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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.

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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3598: Developing zebrafish fin
3598: Developing zebrafish fin
Originally from the waters of India, Nepal, and neighboring countries, zebrafish can now be found swimming in science labs (and home aquariums) throughout the world. This fish is a favorite study subject for scientists interested in how genes guide the early stages of prenatal development (including the developing fin shown here) and in the effects of environmental contamination on embryos.
In this image, green fluorescent protein (GFP) is expressed where the gene sox9b is expressed. Collagen (red) marks the fin rays, and DNA, stained with a dye called DAPI, is in blue. sox9b plays many important roles during development, including the building of the heart and brain, and is also necessary for skeletal development. At the University of Wisconsin, researchers have found that exposure to contaminants that bind the aryl-hydrocarbon receptor results in the downregulation of sox9b. Loss of sox9b severely disrupts development in zebrafish and causes a life-threatening disorder called campomelic dysplasia (CD) in humans. CD is characterized by cardiovascular, neural, and skeletal defects. By studying the roles of genes such as sox9b in zebrafish, scientists hope to better understand normal development in humans as well as how to treat developmental disorders and diseases.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
In this image, green fluorescent protein (GFP) is expressed where the gene sox9b is expressed. Collagen (red) marks the fin rays, and DNA, stained with a dye called DAPI, is in blue. sox9b plays many important roles during development, including the building of the heart and brain, and is also necessary for skeletal development. At the University of Wisconsin, researchers have found that exposure to contaminants that bind the aryl-hydrocarbon receptor results in the downregulation of sox9b. Loss of sox9b severely disrupts development in zebrafish and causes a life-threatening disorder called campomelic dysplasia (CD) in humans. CD is characterized by cardiovascular, neural, and skeletal defects. By studying the roles of genes such as sox9b in zebrafish, scientists hope to better understand normal development in humans as well as how to treat developmental disorders and diseases.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
Jessica Plavicki
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2791: Anti-tumor drug ecteinascidin 743 (ET-743) with hydrogens 02
2791: Anti-tumor drug ecteinascidin 743 (ET-743) with hydrogens 02
Ecteinascidin 743 (ET-743, brand name Yondelis), was discovered and isolated from a sea squirt, Ecteinascidia turbinata, by NIGMS grantee Kenneth Rinehart at the University of Illinois. It was synthesized by NIGMS grantees E.J. Corey and later by Samuel Danishefsky. Multiple versions of this structure are available as entries 2790-2797.
Timothy Jamison, Massachusetts Institute of Technology
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2503: Focal adhesions (with labels)
2503: Focal adhesions (with labels)
Cells walk along body surfaces via tiny "feet," called focal adhesions, that connect with the extracellular matrix. See image 2502 for an unlabeled version of this illustration.
Crabtree + Company
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3405: Disrupted and restored vasculature development in frog embryos
3405: Disrupted and restored vasculature development in frog embryos
Disassembly of vasculature and reassembly after addition and then washout of 250 µM TBZ in kdr:GFP frogs. Related to images 3403 and 3404.
Hye Ji Cha, University of Texas at Austin
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2350: Mandelate racemase from B. subtilis
2350: Mandelate racemase from B. subtilis
Model of the mandelate racemase enzyme from Bacillus subtilis, a bacterium commonly found in soil.
New York Structural GenomiX Research Consortium, PSI
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2626: Telomeres
2626: Telomeres
The 46 human chromosomes are shown in blue, with the telomeres appearing as white pinpoints. The DNA has already been copied, so each chromosome is actually made up of two identical lengths of DNA, each with its own two telomeres.
Hesed Padilla-Nash and Thomas Ried, the National Cancer Institute, a part of NIH
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3644: Zebrafish embryo
3644: Zebrafish embryo
Just 22 hours after fertilization, this zebrafish embryo is already taking shape. By 36 hours, all of the major organs will have started to form. The zebrafish's rapid growth and see-through embryo make it ideal for scientists studying how organs develop.
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.
Philipp Keller, Bill Lemon, Yinan Wan, and Kristin Branson, Janelia Farm Research Campus, Howard Hughes Medical Institute, Ashburn, Va.
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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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1058: Lily mitosis 01
1058: Lily mitosis 01
A light microscope image shows the chromosomes, stained dark blue, in a dividing cell of an African globe lily (Scadoxus katherinae). This is one frame of a time-lapse sequence that shows cell division in action. The lily is considered a good organism for studying cell division because its chromosomes are much thicker and easier to see than human ones.
Andrew S. Bajer, University of Oregon, Eugene
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2392: Sheep hemoglobin crystal
2392: Sheep hemoglobin crystal
A crystal of sheep hemoglobin protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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5881: Zebrafish larva
5881: Zebrafish larva
You are face to face with a 6-day-old zebrafish larva. What look like eyes will become nostrils, and the bulges on either side will become eyes. Scientists use fast-growing, transparent zebrafish to see body shapes form and organs develop over the course of just a few days. Images like this one help researchers understand how gene mutations can lead to facial abnormalities such as cleft lip and palate in people.
This image won a 2016 FASEB BioArt award. In addition, NIH Director Francis Collins featured this on his blog on January 26, 2017.
This image won a 2016 FASEB BioArt award. In addition, NIH Director Francis Collins featured this on his blog on January 26, 2017.
Oscar Ruiz and George Eisenhoffer, University of Texas MD Anderson Cancer Center, Houston
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2533: Dose response curves
2533: Dose response curves
Dose-response curves determine how much of a drug (X-axis) causes a particular effect, or a side effect, in the body (Y-axis). Featured in Medicines By Design.
Crabtree + Company
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2497: Body toxins (with labels)
2497: Body toxins (with labels)
Body organs such as the liver and kidneys process chemicals and toxins. These "target" organs are susceptible to damage caused by these substances. See image 2496 for an unlabeled version of this illustration.
Crabtree + Company
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3397: Myelinated axons 2
3397: Myelinated axons 2
Top view of myelinated axons in a rat spinal root. Myelin is a type of fat that forms a sheath around and thus insulates the axon to protect it from losing the electrical current needed to transmit signals along the axon. The axoplasm inside the axon is shown in pink. Related to 3396.
Tom Deerinck, National Center for Microscopy and Imaging Research (NCMIR)
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2749: Cytoscape network wiring diagram 2
2749: Cytoscape network wiring diagram 2
This image integrates the thousands of known molecular and genetic interactions happening inside our bodies using a computer program called Cytoscape. Images like this are known as network wiring diagrams, but Cytoscape creator Trey Ideker somewhat jokingly calls them "hairballs" because they can be so complicated, intricate and hard to tease apart. Cytoscape comes with tools to help scientists study specific interactions, such as differences between species or between sick and diseased cells. Related to 2737.
Trey Ideker, University of California, San Diego
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2450: Blood clots show their flex
2450: Blood clots show their flex
Blood clots stop bleeding, but they also can cause heart attacks and strokes. A team led by computational biophysicist Klaus Schulten of the University of Illinois at Urbana-Champaign has revealed how a blood protein can give clots their lifesaving and life-threatening abilities. The researchers combined experimental and computational methods to animate fibrinogen, a protein that forms the elastic fibers that enable clots to withstand the force of blood pressure. This simulation shows that the protein, through a series of events, stretches up to three times its length. Adjusting this elasticity could improve how we manage healthful and harmful clots. NIH's National Center for Research Resources also supported this work. Featured in the March 19, 2008, issue of Biomedical Beat.
Eric Lee, University of Illinois at Urbana-Champaign
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2314: Finding one bug
2314: Finding one bug
A nanometer-sized biosensor can detect a single deadly bacterium in tainted ground beef. How? Researchers attached nanoparticles, each packed with thousands of dye molecules, to an antibody that recognizes the microbe E. coli O157:H7. When the nanoball-antibody combo comes into contact with the E. coli bacterium, it glows. Here is the transition, a single bacterial cell glows brightly when it encounters nanoparticle-antibody biosensors, each packed with thousands of dye molecules.
Weihong Tan, University of Florida in Gainesville
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5759: TEM cross-section of C. elegans (roundworm)
5759: TEM cross-section of C. elegans (roundworm)
The worm Caenorhabditis elegans is a popular laboratory animal because its small size and fairly simple body make it easy to study. Scientists use this small worm to answer many research questions in developmental biology, neurobiology, and genetics. This image, which was taken with transmission electron microscopy (TEM), shows a cross-section through C. elegans, revealing various internal structures.
The image is from a figure in an article published in the journal eLife. There is an annotated version of this graphic at 5760.
The image is from a figure in an article published in the journal eLife. There is an annotated version of this graphic at 5760.
Piali Sengupta, Brandeis University
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2382: PanB from M. tuberculosis (2)
2382: PanB from M. tuberculosis (2)
Model of an enzyme, PanB, from Mycobacterium tuberculosis, the bacterium that causes most cases of tuberculosis. This enzyme is an attractive drug target.
Mycobacterium Tuberculosis Center, PSI-1
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3586: Human blood cells with Borrelia hermsii, a bacterium that causes relapsing fever
3586: Human blood cells with Borrelia hermsii, a bacterium that causes relapsing fever
Relapsing fever is caused by a bacterium and transmitted by certain soft-bodied ticks or body lice. The disease is seldom fatal in humans, but it can be very serious and prolonged. This scanning electron micrograph shows Borrelia hermsii (green), one of the bacterial species that causes the disease, interacting with red blood cells. Micrograph by Robert Fischer, NIAID.
For more information on this see, relapsing fever.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
For more information on this see, relapsing fever.
This image was part of the Life: Magnified exhibit that ran from June 3, 2014, to January 21, 2015, at Dulles International Airport.
NIAID
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2809: Vimentin in a quail embryo
2809: Vimentin in a quail embryo
Video of high-resolution confocal images depicting vimentin immunofluorescence (green) and nuclei (blue) at the edge of a quail embryo yolk. These images were obtained as part of a study to understand cell migration in embryos. An NIGMS grant to Professor Garcia was used to purchase the confocal microscope that collected these images. Related to images 2807 and 2808.
Andrés Garcia, Georgia Tech
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5878: Misfolded proteins within in the mitochondria
5878: Misfolded proteins within in the mitochondria
Misfolded proteins (green) within mitochondria (red). Related to video 5877.
Rong Li rong@jhu.edu Department of Chemical and Biomolecular Engineering, Whiting School of Engineering, Johns Hopkins University, Baltimore, Maryland 21218, USA.
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6851: Himastatin, 360-degree view
6851: Himastatin, 360-degree view
A 360-degree view of the molecule himastatin, which was first isolated from the bacterium Streptomyces himastatinicus. Himastatin shows antibiotic activity. The researchers who created this video developed a new, more concise way to synthesize himastatin so it can be studied more easily.
More information about the research that produced this video can be found in the Science paper “Total synthesis of himastatin” by D’Angelo et al.
Related to images 6848 and 6850.
More information about the research that produced this video can be found in the Science paper “Total synthesis of himastatin” by D’Angelo et al.
Related to images 6848 and 6850.
Mohammad Movassaghi, Massachusetts Institute of Technology.
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1272: Cytoskeleton
1272: Cytoskeleton
The three fibers of the cytoskeleton--microtubules in blue, intermediate filaments in red, and actin in green--play countless roles in the cell.
Judith Stoffer
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3331: mDia1 antibody staining- 02
3331: mDia1 antibody staining- 02
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), mDia1 (green), and DAPI to visualize the nucleus (blue). In ARPC3-/- fibroblast cells, mDia1 is localized at the tips of the filopodia-like structures. Related to images 3328, 3329, 3330, 3332, and 3333.
Rong Li and Praveen Suraneni, Stowers Institute for Medical Research
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2529: Aspirin
2529: Aspirin
Acetylsalicylate (bottom) is the aspirin of today. Adding a chemical tag called an acetyl group (shaded box, bottom) to a molecule derived from willow bark (salicylate, top) makes the molecule less acidic (and easier on the lining of the digestive tract), but still effective at relieving pain. See image 2530 for a labeled version of this illustration. Featured in Medicines By Design.
Crabtree + Company
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2398: RNase A (1)
2398: RNase A (1)
A crystal of RNase A protein created for X-ray crystallography, which can reveal detailed, three-dimensional protein structures.
Alex McPherson, University of California, Irvine
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2792: Anti-tumor drug ecteinascidin 743 (ET-743) with hydrogens 03
2792: Anti-tumor drug ecteinascidin 743 (ET-743) with hydrogens 03
Ecteinascidin 743 (ET-743, brand name Yondelis), was discovered and isolated from a sea squirt, Ecteinascidia turbinata, by NIGMS grantee Kenneth Rinehart at the University of Illinois. It was synthesized by NIGMS grantees E.J. Corey and later by Samuel Danishefsky. Multiple versions of this structure are available as entries 2790-2797.
Timothy Jamison, Massachusetts Institute of Technology
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3333: Polarized cells- 02
3333: Polarized cells- 02
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). In the absence of functional Arp2/3 complex, ARPC3-/- fibroblast cells' leading edge morphology is significantly altered with filopodia-like structures. Related to images 3328, 3329, 3330, 3331, and 3332.
Rong Li and Praveen Suraneni, Stowers Institute for Medical Research
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6612: Ciclo circadiano de un adolescente típico
6612: Ciclo circadiano de un adolescente típico
Los ritmos circadianos son cambios físicos, mentales y conductuales que siguen un ciclo de 24 horas. Los ritmos circadianos típicos conducen a un nivel alto de energía durante la mitad del día (de 10 a.m. a 1 p.m.) y un bajón por la tarde. De noche, los ritmos circadianos hacen que la hormona melatonina aumente, lo que hace que la persona se sienta somnolienta.
Vea 6611 para la versión en inglés de esta infografía.
Vea 6611 para la versión en inglés de esta infografía.
NIGMS
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2739: Tetrapolar mitosis
2739: Tetrapolar mitosis
This image shows an abnormal, tetrapolar mitosis. Chromosomes are highlighted pink. The cells shown are S3 tissue cultured cells from Xenopus laevis, African clawed frog.
Gary Gorbsky, Oklahoma Medical Research Foundation
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1335: Telomerase illustration
1335: Telomerase illustration
Reactivating telomerase in our cells does not appear to be a good way to extend the human lifespan. Cancer cells reactivate telomerase.
Judith Stoffer
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3387: NCMIR human spinal nerve
3387: NCMIR human spinal nerve
Spinal nerves are part of the peripheral nervous system. They run within the spinal column to carry nerve signals to and from all parts of the body. The spinal nerves enable all the movements we do, from turning our heads to wiggling our toes, control the movements of our internal organs, such as the colon and the bladder, as well as allow us to feel touch and the location of our limbs.
Tom Deerinck, National Center for Microscopy and Imaging Research (NCMIR)
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2722: Cryogenic storage tanks at the Coriell Institute for Medical Research
2722: Cryogenic storage tanks at the Coriell Institute for Medical Research
Established in 1953, the Coriell Institute for Medical Research distributes cell lines and DNA samples to researchers around the world. Shown here are Coriell's cryogenic tanks filled with liquid nitrogen and millions of vials of frozen cells.
Courtney Sill, Coriell Institute for Medical Research
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7000: Plastic-eating enzymes
7000: Plastic-eating enzymes
PETase enzyme degrades polyester plastic (polyethylene terephthalate, or PET) into monohydroxyethyl terephthalate (MHET). Then, MHETase enzyme degrades MHET into its constituents ethylene glycol (EG) and terephthalic acid (TPA).
Find these in the RCSB Protein Data Bank: PET hydrolase (PDB entry 5XH3) and MHETase (PDB entry 6QGA).
Find these in the RCSB Protein Data Bank: PET hydrolase (PDB entry 5XH3) and MHETase (PDB entry 6QGA).
Amy Wu and Christine Zardecki, RCSB Protein Data Bank.
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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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5883: Beta-galactosidase montage showing cryo-EM improvement--gradient background
5883: Beta-galactosidase montage showing cryo-EM improvement--gradient background
Composite image of beta-galactosidase showing how cryo-EM’s resolution has improved dramatically in recent years. Older images to the left, more recent to the right. Related to image 5882. NIH Director Francis Collins featured this on his blog on January 14, 2016.
Veronica Falconieri, Sriram Subramaniam Lab, National Cancer Institute
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3281: Mouse heart fibroblasts
3281: Mouse heart fibroblasts
This image shows mouse fetal heart fibroblast cells. The muscle protein actin is stained red, and the cell nuclei are stained blue. The image was part of a study investigating stem cell-based approaches to repairing tissue damage after a heart attack. Image and caption information courtesy of the California Institute for Regenerative Medicine.
Kara McCloskey lab, University of California, Merced, via CIRM
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6553: Floral pattern in a mixture of two bacterial species, Acinetobacter baylyi and Escherichia coli, grown on a semi-solid agar for 48 hours (photo 1)
6553: Floral pattern in a mixture of two bacterial species, Acinetobacter baylyi and Escherichia coli, grown on a semi-solid agar for 48 hours (photo 1)
Floral pattern emerging as two bacterial species, motile Acinetobacter baylyi (red) and non-motile Escherichia coli (green), are grown together for 48 hours on 1% agar surface from a small inoculum in the center of a Petri dish.
See 6557 for a photo of this process at 24 hours on 0.75% agar surface.
See 6555 for another photo of this process at 48 hours on 1% agar surface.
See 6556 for a photo of this process at 72 hours on 0.5% agar surface.
See 6550 for a video of this process.
See 6557 for a photo of this process at 24 hours on 0.75% agar surface.
See 6555 for another photo of this process at 48 hours on 1% agar surface.
See 6556 for a photo of this process at 72 hours on 0.5% agar surface.
See 6550 for a video of this process.
L. Xiong et al, eLife 2020;9: e48885
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3753: Coronavirus spike protein structure
3753: Coronavirus spike protein structure
Coronaviruses are enveloped viruses responsible for 30 percent of mild respiratory infections and atypical deadly pneumonia in humans worldwide. These deadly pneumonia include those caused by infections with severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV). The coronavirus spike glycoprotein mediates virus entry into cells and represents an important therapeutic target. The illustration shows a viral membrane decorated with spike glycoproteins; highlighted in red is a potential neutralization site, which is a protein sequence that might be used as a target for vaccines to combat viruses such as MERS-CoV and other coronaviruses.
Melody Campbell, UCSF
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3630: Three muscle fibers; the middle has a defect found in some neuromuscular diseases
3630: Three muscle fibers; the middle has a defect found in some neuromuscular diseases
Of the three muscle fibers shown here, the one on the right and the one on the left are normal. The middle fiber is deficient a large protein called nebulin (blue). Nebulin plays a number of roles in the structure and function of muscles, and its absence is associated with certain neuromuscular disorders.
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.
Christopher Pappas and Carol Gregorio, University of Arizona
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3422: Atomic Structure of Poppy Enzyme
3422: Atomic Structure of Poppy Enzyme
The atomic structure of the morphine biosynthetic enzyme salutaridine reductase bound to the cofactor NADPH. The substrate salutaridine is shown entering the active site.
Judy Coyle, Donald Danforth Plant Science Center
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3743: Developing Arabidopsis flower buds
3743: Developing Arabidopsis flower buds
Flower development is a carefully orchestrated, genetically programmed process that ensures that the male (stamen) and female (pistil) organs form in the right place and at the right time in the flower. In this image of young Arabidopsis flower buds, the gene SUPERMAN (red) is activated at the boundary between the cells destined to form the male and female parts. SUPERMAN activity prevents the central cells, which will ultimately become the female pistil, from activating the gene APETALA3 (green), which induces formation of male flower organs. The goal of this research is to find out how plants maintain cells (called stem cells) that have the potential to develop into any type of cell and how genetic and environmental factors cause stem cells to develop and specialize into different cell types. This work informs future studies in agriculture, medicine and other fields.
Nathanaël Prunet, Caltech
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1312: Cell toxins
1312: Cell toxins
A number of environmental factors cause DNA mutations that can lead to cancer: toxins in cigarette smoke, sunlight and other radiation, and some viruses.
Judith Stoffer
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6582: Group of fluorescent C. elegans showing muscle and ribosomal protein
6582: Group of fluorescent C. elegans showing muscle and ribosomal protein
Three C. elegans, tiny roundworms, with a ribosomal protein glowing red and muscle fibers glowing green. Researchers used these worms to study a molecular pathway that affects aging. The ribosomal protein is involved in protein translation and may play a role in dietary restriction-induced longevity. Image created using confocal microscopy.
View single roundworm here 6581.
View closeup of roundworms here 6583.
View single roundworm here 6581.
View closeup of roundworms here 6583.
Jarod Rollins, Mount Desert Island Biological Laboratory.
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6996: Measles virus proteins
6996: Measles virus proteins
A cross section of the measles virus in which six proteins (enlarged on the outside of the virus) work together to infect cells. The measles virus is extremely infectious; 9 out of 10 people exposed will contract the disease. Fortunately, an effective vaccine protects against infection. Portions of the proteins that have not been determined are shown with dots.
Learn more about the six proteins on PDB 101’s Molecule of the Month: Measles Virus Proteins. Structures are available for the ordered regions of nucleoprotein and phosphoprotein (PDB entries 5E4V, 3ZDO, 1T6O), but the remaining regions are thought to form a flexible, random tangle. For a larger look at the measles virus, see 6995.
Learn more about the six proteins on PDB 101’s Molecule of the Month: Measles Virus Proteins. Structures are available for the ordered regions of nucleoprotein and phosphoprotein (PDB entries 5E4V, 3ZDO, 1T6O), but the remaining regions are thought to form a flexible, random tangle. For a larger look at the measles virus, see 6995.
Amy Wu and Christine Zardecki, RCSB Protein Data Bank.
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6781: Video of Calling Cards in a mouse brain
6781: Video of Calling Cards in a mouse brain
The green spots in this mouse brain are cells labeled with Calling Cards, a technology that records molecular events in brain cells as they mature. Understanding these processes during healthy development can guide further research into what goes wrong in cases of neuropsychiatric disorders. Also fluorescently labeled in this video are neurons (red) and nuclei (blue). Calling Cards and its application are described in the Cell paper “Self-Reporting Transposons Enable Simultaneous Readout of Gene Expression and Transcription Factor Binding in Single Cells” by Moudgil et al.; and the Proceedings of the National Academy of Sciences paper “A viral toolkit for recording transcription factor–DNA interactions in live mouse tissues” by Cammack et al. This video was created for the NIH Director’s Blog post The Amazing Brain: Tracking Molecular Events with Calling Cards.
Related to image 6780.
Related to image 6780.
NIH Director's Blog
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2578: Cellular aging
2578: Cellular aging
A protein called tubulin (green) accumulates in the center of a nucleus (outlined in pink) from an aging cell. Normally, this protein is kept out of the nucleus with the help of gatekeepers known as nuclear pore complexes. But NIGMS-funded researchers found that wear and tear to long-lived components of the complexes eventually lowers the gatekeepers' guard. As a result, cytoplasmic proteins like tubulin gain entry to the nucleus while proteins normally confined to the nucleus seep out. The work suggests that finding ways to stop the leakage could slow the cellular aging process and possibly lead to new therapies for age-related diseases.
Maximiliano D'Angelo and Martin Hetzer, Salk Institute
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