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The NIH Almanac

Recent Photos from the National Institute of General Medical Sciences (NIGMS)

For more scientific images, illustrations, and videos, visit the NIGMS Image Gallery.

2010 Photos

a photo of a frog above an illustration of a molecule. Long-time NIGMS grantee Ei-ichi Negishi shared the 2010 Nobel Prize in chemistry with Richard F. Heck and Akira Suzuki for developing carbon-carbon bond-forming methods. The methods, now widely used in the production of substances ranging from medicines to plastics, let scientists bring two molecules very close together. This allows the molecules to couple, form a compound with a new carbon-carbon bond, release the product and be ready for another cycle. To date, NIGMS has supported the research of 74 Nobel Prize winners. (Structure image courtesy of PubChem)
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2009 Photos

a 3D illustration of a ribosome. NIH grantees Venkatraman Ramakrishnan, Thomas A. Steitz, and Ada E. Yonath shared the 2009 Nobel Prize in chemistry for their “studies of the structure and function of the ribosome.”  Ribosomes are the molecular factories that manufacture proteins in humans and other organisms. Knowing the structure and function of the ribosome has helped us understand one of life's most fundamental processes and manipulate it—many of our antibiotics work by disrupting bacterial ribosomes. (Image courtesy of Catherine Lawson, Rutgers University, and the RCSB Protein Data Bank.)
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a microscopic image of chromosomes with visable telomeres. NIH grantees Elizabeth H. Blackburn, Carol W. Greider, and Jack W. Szostak shared the 2009 Nobel Prize in physiology or medicine for their discovery of "how chromosomes are protected by telomeres and the enzyme telomerase." Like the plastic tips of shoelaces, telomeres protect chromosomes and the genetic information they contain. We now know that these chromosomal caps play critical roles in human health and disease. (Image courtesy of Hesed Padilla-Nash and Thomas Ried.)
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2008 Photos

a 3D illustration of a protein structure.

NIH grantees Martin Chalfie and Roger Y. Tsien shared the 2008 Nobel Prize in chemistry with former grantee Osamu Shimomura for their groundbreaking work on green fluorescent protein. This naturally glowing protein found in jellyfish has become a powerful tool for studying molecules inside living cells. (Image courtesy of Roger Tsien, Univeristy of California, San Diego)
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2007 Photos

an image of the enzyme nicotinic acid phosphoribosyltransferase This model of the enzyme nicotinic acid phosphoribosyltransferase is one of more than 2,000 protein structures solved as part of NIGMS's Protein Structure Initiative. Although the enzyme is from a bacterium, its amino acid sequence suggests that it is structurally similar to a clinically important human protein called B-cell colony enhancing factor. (Image courtesy of Berkeley Structural Genomics Center)
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a microscopic image of cells Hailed as a scientific breakthrough, NIGMS grantee James Thomson used human skin cells to create ones that appear to be indistinguishable from embryonic stem cells. In 2007, Thomson and his colleagues reported that they'd reset the skin cells to the embryonic state by supplying them with 4 genes, giving them the potential to become any of the 220 cell types in the body. The new technique is expected to bring stem cells within easier reach of more scientists, providing them with better models for studying many human diseases and possibly speeding the advent of cell-based therapies for conditions such as diabetes and arthritis. This work also was supported by NIH's National Center for Research Resources (NCRR). (Image courtesy of Junying Yu, University of Wisconsin-Madison)
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This page last reviewed on April 5, 2011

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