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This is a searchable collection of scientific photos, illustrations, and videos. The images and videos in this gallery are licensed under Creative Commons Attribution Non-Commercial ShareAlike 3.0. This license lets you remix, tweak, and build upon this work non-commercially, as long as you credit and license your new creations under identical terms.
2750: Antibodies in silica honeycomb
2750: Antibodies in silica honeycomb
Antibodies are among the most promising therapies for certain forms of cancer, but patients must take them intravenously, exposing healthy tissues to the drug and increasing the risk of side effects. A team of biochemists packed the anticancer antibodies into porous silica particles to deliver a heavy dose directly to tumors in mice.
Chenghong Lei, Pacific Northwest National Laboratory & Karl Erik Hellstrom, University of Washington
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3519: HeLa cells
3519: HeLa cells
Scanning electron micrograph of an apoptotic HeLa cell. Zeiss Merlin HR-SEM. See related images 3518, 3520, 3521, 3522.
National Center for Microscopy and Imaging Research
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6999: HIV enzyme
6999: HIV enzyme
These images model the molecular structures of three enzymes with critical roles in the life cycle of the human immunodeficiency virus (HIV). At the top, reverse transcriptase (orange) creates a DNA copy (yellow) of the virus's RNA genome (blue). In the middle image, integrase (magenta) inserts this DNA copy in the DNA genome (green) of the infected cell. At the bottom, much later in the viral life cycle, protease (turquoise) chops up a chain of HIV structural protein (purple) to generate the building blocks for making new viruses. See these enzymes in action on PDB 101’s video A Molecular View of HIV Therapy.
Amy Wu and Christine Zardecki, RCSB Protein Data Bank.
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1293: Sperm cell
2534: Kinases
2534: Kinases
Kinases are enzymes that add phosphate groups (red-yellow structures) to proteins (green), assigning the proteins a code. In this reaction, an intermediate molecule called ATP (adenosine triphosphate) donates a phosphate group from itself, becoming ADP (adenosine diphosphate). See image 2535 for a labeled version of this illustration. Featured in Medicines By Design.
Crabtree + Company
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2454: Seeing signaling protein activation in cells 04
2454: Seeing signaling protein activation in cells 04
Cdc42, a member of the Rho family of small guanosine triphosphatase (GTPase) proteins, regulates multiple cell functions, including motility, proliferation, apoptosis, and cell morphology. In order to fulfill these diverse roles, the timing and location of Cdc42 activation must be tightly controlled. Klaus Hahn and his research group use special dyes designed to report protein conformational changes and interactions, here in living neutrophil cells. Warmer colors in this image indicate higher levels of activation. Cdc42 looks to be activated at cell protrusions.
Related to images 2451, 2452, and 2453.
Related to images 2451, 2452, and 2453.
Klaus Hahn, University of North Carolina, Chapel Hill Medical School
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6538: Pathways: The Fascinating Cells of Research Organisms
6538: Pathways: The Fascinating Cells of Research Organisms
Learn how research organisms, such as fruit flies and mice, can help us understand and treat human diseases. Discover more resources from NIGMS’ Pathways collaboration with Scholastic. View the video on YouTube for closed captioning.
National Institute of General Medical Sciences
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6928: Axolotls showing nervous system components
6928: Axolotls showing nervous system components
Axolotls—a type of salamander—that have been genetically modified so that various parts of their nervous systems glow purple and green. Researchers often study axolotls for their extensive regenerative abilities. They can regrow tails, limbs, spinal cords, brains, and more. The researcher who took this image focuses on the role of the peripheral nervous system during limb regeneration.
This image was captured using a stereo microscope.
Related to images 6927 and 6932.
This image was captured using a stereo microscope.
Related to images 6927 and 6932.
Prayag Murawala, MDI Biological Laboratory and Hannover Medical School.
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1081: Natcher Building 01
1081: Natcher Building 01
NIGMS staff are located in the Natcher Building on the NIH campus.
Alisa Machalek, National Institute of General Medical Sciences
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3332: Polarized cells- 01
3332: Polarized cells- 01
Cells move forward with lamellipodia and filopodia supported by networks and bundles of actin filaments. Proper, controlled cell movement is a complex process. Recent research has shown that an actin-polymerizing factor called the Arp2/3 complex is the key component of the actin polymerization engine that drives amoeboid cell motility. ARPC3, a component of the Arp2/3 complex, plays a critical role in actin nucleation. In this photo, the ARPC3+/+ fibroblast cells were fixed and stained with Alexa 546 phalloidin for F-actin (red) and DAPI to visualize the nucleus (blue). ARPC3+/+ fibroblast cells with lamellipodia leading edge. Related to images 3328, 3329, 3330, 3331, and 3333.
Rong Li and Praveen Suraneni, Stowers Institute for Medical Research
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1056: Skin cross-section
1056: Skin cross-section
Cross-section of skin anatomy shows layers and different tissue types.
National Institutes of Health Medical Arts
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1101: Red blood cells
1101: Red blood cells
This image of human red blood cells was obtained with the help of a scanning electron microscope, an instrument that uses a finely focused electron beam to yield detailed images of the surface of a sample.
Tina Weatherby Carvalho, University of Hawaii at Manoa
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3648: Symmetrically and asymmetrically elongating cells
3648: Symmetrically and asymmetrically elongating cells
Merged fluorescent images of symmetrically (left) or asymmetrically (right) elongating HeLa cells at the end of early anaphase (magenta) and late anaphase (green). Chromosomes and cortical actin are visualized by expressing mCherry-histone H2B and Lifeact-mCherry. Scale bar, 10µm. See the PubMed abstract of this research.
Tomomi Kiyomitsu and Iain M. Cheeseman, Whitehead Institute for Biomedical Research
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6899: Epithelial cell migration
6899: Epithelial cell migration
High-resolution time lapse of epithelial (skin) cell migration and wound healing. It shows an image taken every 13 seconds over the course of almost 14 minutes. The images were captured with quantitative orientation-independent differential interference contrast (DIC) microscope (left) and a conventional DIC microscope (right).
More information about the research that produced this video can be found in the Journal of Microscopy paper “An Orientation-Independent DIC Microscope Allows High Resolution Imaging of Epithelial Cell Migration and Wound Healing in a Cnidarian Model” by Malamy and Shribak.
More information about the research that produced this video can be found in the Journal of Microscopy paper “An Orientation-Independent DIC Microscope Allows High Resolution Imaging of Epithelial Cell Migration and Wound Healing in a Cnidarian Model” by Malamy and Shribak.
Michael Shribak, Marine Biological Laboratory/University of Chicago.
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3252: Neural circuits in worms similar to those in humans
3252: Neural circuits in worms similar to those in humans
Green and yellow fluorescence mark the processes and cell bodies of some C. elegans neurons. Researchers have found that the strategies used by this tiny roundworm to control its motions are remarkably similar to those used by the human brain to command movement of our body parts. From a November 2011 University of Michigan news release.
Shawn Xu, University of Michigan
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3724: Snowflake DNA origami
3724: Snowflake DNA origami
An atomic force microscopy image shows DNA folded into an intricate, computer-designed structure. The image is featured on Biomedical Beat blog post Cool Images: A Holiday-Themed Collection. For more background on DNA origami, see Cool Image: DNA Origami. See also related image 3690.
Hao Yan, Arizona State University
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3745: Serum albumin structure 2
3745: Serum albumin structure 2
Serum albumin (SA) is the most abundant protein in the blood plasma of mammals. SA has a characteristic heart-shape structure and is a highly versatile protein. It helps maintain normal water levels in our tissues and carries almost half of all calcium ions in human blood. SA also transports some hormones, nutrients and metals throughout the bloodstream. Despite being very similar to our own SA, those from other animals can cause some mild allergies in people. Therefore, some scientists study SAs from humans and other mammals to learn more about what subtle structural or other differences cause immune responses in the body.
Related to entries 3744 and 3746
Related to entries 3744 and 3746
Wladek Minor, University of Virginia
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6755: Honeybee brain
6755: Honeybee brain
Insect brains, like the honeybee brain shown here, are very different in shape from human brains. Despite that, bee and human brains have a lot in common, including many of the genes and neurochemicals they rely on in order to function. The bright-green spots in this image indicate the presence of tyrosine hydroxylase, an enzyme that allows the brain to produce dopamine. Dopamine is involved in many important functions, such as the ability to experience pleasure. This image was captured using confocal microscopy.
Gene Robinson, University of Illinois at Urbana-Champaign.
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5872: Mouse retina close-up
5872: Mouse retina close-up
Keunyoung ("Christine") Kim National Center for Microscopy and Imaging Research (NCMIR)
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6748: Human retinal organoid
6748: Human retinal organoid
A replica of a human retina grown from stem cells. It shows rod photoreceptors (nerve cells responsible for dark vision) in green and red/green cones (nerve cells responsible for red and green color vision) in red. The cell nuclei are stained blue. This image was captured using a confocal microscope.
Kevin Eliceiri, University of Wisconsin-Madison.
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6805: Staphylococcus aureus aggregating upon contact with synovial fluid
6805: Staphylococcus aureus aggregating upon contact with synovial fluid
Staphylococcus aureus bacteria (green) grouping together upon contact with synovial fluid—a viscous substance found in joints. The formation of groups can help protect the bacteria from immune system defenses and from antibiotics, increasing the likelihood of an infection. This video is a 1-hour time lapse and was captured using a confocal laser scanning microscope.
More information about the research that produced this video can be found in the Journal of Bacteriology paper "In Vitro Staphylococcal Aggregate Morphology and Protection from Antibiotics Are Dependent on Distinct Mechanisms Arising from Postsurgical Joint Components and Fluid Motion" by Staats et al.
Related to images 6803 and 6804.
More information about the research that produced this video can be found in the Journal of Bacteriology paper "In Vitro Staphylococcal Aggregate Morphology and Protection from Antibiotics Are Dependent on Distinct Mechanisms Arising from Postsurgical Joint Components and Fluid Motion" by Staats et al.
Related to images 6803 and 6804.
Paul Stoodley, The Ohio State University.
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2375: Protein purification robot
2375: Protein purification robot
Irina Dementieva, a biochemist, and Youngchang Kim, a biophysicist and crystallographer, work with the first robot of its type in the U.S. to automate protein purification. The robot, which is housed in a refrigerator, is an integral part of the Midwest Structural Genomics Center's plan to automate the protein crystallography process.
Midwest Center for Structural Genomics
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2483: Trp_RS - tryptophanyl tRNA-synthetase family of enzymes
2483: Trp_RS - tryptophanyl tRNA-synthetase family of enzymes
This image represents the structure of TrpRS, a novel member of the tryptophanyl tRNA-synthetase family of enzymes. By helping to link the amino acid tryptophan to a tRNA molecule, TrpRS primes the amino acid for use in protein synthesis. A cluster of iron and sulfur atoms (orange and red spheres) was unexpectedly found in the anti-codon domain, a key part of the molecule, and appears to be critical for the function of the enzyme. TrpRS was discovered in Thermotoga maritima, a rod-shaped bacterium that flourishes in high temperatures.
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6569: Cryo-electron tomography of a Caulobacter bacterium
6569: Cryo-electron tomography of a Caulobacter bacterium
3D image of Caulobacter bacterium with various components highlighted: cell membranes (red and blue), protein shell (green), protein factories known as ribosomes (yellow), and storage granules (orange).
Peter Dahlberg, Stanford University.
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6886: Neutrophil-like cells migrating in a microfluidic chip
6886: Neutrophil-like cells migrating in a microfluidic chip
Neutrophil-like cells (blue) in a microfluidic chip preferentially migrating toward LTB4 over fMLP. A neutrophil is a type of white blood cell that is part of the immune system and helps the body fight infection. Both LTB4 and fMLP are molecules involved in immune response. Microfluidic chips are small devices containing microscopic channels, and they are used in a range of applications, from basic research on cells to pathogen detection. The scale bar in this video is 500μm.
Caroline Jones, University of Texas at Dallas.
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6346: Intasome
6346: Intasome
Salk researchers captured the structure of a protein complex called an intasome (center) that lets viruses similar to HIV establish permanent infection in their hosts. The intasome hijacks host genomic material, DNA (white) and histones (beige), and irreversibly inserts viral DNA (blue). The image was created by Jamie Simon and Dmitry Lyumkis. Work that led to the 3D map was published in: Ballandras-Colas A, Brown M, Cook NJ, Dewdney TG, Demeler B, Cherepanov P, Lyumkis D, & Engelman AN. (2016). Cryo-EM reveals a novel octameric integrase structure for ?-retroviral intasome function. Nature, 530(7590), 358—361
National Resource for Automated Molecular Microscopy http://nramm.nysbc.org/nramm-images/ Source: Bridget Carragher
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2378: Most abundant protein in M. tuberculosis
2378: Most abundant protein in M. tuberculosis
Model of a protein, antigen 85B, that is the most abundant protein exported by Mycobacterium tuberculosis, which causes most cases of tuberculosis. Antigen 85B is involved in building the bacterial cell wall and is an attractive drug target. Based on its structure, scientists have suggested a new class of antituberculous drugs.
Mycobacterium Tuberculosis Center, PSI
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3427: Antitoxin GhoS (Illustration 1)
3427: Antitoxin GhoS (Illustration 1)
Structure of the bacterial antitoxin protein GhoS. GhoS inhibits the production of a bacterial toxin, GhoT, which can contribute to antibiotic resistance. GhoS is the first known bacterial antitoxin that works by cleaving the messenger RNA that carries the instructions for making the toxin. More information can be found in the paper: Wang X, Lord DM, Cheng HY, Osbourne DO, Hong SH, Sanchez-Torres V, Quiroga C, Zheng K, Herrmann T, Peti W, Benedik MJ, Page R, Wood TK. A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS. Nat Chem Biol. 2012 Oct;8(10):855-61. Related to 3428.
Rebecca Page and Wolfgang Peti, Brown University and Thomas K. Wood, Pennsylvania State University
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2385: Heat shock protein complex from Methanococcus jannaschii
2385: Heat shock protein complex from Methanococcus jannaschii
Model based on X-ray crystallography of the structure of a small heat shock protein complex from the bacteria, Methanococcus jannaschii. Methanococcus jannaschii is an organism that lives at near boiling temperature, and this protein complex helps it cope with the stress of high temperature. Similar complexes are produced in human cells when they are "stressed" by events such as burns, heart attacks, or strokes. The complexes help cells recover from the stressful event.
Berkeley Structural Genomics Center, PSI-1
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2404: Bovine milk alpha-lactalbumin (2)
2404: Bovine milk alpha-lactalbumin (2)
Crystals of bovine milk alpha-lactalbumin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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2524: Plasma membrane (with labels)
2524: Plasma membrane (with labels)
The plasma membrane is a cell's protective barrier. See image 2523 for an unlabeled version of this illustration. Featured in The Chemistry of Health.
Crabtree + Company
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5800: Mouse cerebellum in pink and blue
5800: Mouse cerebellum in pink and blue
The cerebellum is the brain's locomotion control center. Found at the base of your brain, the cerebellum is a single layer of tissue with deep folds like an accordion. People with damage to this region of the brain often have difficulty with balance, coordination and fine motor skills.
This image of a mouse cerebellum is part of a collection of such images in different colors and at different levels of magnification from the National Center for Microscopy and Imaging Research (NCMIR). Related to image 5795.
This image of a mouse cerebellum is part of a collection of such images in different colors and at different levels of magnification from the National Center for Microscopy and Imaging Research (NCMIR). Related to image 5795.
National Center for Microscopy and Imaging Research (NCMIR)
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2716: Mycobacterium tuberculosis
2716: Mycobacterium tuberculosis
Mycobacterium tuberculosis, the bacterium that causes tuberculosis, has infected one-quarter of the world's population and causes more than one million deaths each year, according to the World Health Organization.
Reuben Peters, Iowa State University
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3287: Retinal pigment epithelium derived from human ES cells 02
3287: Retinal pigment epithelium derived from human ES cells 02
This image shows a layer of retinal pigment epithelium cells derived from human embryonic stem cells, highlighting the nuclei (red) and cell surfaces (green). This kind of retinal cell is responsible for macular degeneration, the most common cause of blindness. Image and caption information courtesy of the California Institute for Regenerative Medicine. Related to image 3286
David Buckholz and Sherry Hikita, University of California, Santa Barbara, via CIRM
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2383: PanC from M. tuberculosis
2383: PanC from M. tuberculosis
Model of an enzyme, PanC, that is involved in the last step of vitamin B5 biosynthesis in Mycobacterium tuberculosis. PanC is essential for the growth of M. tuberculosis, which causes most cases of tuberculosis, and is therefore a potential drug target.
Mycobacterium Tuberculosis Center, PSI
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1314: Chromosomes after crossing over
1314: Chromosomes after crossing over
Duplicated pair of chromosomes have exchanged material.
Judith Stoffer
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3451: Proteasome
3451: Proteasome
This fruit fly spermatid recycles various molecules, including malformed or damaged proteins. Actin filaments (red) in the cell draw unwanted proteins toward a barrel-shaped structure called the proteasome (green clusters), which degrades the molecules into their basic parts for re-use.
Sigi Benjamin-Hong, Rockefeller University
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3492: Glowing bacteria make a pretty postcard
3492: Glowing bacteria make a pretty postcard
This tropical scene, reminiscent of a postcard from Key West, is actually a petri dish containing an artistic arrangement of genetically engineered bacteria. The image showcases eight of the fluorescent proteins created in the laboratory of the late Roger Y. Tsien, a cell biologist at the University of California, San Diego. Tsien, along with Osamu Shimomura of the Marine Biology Laboratory and Martin Chalfie of Columbia University, share the 2008 Nobel Prize in chemistry for their work on green fluorescent protein-a naturally glowing molecule from jellyfish that has become a powerful tool for studying molecules inside living cells.
Nathan C. Shaner, The Scintillon Institute
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6967: Multinucleated cancer cell
6967: Multinucleated cancer cell
A cancer cell with three nuclei, shown in turquoise. The abnormal number of nuclei indicates that the cell failed to go through cell division, probably more than once. Mitochondria are shown in yellow, and a protein of the cell’s cytoskeleton appears in red. This video was captured using a confocal microscope.
Dylan T. Burnette, Vanderbilt University School of Medicine.
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3635: The eye uses many layers of nerve cells to convert light into sight
3635: The eye uses many layers of nerve cells to convert light into sight
This image captures the many layers of nerve cells in the retina. The top layer (green) is made up of cells called photoreceptors that convert light into electrical signals to relay to the brain. The two best-known types of photoreceptor cells are rod- and cone-shaped. Rods help us see under low-light conditions but can't help us distinguish colors. Cones don't function well in the dark but allow us to see vibrant colors in daylight.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
Wei Li, National Eye Institute, National Institutes of Health
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6534: Mosaicism in C. elegans (White Background)
6534: Mosaicism in C. elegans (White Background)
In the worm C. elegans, double-stranded RNA made in neurons can silence matching genes in a variety of cell types through the transport of RNA between cells. The head region of three worms that were genetically modified to express a fluorescent protein were imaged and the images were color-coded based on depth. The worm on the left lacks neuronal double-stranded RNA and thus every cell is fluorescent. In the middle worm, the expression of the fluorescent protein is silenced by neuronal double-stranded RNA and thus most cells are not fluorescent. The worm on the right lacks an enzyme that amplifies RNA for silencing. Surprisingly, the identities of the cells that depend on this enzyme for gene silencing are unpredictable. As a result, worms of identical genotype are nevertheless random mosaics for how the function of gene silencing is carried out. For more, see journal article and press release. Related to image 6532.
Snusha Ravikumar, Ph.D., University of Maryland, College Park, and Antony M. Jose, Ph.D., University of Maryland, College Park
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6389: Red and white blood cells in the lung
2801: Trajectories of labeled cell receptors
1337: Bicycling cell
1337: Bicycling cell
A humorous treatment of the concept of a cycling cell.
Judith Stoffer
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3364: Nociceptin/orphanin FQ peptide opioid receptor
3364: Nociceptin/orphanin FQ peptide opioid receptor
The receptor is shown bound to an antagonist, compound-24
Raymond Stevens, The Scripps Research Institute
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2358: Advanced Photon Source (APS) at Argonne National Lab
2358: Advanced Photon Source (APS) at Argonne National Lab
The intense X-rays produced by synchrotrons such as the Advanced Photon Source are ideally suited for protein structure determination. Using synchrotron X-rays and advanced computers scientists can determine protein structures at a pace unheard of decades ago.
Southeast Collaboratory for Structural Genomics
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2488: VDAC-1 (1)
2488: VDAC-1 (1)
The structure of the pore-forming protein VDAC-1 from humans. This molecule mediates the flow of products needed for metabolism--in particular the export of ATP--across the outer membrane of mitochondria, the power plants for eukaryotic cells. VDAC-1 is involved in metabolism and the self-destruction of cells--two biological processes central to health.
Related to images 2491, 2494, and 2495.
Related to images 2491, 2494, and 2495.
Gerhard Wagner, Harvard Medical School
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3460: Prion protein fibrils 1
3460: Prion protein fibrils 1
Recombinant proteins such as the prion protein shown here are often used to model how proteins misfold and sometimes polymerize in neurodegenerative disorders. This prion protein was expressed in E. coli, purified and fibrillized at pH 7. Image taken in 2004 for a research project by Roger Moore, Ph.D., at Rocky Mountain Laboratories that was published in 2007 in Biochemistry. This image was not used in the publication.
Ken Pekoc (public affairs officer) and Julie Marquardt, NIAID/ Rocky Mountain Laboratories
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3730: A molecular interaction network in yeast 1
3730: A molecular interaction network in yeast 1
The image visualizes a part of the yeast molecular interaction network. The lines in the network represent connections among genes (shown as little dots) and different-colored networks indicate subnetworks, for instance, those in specific locations or pathways in the cell. Researchers use gene or protein expression data to build these networks; the network shown here was visualized with a program called Cytoscape. By following changes in the architectures of these networks in response to altered environmental conditions, scientists can home in on those genes that become central "hubs" (highly connected genes), for example, when a cell encounters stress. They can then further investigate the precise role of these genes to uncover how a cell's molecular machinery deals with stress or other factors. Related to images 3732 and 3733.
Keiichiro Ono, UCSD
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2559: RNA interference (with labels)
2559: RNA interference (with labels)
RNA interference or RNAi is a gene-silencing process in which double-stranded RNAs trigger the destruction of specific RNAs. See 2558 for an unlabeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
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