friend and Supporter

I am pleased to share with you some of the groundbreaking discoveries made at MSRI over the last few months due to your generous support.

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  • August 10, 2018
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2018 May 30. doi: 10.1089/rej.2017.2049

Abstract

Proteostasis, which includes the repair and disposal of misfolded proteins, depends, in part, on the activity of heat shock proteins (HSPs), a well-known class of chaperone molecules. When this process fails, abnormally folded proteins may accumulate in cells, tissues, and blood. These species are a hallmark of protein aggregation diseases, but also amass during aging, often in the absence of an identified clinical disorder.

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