- published: 11 Oct 2013
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Khan Academy is a non-profit educational organization created in 2006 by educator Salman Khan with the aim of providing a free, world-class education for anyone, anywhere. The organization produces short lectures in the form of YouTube videos. In addition to micro lectures, the organization's website features practice exercises and tools for educators. All resources are available for free to anyone around the world. The main language of the website is English, but the content is also available in other languages.
The founder of the organization, Salman Khan, was born in New Orleans, Louisiana, United States to immigrant parents from Bangladesh and India. After earning three degrees from the Massachusetts Institute of Technology (a BS in mathematics, a BS in electrical engineering and computer science, and an MEng in electrical engineering and computer science), he pursued an MBA from Harvard Business School.
In late 2004, Khan began tutoring his cousin Nadia who needed help with math using Yahoo!'s Doodle notepad.When other relatives and friends sought similar help, he decided that it would be more practical to distribute the tutorials on YouTube. The videos' popularity and the testimonials of appreciative students prompted Khan to quit his job in finance as a hedge fund analyst at Connective Capital Management in 2009, and focus on the tutorials (then released under the moniker "Khan Academy") full-time.
The transient receptor potential cation channel subfamily V member 1 (TrpV1), also known as the capsaicin receptor and the vanilloid receptor 1, is a protein that, in humans, is encoded by the TRPV1 gene. It was the first isolated member of the transient receptor potential vanilloid receptor proteins that in turn are a sub-family of the transient receptor potential protein group. This protein is a member of the TRPV group of transient receptor potential family of ion channels.
The function of TRPV1 is detection and regulation of body temperature. In addition, TRPV1 provides a sensation of scalding heat and pain (nociception).
TRPV1 is a nonselective cation channel that may be activated by a wide variety of exogenous and endogenous physical and chemical stimuli. The best-known activators of TRPV1 are: temperature greater than 43 °C (109 °F); acidic conditions; capsaicin, the irritating compound in hot chili peppers; and allyl isothiocyanate, the pungent compound in mustard and wasabi. The activation of TRPV1 leads to a painful, burning sensation. Its endogenous activators include: low pH (acidic conditions), the endocannabinoid anandamide, N-oleyl-dopamine, and N-arachidonoyl-dopamine. TRPV1 receptors are found mainly in the nociceptive neurons of the peripheral nervous system, but they have also been described in many other tissues, including the central nervous system. TRPV1 is involved in the transmission and modulation of pain (nociception), as well as the integration of diverse painful stimuli.
Explore our senses of pain & temperature. By Ron. Created by Ronald Sahyouni. Watch the next lesson: https://www.khanacademy.org/test-prep/nclex-rn/rn-integumentary-system-physiology/rn-integumentary-system/v/thermoregulation-by-muscles?utm_source=YT&utm;_medium=Desc&utm;_campaign=Nclex-rn Missed the previous lesson? https://www.khanacademy.org/test-prep/nclex-rn/rn-integumentary-system-physiology/rn-integumentary-system/v/ruffinis-ending-and-hair-follicle-receptor-2?utm_source=YT&utm;_medium=Desc&utm;_campaign=Nclex-rn NCLEX-RN on Khan Academy: A collection of questions from content covered on the NCLEX-RN. These questions are available under a Creative Commons Attribution-NonCommercial-ShareAlike 3.0 United States License (available at http://creativecommons.org/licenses/by-nc-sa/3.0/us...
UC Davis researchers have identified the molecular interactions that allow capsaicin to activate the body’s primary receptor for sensing heat and pain, paving the way for the design of more selective and effective drugs to relieve pain. “While we have known that capsaicin binds to the TRPV1 receptor with exquisite potency and selectivity, we were missing important atomic-level details about exactly how the capsaicin molecule interacts with TRPV1, one of the body’s primary receptors for sensing pain and heat,” said Jie Zheng, professor of physiology and membrane biology at UC Davis and an author on the paper. Using computer models based on atomic force fields and existing low resolution 3-D reconstruction of TRPV1-capsaicin complex from cryo-electron microscopy (cryo-EM) studies, the rese...
Heidelberg University: At the Institute of Pharmacology, CellNetworks member Prof. Jan Siemens and his research group explore sensory mechanisms at the molecular level. In their paper, published in Cell in 2015, they discovered a molecular mechanism in nerve cells which reverts the sensitized state of the capsaicin receptor TRPV1. With the activiation of GABAB1, the receptor forms a complex with TRPV1 to counteract inflammatory pain. Harnessing this mechanism for anti-pain therapy may prevent adverse effects associated with currently availabe TRPV1 blockers. http://bit.ly/2bQ60W4
The capsaicin receptor transient receptor potential vanilloid (TRPV)1 is a highly heat-sensitive ion channel. Although chemical activation and heat activation of TRPV1 elicit similar pungent, painful sensation, the molecular mechanism underlying synergistic activation remains mysterious. In particular, where the temperature sensor is located and whether heat and capsaicin share a common activation pathway are debated. To address these fundamental issues, we searched for channel mutations that selectively affected one form of activation. We found that deletion of the first 10 amino acids of the pore turret significantly reduced the heat response amplitude and shifted the heat activation threshold, whereas capsaicin activation remained unchanged. Removing larger portions of the turret disrup...
http://www.ucsf.edu/news/2013/12/110571/structure-key-pain-related-protein-unveiled In a technical tour de force, UC San Francisco (UCSF) scientists have determined, at near-atomic resolution, the structure of a protein that plays a central role in the perception of pain and heat. Led by UCSF postdoctoral fellows Erhu Cao, PhD, and Maofu Liao, PhD, the new research will offer fresh insights to drug designers searching for new and better pain treatments, but it also is a watershed for the field of structural biology, which aims to discover how proteins are physically constructed in order to better understand their function.
Subscribe! http://bit.ly/ACSReactions You have probably had the burning sensation of eating a hot jalapeno or other tear-inducing pepper. What causes this painful fire in your mouth? The short answer is capsaicin. But what exactly is capsaicin? How does it work? Why do people drink milk and not water to relieve the pain? Reactions has the chemistry to answer all of these sizzling questions. Find us on all these places: Subscribe! http://bit.ly/ACSReactions Facebook! http://facebook.com/ACSReactions Twitter! http://twitter.com/ACSReactions Tumblr! http://tumblr.com/ACSReactions Old School - Funk It Up The Drive Producer: Elaine Seward Writer: Elaine Seward Executive Producer: Adam Dylewski Scientific consultants: Todd Brethauer Sophia Cai Darcy Gentleman, Ph.D. Sources: Milk - ht...