In a new video on iBiology, NIGMS Director Jon Lorsch discusses the relationship of lab size and funding levels to productivity, diversity and scientific impact.
The talk covers information detailed in previous Feedback Loop posts:
Read the Molecular Biology of the Cell paper mentioned at the end of the video for more discussion of lab size and other topics related to maximizing the return on taxpayers’ investments in fundamental biomedical research .
We’re pleased that two long-time NIGMS grantees have been recognized with the 2015 Nobel Prize in chemistry for their studies of the repair processes that correct damage affecting base pairing or causing a distortion in the helical structure of DNA. This comes on the heels of the 2015 Albert Lasker Basic Medical Research Award, which was also given for discoveries concerning the DNA-damage response.
Paul Modrich and Aziz Sancar, who will share the Nobel Prize with Tomas Lindahl, have received continuous support from us since 1975 and 1982, respectively. By asking questions about basic cellular processes, these scientists have provided a detailed understanding of some of the molecular repair mechanisms involved in health and disease.
Like any groundbreaking research, their studies have raised numerous other important questions. Some of these include: How do cells sense damaged DNA? How are the proteins that repair damaged regions cleared from the DNA after repairs are complete? How can we specifically undermine the DNA repair systems in cancerous cells so that those cells die?
For more details about the Nobel Prize-winning work, see our statement and links to additional material.
The 15-year Protein Structure Initiative (PSI) ended on June 30, 2015. In preparation for the termination of the program, an external committee of structural biologists and biomedical researchers identified high-priority areas for NIGMS’ future support of structural biology and the preservation of certain PSI resources. Here are some of their key recommendations and what we’re planning to do in response.
Continue to support synchrotron beamlines for macromolecular crystallography.
Recognizing the importance of synchrotron beamlines in modern structural biology, we intend to continue to support these community resources. Part of this effort includes using a new funding approach to ensure that NIH-supported investigators have reliable access to mature synchrotron-based resources.
Maintain the technologies that make structural investigations possible at the most advanced level; meet the need for modern cryo-electron microscopy resources.
We’ll continue to use existing grant mechanisms to support structural biology research, including
X-ray crystallography, NMR, cryo-EM and integrative or hybrid methods. To facilitate the use of
cryo-EM for structure determination we have started a program to provide support for consortia of
cryo-EM labs to upgrade their facilities. NIGMS is also developing plans for establishing regional
cryo-EM centers that could provide access to state-of-the-art cryo-EM resources for the broader structural biology community.
On November 5, we’ll host my favorite NIGMS science education event: Cell Day! As in previous years, we hope this free, interactive Web chat geared for middle and high school students will spark interest in cell biology, biochemistry and research careers. Please help us spread the word by letting people in your local schools and communities know about this special event and encouraging them to register. It runs from 10 a.m. to 3 p.m. EST and is open to all.
As the moderator of these Cell Day chats, I’ve fielded a lot of great questions, including “Why are centrioles not found in plant cells?” and “If you cut a cell in half and then turn it upside down will the nucleus, ribosomes, and other parts of the cell fall out?” It’s always amazing to hear what science students are thinking or wondering about. I’m looking forward to seeing what fantastic questions we’ll get this year!