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Workforce Developement
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Enhancing Diversity in Training Programs
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Laboratory Safety and Guidelines
Training Resources
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Division for Research Capacity Building
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Native American Research Centers for Health (NARCH)
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Related Information
DRCB News
DRCB Staff Contacts
Resources
NIH RePORTER
Grants and Funding
Funding Opportunities
Current NIGMS Funding Opportunities
Parent Announcements for Investigator-Initiated Applications
Research Funding
Research Project Grants (NIH Parent R01)
Research With Activities Related to Diversity (ReWARD)
Maximizing Investigators' Research Awards (MIRA)
Instrumentation Grant Program for Resource-Limited Institutions (RLI-S10)
Undergraduate-Focused Institutions
Small Business Research
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Research Resources
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All Funding Opportunities
Grant Application and Post-Award Information
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Post-Award Information
Talking to NIH Staff About Your Application and Grant
Considerations for Multiple Principal Investigator (MPI) Applications
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Attribution of NIH/NIGMS Support
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NIH RePORTER
Research Using Human Subjects or Specimens
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2500
3239
Glucose (top) and sucrose (bottom) are sugars made of carbon, hydrogen, and oxygen atoms. Carbohydrates include simple sugars like these and are the main source of energy for the human body. Featured in <a href=http://www.nigms.nih.gov/Publications/Findings.htm target="_blank"><i>Findings</i></a>, October 2004.
9/18/2020 5:38:14 PM
9/18/2020 5:38:14 PM
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A representation of a patient’s brain waves after receiving the anesthetic propofol. All anesthetics create brain wave changes that vary depending on the patient’s age and the type and dose of anesthetic used. These changes are visible in raw electroencephalogram (EEG) readings, but they’re easier to interpret using a spectrogram where the signals are broken down by time (x-axis), frequency (y-axis), and power (color scale). This spectrogram shows the changes in brain waves before, during, and after propofol-induced anesthesia. The patient is unconscious from minute 5, upon propofol administration, through minute 69 (change in power and frequency). But, between minutes 35 and 48, the patient fell into a profound state of unconsciousness (disappearance of dark red oscillations between 8 to 12 Hz), which required the anesthesiologist to adjust the rate of propofol administration. The propofol was stopped at minute 62 and the patient woke up around minute 69.
8/24/2021 4:39:56 PM
8/24/2021 4:39:56 PM
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This image is a computer-generated model of the approximately 4.2 million atoms of the HIV capsid, the shell that contains the virus' genetic material. Scientists determined the exact structure of the capsid and the proteins that it's made of using a variety of imaging techniques and analyses. They then entered these data into a supercomputer that produced the atomic-level image of the capsid. This structural information could be used for developing drugs that target the capsid, possibly leading to more effective therapies
11/14/2023 1:23:33 PM
11/14/2023 1:23:33 PM
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This structural information could be used for developing
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Ionic and covalent bonds hold molecules, like sodium chloride and chlorine gas, together. Hydrogen bonds among molecules, notably involving water, also play an important role in biology. Featured in <a href=http://publications.nigms.nih.gov/chemhealth/ target="_blank"><i>The Chemistry of Health</i></a>.
3/4/2022 8:07:52 PM
3/4/2022 8:07:52 PM
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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 (Top) and overhead views (Bottom) are shown.
10/5/2020 5:20:22 AM
10/5/2020 5:20:22 AM
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br>For imagery of the overhead
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Acetylsalicylate (bottom) is the aspirin of today. Adding a chemical tag called an acetyl group (shaded yellow 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 <a href=http://publications.nigms.nih.gov/medbydesign/ target="_blank"><i>Medicines By Design</i></a>.
11/4/2021 6:30:06 PM
11/4/2021 6:30:06 PM
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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 <a href=http://publications.nigms.nih.gov/medbydesign/ target="_blank"><i>Medicines By Design</i></a>.
10/9/2020 4:27:14 PM
10/9/2020 4:27:14 PM
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A model of the molecule himastatin, which was first isolated from the bacterium <em>Streptomyces himastatinicus</em>. Himastatin shows antibiotic activity. The researchers who created this image developed a new, more concise way to synthesize himastatin so it can be studied more easily. <Br><Br> More information about the research that produced this image can be found in the <em>Science</em> paper <a href="https://www.science.org/doi/10.1126/science.abm6509">“Total synthesis of himastatin”</a> by D’Angelo et al. <Br><Br> Related to image <a href="https://images.nigms.nih.gov/pages/DetailPage.aspx?imageid2=6850">6850</a> and video <a href="https://images.nigms.nih.gov/pages/DetailPage.aspx?imageid2=6851">6851</a>.
3/7/2022 9:09:53 PM
3/7/2022 9:09:53 PM
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A 360-degree view of the molecule himastatin, which was first isolated from the bacterium <em>Streptomyces himastatinicus</em>. 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. <Br><Br> More information about the research that produced this video can be found in the <em>Science</em> paper <a href="https://www.science.org/doi/10.1126/science.abm6509">“Total synthesis of himastatin”</a> by D’Angelo et al. <Br><Br> Related to images <a href="https://images.nigms.nih.gov/pages/DetailPage.aspx?imageid2=6848">6848</a> and <a href="https://images.nigms.nih.gov/pages/DetailPage.aspx?imageid2=6850">6850</a>.
3/7/2022 9:12:07 PM
3/7/2022 9:12:07 PM
Type Name Media Type File Size Modified
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Opioid receptors on the surfaces of brain cells are involved in pleasure, pain, addiction, depression, psychosis, and other conditions. The receptors bind to both innate opioids and drugs ranging from hospital anesthetics to opium. Researchers at The Scripps Research Institute, supported by the NIGMS Protein Structure Initiative, determined the first three-dimensional structure of a human opioid receptor, a kappa-opioid receptor. In this illustration, the submicroscopic receptor structure is shown while bound to an agonist (or activator). The structure is superimposed on a poppy flower, the source of opium. From a Scripps Research Institute <a href=http://www.scripps.edu/news/press/20120321stevens.html target="_blank">news release</a>.
12/23/2020 4:46:54 PM
12/23/2020 4:46:54 PM
Type Name Media Type File Size Modified
opioid_ill_v10_L Low 122 KB 6/3/2016 3:26 PM aamishral2 (NIH/NIGMS) [C
Opioid receptors on the surfaces of
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X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Found in the journal, Nature, Chemical Biology 8, 366-374 (2012). Series of seven images. Related to <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3414">image 3414</a> , <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3415">image 3415</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3416">image 3416</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3417">image 3417</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3418">image 3418</a> and <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3419">image 3419</a>.
12/23/2020 11:02:46 PM
12/23/2020 11:02:46 PM
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WE are happy to give you
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X-ray co-crystal structure of Src kinase bound to a DNA-templated macrocycle inhibitor. Found in the journal, Nature, Chemical Biology 8, 366-374 (2012). <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3413">image 3413</a> , <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3414">image 3414</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3415">image 3415</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3416">image 3416</a>, <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3417">image 3417</a> and <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3419">image 3419</a>.
12/23/2020 11:12:00 PM
12/23/2020 11:12:00 PM
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Bacterial biofilms are tightly knit communities of bacterial cells growing on, for example, solid surfaces, such as in water pipes or on teeth. Here, cells of the bacterium Bacillus subtilis have formed a biofilm in a laboratory culture. Researchers have discovered that the bacterial cells in a biofilm communicate with each other through electrical signals via specialized potassium ion channels to share resources, such as nutrients, with each other. This insight may help scientists to improve sanitation systems to prevent biofilms, which often resist common treatments, from forming and to develop better medicines to combat bacterial infections. See the Biomedical Beat blog post <a href="http://biobeat.nigms.nih.gov/2015/12/bacterial-biofilms-a-charged-environment /">Bacterial Biofilms: A Charged Environment</a> for more information.
2/4/2020 6:02:20 PM
2/4/2020 6:02:20 PM
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The plasma membrane is a cell's protective barrier Featured in <a href=http://publications.nigms.nih.gov/chemhealth/ target="_blank"><i>The Chemistry of Health</i></a>.
3/4/2022 8:02:56 PM
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Signal obtained by allowing proteins in human serum to interact with glycan (polysaccharide) arrays. The arrays are shown in replicate so the pattern is clear. Each spot contains a specific type of glycan. Proteins have bound to the spots highlighted in green.
10/28/2020 4:09:56 PM
10/28/2020 4:09:56 PM
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A model of the molecule himastatin overlaid on an image of <em>Bacillus subtilis bacteria</em>. Scientists first isolated himastatin from the bacterium <em>Streptomyces himastatinicus</em>, and the molecule shows antibiotic activity. The researchers who created this image developed a new, more concise way to synthesize himastatin so it can be studied more easily. They also tested the effects of himastatin and derivatives of the molecule on <em>B. subtilis</em>. <Br><Br> More information about the research that produced this image can be found in the <em>Science</em> paper <a href="https://www.science.org/doi/10.1126/science.abm6509">“Total synthesis of himastatin”</a> by D’Angelo et al. <Br><Br> Related to image <a href="https://images.nigms.nih.gov/pages/DetailPage.aspx?imageid2=6848">6848</a> and video <a href="https://images.nigms.nih.gov/pages/DetailPage.aspx?imageid2=6851">6851</a>.
3/7/2022 9:11:07 PM
3/7/2022 9:11:07 PM
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A red poppy.
8/12/2020 6:27:27 AM
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Ionic and covalent bonds hold molecules, like sodium chloride and chlorine gas, together. Hydrogen bonds among molecules, notably involving water, also play an important role in biology. Featured in <a href=http://publications.nigms.nih.gov/chemhealth/ target="_blank"><i>The Chemistry of Health</i></a>.
3/4/2022 8:07:29 PM
3/4/2022 8:07:29 PM
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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 <i>Biochemistry</i>. This image was not used in the publication.
8/31/2020 4:08:32 AM
8/31/2020 4:08:32 AM
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that was published in 2007 in <i>
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</i>. This image was not used in the
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This wreath represents the molecular structure of a protein, Cas4, which is part of a system, known as CRISPR, that bacteria use to protect themselves against viral invaders. The green ribbons show the protein's structure, and the red balls show the location of iron and sulfur molecules important for the protein's function. Scientists harnessed Cas9, a different protein in the bacterial CRISPR system, to create a gene-editing tool known as CRISPR-Cas9. Using this tool, researchers are able to study a range of cellular processes and human diseases more easily, cheaply and precisely. In December, 2015, Science magazine recognized the CRISPR-Cas9 gene-editing tool as the "breakthrough of the year." Read more about Cas4 in the December 2015 Biomedical Beat post <a href="https://biobeat.nigms.nih.gov/2015/12/cool-images-a-holiday-themed-collection/">A Holiday-Themed Image Collection</a>.
12/3/2020 8:52:01 PM
12/3/2020 8:52:01 PM
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Shiga toxin (green) is sorted from the endosome into membrane tubules (red), which then pinch off and move to the Golgi apparatus.
9/8/2020 11:05:30 PM
9/8/2020 11:05:30 PM
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T cells are white blood cells that are important in defending the body against bacteria, viruses and other pathogens. Each T cell carries proteins, called T-cell receptors, on its surface that are activated when they come in contact with an invader. This activation sets in motion a cascade of biochemical changes inside the T cell to mount a defense against the invasion. Scientists have been interested for some time what happens after a T-cell receptor is activated. One obstacle has been to study how this signaling cascade, or pathway, proceeds inside T cells. <Br><Br>In this video, researchers have created a T-cell receptor pathway consisting of 12 proteins outside the cell on an artificial membrane. The video shows three key steps during the signaling process: phosphorylation of the T-cell receptor (green), clustering of a protein called linker for activation of T cells (LAT) (blue) and polymerization of the cytoskeleton protein actin (red). The findings show that the T-cell receptor signaling proteins self-organize into separate physical and biochemical compartments. This new system of studying molecular pathways outside the cells will enable scientists to better understand how the immune system combats microbes or other agents that cause infection. <Br><Br>To learn more how researchers assembled this T-cell receptor pathway, see <a href="http://www.mbl.edu/blog/building-immunity-mbl-whitman-center-scientists-recreate-a-t-cell-receptor-signaling-pathway/">this press release from HHMI's Marine Biological Laboratory Whitman Center.</a> Related to <a href="https://imagesadminprod.nigms.nih.gov/Pages/DetailPage.aspx?imageID=718">video 3786</a>.
12/17/2020 7:19:29 PM
12/17/2020 7:19:29 PM
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T cells are white blood cells
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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. <Br><Br>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. <Br><Br> To learn more about how the researchers studied antibiotic resistance in Mycobacterium, see <a href="http://now.tufts.edu/news-releases/individual-mycobacteria-respond-differently-antibiotics-based-growth-and-timing">this news release from Tufts University</a>. Related to <a href="https://imagesadminprod.nigms.nih.gov/Pages/DetailPage.aspx?imageID=2990">video 5752</a>.
12/18/2020 4:27:18 PM
12/18/2020 4:27:18 PM
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Colonies of bacteria growing despite high concentrations of antibiotics. These colonies are visible both by eye, as seen on the left, and by bioluminescence imaging, as seen on the right. The bioluminescent color indicates the metabolic activity of these bacteria, with their red centers indicating high metabolism. <Br><Br> More information about the research that produced this image can be found in the <em> Antimicrobial Agents and Chemotherapy</em> paper <a href="https://journals.asm.org/doi/full/10.1128/AAC.00623-20">“Novel aminoglycoside-tolerant phoenix colony variants of <em>Pseudomonas aeruginosa</em>”</a> by Sindeldecker et al.
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This illustration of an epoxide-opening cascade promoted by water emulates the proposed biosynthesis of some of the Red Tide toxins.
9/18/2020 5:17:23 PM
9/18/2020 5:17:23 PM
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The nucleolus is a small but very important protein complex located in the cell's nucleus. It forms on the chromosomes at the location where the genes for the RNAs are that make up the structure of the ribosome, the indispensable cellular machine that make proteins from messenger RNAs. <Br><Br>However, how the nucleolus grows and maintains its structure has puzzled scientists for some time. It turns out that even though it looks like a simple liquid blob, it's rather well-organized, consisting of three distinct layers: the fibrillar center, where the RNA polymerase is active; the dense fibrillar component, which is enriched in the protein fibrillarin; and the granular component, which contains a protein called nucleophosmin. Researchers have now discovered that this multilayer structure of the nucleolus arises from differences in how the proteins in each compartment mix with water and with each other. These differences let the proteins readily separate from each other into the three nucleolus compartments. <Br><Br>This video of nucleoli in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows how each of the compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue) spontaneously fuse with each other on encounter without mixing with the other compartments. <Br><Br>For more details on this research, see <a href="http://www.princeton.edu/main/news/archive/S46/35/80M01/?section=topstories">this press release from Princeton</a>. Related to <a href="https://imagesadminprod.nigms.nih.gov/Pages/DetailPage.aspx?imageID=721"> video 3789</a>, <a href="https://imagesadminprod.nigms.nih.gov/Pages/DetailPage.aspx?imageID=723"> image 3792</a> and <a href="https://imagesadminprod.nigms.nih.gov/Pages/DetailPage.aspx?imageID=724"> image 3793</a>.
12/17/2020 7:33:57 PM
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The nucleolus is a small but very important protein complex located in the cell's nucleus. It forms on the chromosomes at the location where the genes for the RNAs are that make up the structure of the ribosome, the indispensable cellular machine that make proteins from messenger RNAs.<Br><Br> However, how the nucleolus grows and maintains its structure has puzzled scientists for some time. It turns out that even though it looks like a simple liquid blob, it's rather well-organized, consisting of three distinct layers: the fibrillar center, where the RNA polymerase is active; the dense fibrillar component, which is enriched in the protein fibrillarin; and the granular component, which contains a protein called nucleophosmin. Researchers have now discovered that this multilayer structure of the nucleolus arises from difference in how the proteins in each compartment mix with water and with each other. These differences let them readily separate from each other into the three nucleolus compartments. <Br><Br>This video of nucleoli in the eggs of a commonly used lab animal, the frog Xenopus laevis, shows how each of the compartments (the granular component is shown in red, the fibrillarin in yellow-green, and the fibrillar center in blue) spontaneously fuse with each other on encounter without mixing with the other compartments. For more details on this research, see <a href="http://www.princeton.edu/main/news/archive/S46/35/80M01/?section=topstories">this press release from Princeton.</a> Related to <a href="https://imagesadminprod.nigms.nih.gov/Pages/DetailPage.aspx?imageID=721"> video 3791</a>, <a href="https://imagesadminprod.nigms.nih.gov/Pages/DetailPage.aspx?imageID=722"> image 3792</a> and <a href="https://imagesadminprod.nigms.nih.gov/Pages/DetailPage.aspx?imageID=723"> image 3793</a>.
12/17/2020 7:25:03 PM
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A 3-D model of the alkaloid serratezomine A shows the molecule's complex ring structure.
11/6/2020 9:17:27 PM
11/6/2020 9:17:27 PM
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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 to cause serious disease.<Br><Br> In this video, 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. <Br><Br> To learn more about how the researchers studied antibiotic resistance in Mycobacterium, see <a href="http://now.tufts.edu/news-releases/individual-mycobacteria-respond-differently-antibiotics-based-growth-and-timing">this news release from Tufts University</a>. Related to <a href="https://imagesadminprod.nigms.nih.gov/Pages/DetailPage.aspx?imageID=2986">image 5751</a>.
12/18/2020 4:30:09 PM
12/18/2020 4:30:09 PM
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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. Featured in the June 16, 2010, issue of <a href=http://publications.nigms.nih.gov/biobeat/10-06-16/index.html#3 target="_blank"><em>Biomedical Beat</em></a>.
8/21/2020 5:49:28 PM
8/21/2020 5:49:28 PM
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Chemistry,
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Antibody,
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, Biochemical, Drug Delivery, Immune System
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A white poppy.
8/12/2020 6:24:02 AM
8/12/2020 6:24:02 AM
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A white poppy.
8/12/2020 6:26:03 AM
8/12/2020 6:26:03 AM
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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 (overhead view).
10/5/2020 5:19:11 AM
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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).
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Luciferase-based imaging enables visualization and quantification of internal organs and transplanted cells in live adult zebrafish. This image shows how luciferase-based imaging could be used to visualize the heart for regeneration studies (left), or label all tissues for stem cell transplantation (right).
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<i>Bacillus anthracis</i> (anthrax) cells being killed by a fluorescent trans-translation inhibitor, which disrupts bacterial protein synthesis. The inhibitor is naturally fluorescent and looks blue when it is excited by ultraviolet light in the microscope. This is a black-and-white version of <a href="http://images.nigms.nih.gov/index.cfm?event=viewDetail&imageID=3525">Image 3525</a>.
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Keiler Associate Professor of
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Sulfite oxidase is an enzyme that is essential for normal neurological development in children. This video shows the active site of the enzyme and its molybdenum cofactor visible as a faint ball-and-stick representation buried within the protein. The positively charged channel (blue) at the active site contains a chloride ion (green) and three water molecules (red). As the protein oscillates, one can see directly down the positively charged channel. At the bottom is the molybdenum atom of the active site (light blue) and its oxo group (red) that is transferred to sulfite to form sulfate in the catalytic reaction.
8/18/2020 7:39:49 PM
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Acetylsalicylate (bottom) is the aspirin of today. Adding a chemical tag called an acetyl group (shaded yellow 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 2529 for an unlabled version of this illustration. Featured in <a href=http://publications.nigms.nih.gov/medbydesign/ target="_blank"><i>Medicines By Design</i></a>.
11/4/2021 6:29:28 PM
11/4/2021 6:29:28 PM
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To become products, reactants must overcome an energy hill. Featured in <a href=http://publications.nigms.nih.gov/chemhealth/ target="_blank"><i>The Chemistry of Health</i></a>.
3/4/2022 7:59:11 PM
3/4/2022 7:59:11 PM
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CCD-1 is an enzyme produced by the bacterium <em>Clostridioides difficile</em> 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. <Br><Br> Related to images <a href="/Pages/DetailPage.aspx?imageID2=6764">6764</a>, <a href="/Pages/DetailPage.aspx?imageID2=6765">6765</a>, and <a href="/Pages/DetailPage.aspx?imageID2=6766">6766</a>.
5/16/2022 3:26:06 PM
5/16/2022 3:26:06 PM
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A drug's life in the body. Medicines taken by mouth pass through the liver before they are absorbed into the bloodstream. Other forms of drug administration bypass the liver, entering the blood directly. See <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=2528">image 2528</a> for a labeled version of this illustration. Featured in <a href=http://publications.nigms.nih.gov/medbydesign/ target="_blank"><i>Medicines By Design</i></a>.
11/4/2021 7:07:50 PM
11/4/2021 7:07:50 PM
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Chemistry,
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Pharmacology
pharmacokinetics, PK, Pharmacodynamics, PD,
Pharmacology
, Drug Delivery
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A drug's life in the body. Medicines taken by mouth (oral) pass through the liver before they are absorbed into the bloodstream. Other forms of drug administration bypass the liver, entering the blood directly. See <a href="https://imagesadminprod.nigms.nih.gov/index.cfm?event=viewDetail&imageID=2527">image 2527</a> for an unlabeled version of this illustration. . Featured in <a href=http://publications.nigms.nih.gov/medbydesign/ target="_blank"><i>Medicines By Design</i></a>.
11/4/2021 7:07:29 PM
11/4/2021 7:07:29 PM
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12/23/2020 8:54:32 PM
12/23/2020 8:54:32 PM
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The world's smallest motor, ATP synthase, generates energy for the cell. Featured in <a href=http://publications.nigms.nih.gov/chemhealth/ target="_blank"><i>The Chemistry of Health</i></a>.
3/4/2022 8:13:22 PM
3/4/2022 8:13:22 PM
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The world's smallest motor, ATP synthase, generates energy for the cell. Featured in <a href=http://publications.nigms.nih.gov/chemhealth/ target="_blank"><i>The Chemistry of Health</i></a>.
3/4/2022 8:12:48 PM
3/4/2022 8:12:48 PM
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Chemistry,
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A protein called kinesin (blue) is in charge of moving cargo around inside cells and helping them divide. It's powered by biological fuel called ATP (bright yellow) as it scoots along tube-like cellular tracks called microtubules (gray).
9/8/2020 11:21:32 PM
9/8/2020 11:21:32 PM
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Would you allow us to do so, and would you please let us know how you would like
Dept. of Molecular Biophysics and
Biochemistry
Yale University SHMC-E25 333 Cedar
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T cells are white blood cells that are important in defending the body against bacteria, viruses and other pathogens. Each T cell carries proteins, called T-cell receptors, on its surface that are activated when they come in contact with an invader. This activation sets in motion a cascade of biochemical changes inside the T cell to mount a defense against the invasion. Scientists have been interested for some time what happens after a T-cell receptor is activated. One obstacle has been to study how this signaling cascade, or pathway, proceeds inside T cells. <Br><Br>In this video, researchers have created a T-cell receptor pathway consisting of 12 proteins outside the cell on an artificial membrane. The video shows three key steps during the signaling process: phosphorylation of the T-cell receptor (green), clustering of a protein called linker for activation of T cells (LAT) (blue) and polymerization of the cytoskeleton protein actin (red). The findings show that the T-cell receptor signaling proteins self-organize into separate physical and biochemical compartments. This new system of studying molecular pathways outside the cells will enable scientists to better understand how the immune system combats microbes or other agents that cause infection. <Br><Br>To learn more how researchers assembled this T-cell receptor pathway, see <a href="http://www.mbl.edu/blog/building-immunity-mbl-whitman-center-scientists-recreate-a-t-cell-receptor-signaling-pathway/">this press release from HHMI's Marine Biological Laboratory Whitman Center.</a> Related to <a href="https://imagesadminprod.nigms.nih.gov/Pages/DetailPage.aspx?imageID=719">image 3787</a>.
12/17/2020 7:14:36 PM
12/17/2020 7:14:36 PM
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The arrangement of identical molecular components can make a dramatic difference. For example, carbon atoms can be arranged into dull graphite (left) or sparkly diamonds (right). Featured in <a href=http://www.nigms.nih.gov/Publications/Findings.htm target="_blank"><i>Findings</i></a>, March 2006.
3/4/2022 8:17:53 PM
3/4/2022 8:17:53 PM
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National Institute of General Medical Sciences
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This network map shows the overlap (green) between the long QT syndrome (yellow) and epilepsy (blue) protein-interaction neighborhoods located within the human interactome. Researchers have learned to integrate genetic, cellular and clinical information to find out why certain medicines can trigger fatal heart arrhythmias. Featured in an <a href=http://publications.nigms.nih.gov/computinglife/genetic_framework.htm target="_blank">article in <em>Computing Life</em></a> magazine.
8/12/2020 6:20:49 PM
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This network map shows the overlap
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Ecteinascidin 743 (ET-743, brand name Yondelis), was discovered and isolated from a sea squirt, <i>Ecteinascidia turbinata</i>, by NIGMS grantee Kenneth Rinehart at the University of Illinois. It was synthesized by NIGMS grantees E.J. Corey and later by Samuel Danishefsky. It is being tested for the treatment of several types of cancer. Multiple versions of this structure are available as entries 2790-2797.
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2/22/2021 9:16:48 PM
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