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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.
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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3620: Anglerfish ovary cross-section
3620: Anglerfish ovary cross-section
This image captures the spiral-shaped ovary of an anglerfish in cross-section. Once matured, these eggs will be released in a gelatinous, floating mass. For some species of anglerfish, this egg mass can be up to 3 feet long and include nearly 200,000 eggs.
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.
James E. Hayden, The Wistar Institute, Philadelphia, Pa.
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6353: ATP Synthase
6353: ATP Synthase
Atomic model of the membrane region of the mitochondrial ATP synthase built into a cryo-EM map at 3.6 Å resolution. ATP synthase is the primary producer of ATP in aerobic cells. Drugs that inhibit the bacterial ATP synthase, but not the human mitochondrial enzyme, can serve as antibiotics. This therapeutic approach was successfully demonstrated with the bedaquiline, an ATP synthase inhibitor now used in the treatment of extensively drug resistant tuberculosis.
More information about this structure can be found in the Science paper ”Atomic model for the dimeric F0 region of mitochondrial ATP synthase” by Guo et. al.
More information about this structure can be found in the Science paper ”Atomic model for the dimeric F0 region of mitochondrial ATP synthase” by Guo et. al.
Bridget Carragher, <a href="http://nramm.nysbc.org/">NRAMM National Resource for Automated Molecular Microscopy</a>
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5888: Independence Day
5888: Independence Day
This graphic that resembles a firework was created from a picture of a fruit fly spermatid. 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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3328: Spreading Cells 01
3328: Spreading 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), Arp2 (green), and DAPI to visualize the nucleus (blue). Arp2, a subunit of the Arp2/3 complex, is localized at the lamellipodia leading edge of ARPC3+/+ fibroblast cells. Related to images 3329, 3330, 3331, 3332, and 3333.
Rong Li and Praveen Suraneni, Stowers Institute for Medical Research
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6355: H1N1 Influenza Virus
6355: H1N1 Influenza Virus
CellPack image of the H1N1 influenza virus, with hemagglutinin and neuraminidase glycoproteins in green and red, respectively, on the outer envelope (white); matrix protein in gray, and ribonucleoprotein particles inside the virus in red and green. Related to image 6356.
Dr. Rommie Amaro, University of California, San Diego
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1047: Sea urchin embryo 01
1047: Sea urchin embryo 01
Stereo triplet of a sea urchin embryo stained to reveal actin filaments (orange) and microtubules (blue). This image is part of a series of images: image 1048, image 1049, image 1050, image 1051 and image 1052.
George von Dassow, University of Washington
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2428: Colorful cells
2428: Colorful cells
Actin (purple), microtubules (yellow), and nuclei (green) are labeled in these cells by immunofluorescence. This image won first place in the Nikon 2003 Small World photo competition.
Torsten Wittmann, Scripps Research Institute
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6549: The Structure of Cilia’s Doublet Microtubules
6549: The Structure of Cilia’s Doublet Microtubules
Cilia (cilium in singular) are complex molecular machines found on many of our cells. One component of cilia is the doublet microtubule, a major part of cilia’s skeletons that give them support and shape. This animated video illustrates the structure of doublet microtubules, which contain 451 protein chains that were mapped using cryo-electron microscopy. Image can be found here 6548.
Brown Lab, Harvard Medical School and Veronica Falconieri Hays
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2541: Nucleotides make up DNA
2541: Nucleotides make up DNA
DNA consists of two long, twisted chains made up of nucleotides. Each nucleotide contains one base, one phosphate molecule, and the sugar molecule deoxyribose. The bases in DNA nucleotides are adenine, thymine, cytosine, and guanine. See image 2542 for a labeled version of this illustration. Featured in The New Genetics.
Crabtree + Company
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3750: A dynamic model of the DNA helicase protein complex
3750: A dynamic model of the DNA helicase protein complex
This short video shows a model of the DNA helicase in yeast. This DNA helicase has 11 proteins that work together to unwind DNA during the process of copying it, called DNA replication. Scientists used a technique called cryo-electron microscopy (cryo-EM), which allowed them to study the helicase structure in solution rather than in static crystals. Cryo-EM in combination with computer modeling therefore allows researchers to see movements and other dynamic changes in the protein. The cryo-EM approach revealed the helicase structure at much greater resolution than could be obtained before. The researchers think that a repeated motion within the protein as shown in the video helps it move along the DNA strand. To read more about DNA helicase and this proposed mechanism, see this news release by Brookhaven National Laboratory.
Huilin Li, Stony Brook University
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3611: Tiny strands of tubulin, a protein in a cell's skeleton
3611: Tiny strands of tubulin, a protein in a cell's skeleton
Just as our bodies rely on bones for structural support, our cells rely on a cellular skeleton. In addition to helping cells keep their shape, this cytoskeleton transports material within cells and coordinates cell division. One component of the cytoskeleton is a protein called tubulin, shown here as thin strands.
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.
Pakorn Kanchanawong, National University of Singapore and National Heart, Lung, and Blood Institute, National Institutes of Health; and Clare Waterman, National Heart, Lung, and Blood Institute, National Institutes of Health
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2312: Color-coded chromosomes
2312: Color-coded chromosomes
By mixing fluorescent dyes like an artist mixes paints, scientists are able to color code individual chromosomes. The technique, abbreviated multicolor-FISH, allows researchers to visualize genetic abnormalities often linked to disease. In this image, "painted" chromosomes from a person with a hereditary disease called Werner Syndrome show where a piece of one chromosome has fused to another (see the gold-tipped maroon chromosome in the center). As reported by molecular biologist Jan Karlseder of the Salk Institute for Biological Studies, such damage is typical among people with this rare syndrome.
Anna Jauch, Institute of Human Genetics, Heidelberg, Germany
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6992: Molecular view of glutamatergic synapse
6992: Molecular view of glutamatergic synapse
This illustration highlights spherical pre-synaptic vesicles that carry the neurotransmitter glutamate. The presynaptic and postsynaptic membranes are shown with proteins relevant for transmitting and modulating the neuronal signal.
PDB 101’s Opioids and Pain Signaling video explains how glutamatergic synapses are involved in the process of pain signaling.
PDB 101’s Opioids and Pain Signaling video explains how glutamatergic synapses are involved in the process of pain signaling.
Amy Wu and Christine Zardecki, RCSB Protein Data Bank.
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3295: Cluster analysis of mysterious protein
3295: Cluster analysis of mysterious protein
Researchers use cluster analysis to study protein shape and function. Each green circle represents one potential shape of the protein mitoNEET. The longer the blue line between two circles, the greater the differences between the shapes. Most shapes are similar; they fall into three clusters that are represented by the three images of the protein. From a Rice University news release. Graduate student Elizabeth Baxter and Patricia Jennings, professor of chemistry and biochemistry at UCSD, collaborated with José Onuchic, a physicist at Rice University, on this work.
Patricia Jennings and Elizabeth Baxter, University of California, San Diego
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3284: Neurons from human ES cells
3284: Neurons from human ES cells
These neural precursor cells were derived from human embryonic stem cells. The neural cell bodies are stained red, and the nuclei are blue. Image and caption information courtesy of the California Institute for Regenerative Medicine.
Xianmin Zeng lab, Buck Institute for Age Research, via CIRM
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2509: From DNA to Protein
2509: From DNA to Protein
Nucleotides in DNA are copied into RNA, where they are read three at a time to encode the amino acids in a protein. Many parts of a protein fold as the amino acids are strung together.
See image 2510 for a labeled version of this illustration.
Featured in The Structures of Life.
See image 2510 for a labeled version of this illustration.
Featured in The Structures of Life.
Crabtree + Company
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5751: Genetically identical mycobacteria respond differently to antibiotic 1
5751: Genetically identical mycobacteria respond differently to antibiotic 1
Antibiotic resistance in microbes is a serious health concern. So researchers have turned their attention to how bacteria undo the action of some antibiotics. Here, scientists set out to find the conditions that help individual bacterial cells survive in the presence of the antibiotic rifampicin. The research team used Mycobacterium smegmatis, a more harmless relative of Mycobacterium tuberculosis, which infects the lung and other organs and causes serious disease.
In this image, genetically identical mycobacteria are growing in a miniature growth chamber called a microfluidic chamber. Using live imaging, the researchers found that individual mycobacteria will respond differently to the antibiotic, depending on the growth stage and other timing factors. The researchers used genetic tagging with green fluorescent protein to distinguish cells that can resist rifampicin and those that cannot. With this gene tag, cells tolerant of the antibiotic light up in green and those that are susceptible in violet, enabling the team to monitor the cells' responses in real time.
To learn more about how the researchers studied antibiotic resistance in mycobacteria, see this news release from Tufts University. Related to video 5752.
In this image, genetically identical mycobacteria are growing in a miniature growth chamber called a microfluidic chamber. Using live imaging, the researchers found that individual mycobacteria will respond differently to the antibiotic, depending on the growth stage and other timing factors. The researchers used genetic tagging with green fluorescent protein to distinguish cells that can resist rifampicin and those that cannot. With this gene tag, cells tolerant of the antibiotic light up in green and those that are susceptible in violet, enabling the team to monitor the cells' responses in real time.
To learn more about how the researchers studied antibiotic resistance in mycobacteria, see this news release from Tufts University. Related to video 5752.
Bree Aldridge, Tufts University
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2512: X-ray crystallography (with labels)
2512: X-ray crystallography (with labels)
X-ray crystallography allows researchers to see structures too small to be seen by even the most powerful microscopes. To visualize the arrangement of atoms within molecules, researchers can use the diffraction patterns obtained by passing X-ray beams through crystals of the molecule. This is a common way for solving the structures of proteins. See image 2511 for an unlabeled version of this illustration. Featured in The Structures of Life.
Crabtree + Company
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2549: Central dogma, illustrated (with labels and numbers for stages)
2549: Central dogma, illustrated (with labels and numbers for stages)
DNA encodes RNA, which encodes protein. DNA is transcribed to make messenger RNA (mRNA). The mRNA sequence (dark red strand) is complementary to the DNA sequence (blue strand). On ribosomes, transfer RNA (tRNA) reads three nucleotides at a time in mRNA to bring together the amino acids that link up to make a protein. See image 2548 for a version of this illustration that isn't numbered and 2547 for a an entirely unlabeled version. Featured in The New Genetics.
Crabtree + Company
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6767: Space-filling model of a cefotaxime-CCD-1 complex
6767: Space-filling model of a cefotaxime-CCD-1 complex
CCD-1 is an enzyme produced by the bacterium Clostridioides difficile that helps it resist antibiotics. Using X-ray crystallography, researchers determined the structure of a complex between CCD-1 and the antibiotic cefotaxime (purple, yellow, and blue molecule). The structure revealed that CCD-1 provides extensive hydrogen bonding (shown as dotted lines) and stabilization of the antibiotic in the active site, leading to efficient degradation of the antibiotic.
Related to images 6764, 6765, and 6766.
Related to images 6764, 6765, and 6766.
Keith Hodgson, Stanford University.
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2564: Recombinant DNA
2564: Recombinant DNA
To splice a human gene into a plasmid, scientists take the plasmid out of an E. coli bacterium, cut the plasmid with a restriction enzyme, and splice in human DNA. The resulting hybrid plasmid can be inserted into another E. coli bacterium, where it multiplies along with the bacterium. There, it can produce large quantities of human protein. See image 2565 for a labeled version of this illustration. Featured in The New Genetics.
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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6579: Full-length serotonin receptor (ion channel)
6579: Full-length serotonin receptor (ion channel)
A 3D reconstruction, created using cryo-electron microscopy, of an ion channel known as the full-length serotonin receptor in complex with the antinausea drug granisetron (orange). Ion channels are proteins in cell membranes that help regulate many processes.
Sudha Chakrapani, Case Western Reserve University School of Medicine.
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2515: Life of an AIDS virus (with labels and stages)
2515: Life of an AIDS virus (with labels and stages)
HIV is a retrovirus, a type of virus that carries its genetic material not as DNA but as RNA. Long before anyone had heard of HIV, researchers in labs all over the world studied retroviruses, tracing out their life cycle and identifying the key proteins the viruses use to infect cells. When HIV was identified as a retrovirus, these studies gave AIDS researchers an immediate jump-start. The previously identified viral proteins became initial drug targets. See images 2513 and 2514 for other versions of this illustration. Featured in The Structures of Life.
Crabtree + Company
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3425: Red Poppy
6604: Enzyme reaction
6604: Enzyme reaction
Enzymes speed up chemical reactions by reducing the amount of energy needed for the reactions. The substrate (lactose) binds to the active site of the enzyme (lactase) and is converted into products (sugars).
NIGMS
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3558: Bioluminescent imaging in adult zebrafish - lateral view
3558: Bioluminescent imaging in adult zebrafish - lateral view
Luciferase-based imaging enables visualization and quantification of internal organs and transplanted cells in live adult zebrafish. In this image, a cardiac muscle-restricted promoter drives firefly luciferase expression (lateral view).
For imagery of both the lateral and overhead view go to 3556.
For imagery of the overhead view go to 3557.
For more information about the illumated area go to 3559.
For imagery of both the lateral and overhead view go to 3556.
For imagery of the overhead view go to 3557.
For more information about the illumated area go to 3559.
Kenneth Poss, Duke University
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2365: Map of protein structures 01
2365: Map of protein structures 01
A global "map of the protein structure universe." The Berkeley Structural Genomics Center has developed a method to visualize the vast universe of protein structures in which proteins of similar structure are located close together and those of different structures far away in the space. This map, constructed using about 500 of the most common protein folds, reveals a highly non-uniform distribution, and shows segregation between four elongated regions corresponding to four different protein classes (shown in four different colors). Such a representation reveals a high-level of organization of the protein structure universe.
Berkeley Structural Genomics Center, PSI
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3274: Human embryonic stem cells on feeder cells
3274: Human embryonic stem cells on feeder cells
This fluorescent microscope image shows human embryonic stem cells whose nuclei are stained green. Blue staining shows the surrounding supportive feeder cells. Image and caption information courtesy of the California Institute for Regenerative Medicine. See related image 3275.
Michael Longaker lab, Stanford University School of Medicine, via CIRM
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3746: Serum albumin structure 3
3746: Serum albumin structure 3
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 3745.
Related to entries 3744 and 3745.
Wladek Minor, University of Virginia
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3632: Developing nerve cells
3632: Developing nerve cells
These developing mouse nerve cells have a nucleus (yellow) surrounded by a cell body, with long extensions called axons and thin branching structures called dendrites. Electrical signals travel from the axon of one cell to the dendrites of another.
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.
Torsten Wittmann, University of California, San Francisco
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2596: Sleep and the fly brain
2596: Sleep and the fly brain
In the top snapshots, the brain of a sleep-deprived fruit fly glows orange, marking high concentrations of a synaptic protein called Bruchpilot (BRP) involved in communication between neurons. The color particularly lights up brain areas associated with learning. By contrast, the bottom images from a well-rested fly show lower levels of the protein. These pictures illustrate the results of an April 2009 study showing that sleep reduces the protein's levels, suggesting that such "downscaling" resets the brain to normal levels of synaptic activity and makes it ready to learn after a restful night.
Chiara Cirelli, University of Wisconsin-Madison
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2489: Immune cell attacks cell infected with a retrovirus
2489: Immune cell attacks cell infected with a retrovirus
T cells engulf and digest cells displaying markers (or antigens) for retroviruses, such as HIV.
Kristy Whitehouse, science illustrator
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6811: Fruit fly egg chamber
6811: Fruit fly egg chamber
A fruit fly (Drosophila melanogaster) egg chamber with microtubules shown in green and actin filaments shown in red. Egg chambers are multicellular structures in fruit flies ovaries that each give rise to a single egg. Microtubules and actin filaments give the chambers structure and shape. This image was captured using a confocal microscope.
More information on the research that produced this image can be found in the Current Biology paper "Gatekeeper function for Short stop at the ring canals of the Drosophila ovary" by Lu et al.
More information on the research that produced this image can be found in the Current Biology paper "Gatekeeper function for Short stop at the ring canals of the Drosophila ovary" by Lu et al.
Vladimir I. Gelfand, Feinberg School of Medicine, Northwestern University.
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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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6750: C. elegans with blue and yellow lights in the background
6750: C. elegans with blue and yellow lights in the background
These microscopic roundworms, called Caenorhabditis elegans, lack eyes and the opsin proteins used by visual systems to detect colors. However, researchers found that the worms can still sense the color of light in a way that enables them to avoid pigmented toxins made by bacteria. This image was captured using a stereo microscope.
H. Robert Horvitz and Dipon Ghosh, Massachusetts Institute of Technology.
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3489: Worm sperm
3489: Worm sperm
To develop a system for studying cell motility in unnatrual conditions -- a microscope slide instead of the body -- Tom Roberts and Katsuya Shimabukuro at Florida State University disassembled and reconstituted the motility parts used by worm sperm cells.
Tom Roberts, Florida State University
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1166: Leptospira bacteria
1166: Leptospira bacteria
Leptospira, shown here in green, is a type (genus) of elongated, spiral-shaped bacteria. Infection can cause Weil's disease, a kind of jaundice, in humans.
Tina Weatherby Carvalho, University of Hawaii at Manoa
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3574: Cytonemes in developing fruit fly cells
3574: Cytonemes in developing fruit fly cells
Scientists have long known that multicellular organisms use biological molecules produced by one cell and sensed by another to transmit messages that, for instance, guide proper development of organs and tissues. But it's been a puzzle as to how molecules dumped out into the fluid-filled spaces between cells can precisely home in on their targets. Using living tissue from fruit flies, a team led by Thomas Kornberg of the University of California, San Francisco, has shown that typical cells in animals can talk to each other via long, thin cell extensions called cytonemes (Latin for "cell threads") that may span the length of 50 or 100 cells. The point of contact between a cytoneme and its target cell acts as a communications bridge between the two cells.
Sougata Roy, University of California, San Francisco
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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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6756: Honeybees marked with paint
6756: Honeybees marked with paint
Researchers doing behavioral experiments with honeybees sometimes use paint or enamel to give individual bees distinguishing marks. The elaborate social structure and impressive learning and navigation abilities of bees make them good models for behavioral and neurobiological research. Since the sequencing of the honeybee genome, published in 2006, bees have been used increasingly for research into the molecular basis for social interaction and other complex behaviors.
Gene Robinson, University of Illinois at Urbana-Champaign.
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2426: Zinc finger
2426: Zinc finger
The structure of a gene-regulating zinc finger protein bound to DNA.
Jeremy M. Berg, National Institute of General Medical Sciences
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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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2532: Drugs enter skin (with labels)
2532: Drugs enter skin (with labels)
Drugs enter different layers of skin via intramuscular, subcutaneous, or transdermal delivery methods. See image 2531 for an unlabeled version of this illustration. Featured in Medicines By Design.
Crabtree + Company
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3432: Mouse mammary cells lacking anti-cancer protein
3432: Mouse mammary cells lacking anti-cancer protein
Shortly after a pregnant woman gives birth, her breasts start to secrete milk. This process is triggered by hormonal and genetic cues, including the protein Elf5. Scientists discovered that Elf5 also has another job--it staves off cancer. Early in the development of breast cancer, human breast cells often lose Elf5 proteins. Cells without Elf5 change shape and spread readily--properties associated with metastasis. This image shows cells in the mouse mammary gland that are lacking Elf5, leading to the overproduction of other proteins (red) that increase the likelihood of metastasis.
Nature Cell Biology, November 2012, Volume 14 No 11 pp1113-1231
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2714: Stretch detectors
2714: Stretch detectors
Muscles stretch and contract when we walk, and skin splits open and knits back together when we get a paper cut. To study these contractile forces, researchers built a three-dimensional scaffold that mimics tissue in an organism. Researchers poured a mixture of cells and elastic collagen over microscopic posts in a dish. Then they studied how the cells pulled and released the posts as they formed a web of tissue. To measure forces between posts, the researchers developed a computer model. Their findings--which show that contractile forces vary throughout the tissue--could have a wide range of medical applications.
Christopher Chen, University of Pennsylvania
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1011: Lily mitosis 11
1011: Lily mitosis 11
A light microscope image of cells from the endosperm 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. Staining shows microtubules in red and chromosomes in blue. Here, condensed chromosomes are clearly visible and have separated into the opposite sides of a dividing cell.
Related to images 1010, 1012, 1013, 1014, 1015, 1016, 1017, 1018, 1019, and 1021.
Related to images 1010, 1012, 1013, 1014, 1015, 1016, 1017, 1018, 1019, and 1021.
Andrew S. Bajer, University of Oregon, Eugene
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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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3723: Fluorescent microscopy of kidney tissue
3723: Fluorescent microscopy of kidney tissue
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 3725 and 3675.
Related to entries 3725 and 3675.
Tom Deerinck , National Center for Microscopy and Imaging Research
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