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Sjors Scheres
Sjors Hendrik Willem Scheres FRS (born 1975) is a Dutch scientist at the MRC Laboratory of Molecular Biology Cambridge, UK. Education Scheres studied Chemistry at Utrecht University in The Netherlands, and spent nine months at the European Synchrotron Radiation Facility in France for his undergraduate research thesis. He then came back to Utrecht University for his DPhil in Protein Crystallography, which was supervised by Piet Gros. Career Scheres worked as a Postdoctoral researcher at the Spanish National Center for Biotechnology (CNB) with José Maria Carazo from 2003-2010, where he developed classification algorithms for Cryogenic electron microscopy (cryo-EM) images based on Maximum likelihood estimation. In 2010 Scheres was appointed as a group leader at the MRC Laboratory of Molecular Biology, Cambridge. There, he extended his maximum-likelihood methods to a general Empirical Bayes method for Protein structure determination by cryo-EM, which he implemented in the compu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MRC Laboratory Of Molecular Biology
The Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) is a research institute in Cambridge, England, involved in the revolution in molecular biology which occurred in the 1950–60s. Since then it has remained a major medical research laboratory at the forefront of scientific discovery, dedicated to improving the understanding of key biological processes at atomic, molecular and cellular levels using multidisciplinary methods, with a focus on using this knowledge to address key issues in human health. A new replacement building constructed close by to the original site on the Cambridge Biomedical Campus was opened by Her Majesty the Queen in May 2013. The road outside the new building is named Francis Crick Avenue after the 1962 joint Nobel Prize winner and LMB alumnus, who co-discovered the helical structure of DNA in 1953. History Origins: 1947-61 Max Perutz, following undergraduate training in organic chemistry, left Austria in 1936 and came to the Univers ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amyloid Fibrils
Amyloids are aggregates of proteins characterised by a fibrillar morphology of 7–13 nm in diameter, a beta sheet (β-sheet) secondary structure (known as cross-β) and ability to be stained by particular dyes, such as Congo red. In the human body, amyloids have been linked to the development of various diseases. Pathogenic amyloids form when previously healthy proteins lose their normal structure and physiological functions ( misfolding) and form fibrous deposits in amyloid plaques around cells which can disrupt the healthy function of tissues and organs. Such amyloids have been associated with (but not necessarily as the cause of) more than 50 human diseases, known as amyloidosis, and may play a role in some neurodegenerative diseases. Some of these diseases are mainly sporadic and only a few cases are familial. Others are only familial. Some are iatrogenic as they result from medical treatment. Prions are an infectious form of amyloids that can act as a template to conver ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nature's 10
''Nature'' 10 is an annual listicle of ten "people who mattered" in science, produced by the scientific journal ''Nature''. Nominees have made a significant impact in science either for good or for bad. Reporters and editorial staff at ''Nature'' judge nominees to have had "a significant impact on the world, or their position in the world may have had an important impact on science". Short biographical profiles describe the people behind some of the year's most important discoveries and events. Alongside the ten, five "ones to watch" for the following year are also listed. 2022 2022 awardees included: # Jane Rigby: Sky hunter # Yunlong Cao: COVID predictor # Saleemul Huq: Climate revolutionary # Svitlana Krakovska: Voice for Ukraine # Dimie Ogoina: Monkeypox watchman # Lisa McCorkell: Long-COVID advocate # Diana Greene Foster: Abortion fact-finder # António Guterres: Crisis diplomat # Muhammad Mohiuddin: Transplant trailblazer # Alondra Nelson: Policy principal Ones to ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EMBO Member
Membership of the European Molecular Biology Organization (EMBO) is an award granted by the European Molecular Biology Organization (EMBO) in recognition of "research excellence and the outstanding achievements made by a life scientist". , 88 EMBO Members and Associate Members have been awarded Nobel Prizes in either Physiology or Medicine, Chemistry or Physics. See :Members of the European Molecular Biology Organization for examples of EMBO members. Nomination and election of new members Elections for membership are held annually with candidates for membership being nominated and elected exclusively by existing EMBO members, membership cannot be applied for directly. Three types of membership exist: # EMBO Member, for scientists living (or who have lived) in a European Molecular Biology Conference (EMBC) Member State # EMBO Associate Member, for scientists living outside of the EMBC Member States # EMBO Young Investigator See also * List of biology awards This list of bi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bijvoet Center For Biomolecular Research
The Bijvoet Centre for Biomolecular Research is a research institute at Utrecht University. The Bijvoet Centre performs research on the relation between the structure and function of biomolecules, including proteins and lipids, which play a role in biological processes such as regulation, interaction and recognition. The Bijvoet Centre houses advanced infrastructures for the analysis of proteins and other biomolecules using NMR, X-ray crystallography, electron microscopy and mass spectrometry. The institute is named after famous Dutch chemist Johannes Martin Bijvoet, who worked at Utrecht University. History Utrecht University and the Netherlands Foundation for Chemical Research (SON, which later became the Chemical Sciences division of NWO, the Netherlands Organisation for Scientific Research) founded the Bijvoet Centre for Biomolecular Research as a joint research institute on March 25, 1988. The goal was to create a centre for research and expertise in structural biology with ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Royal Society
The Royal Society, formally The Royal Society of London for Improving Natural Knowledge, is a learned society and the United Kingdom's national academy of sciences. The society fulfils a number of roles: promoting science and its benefits, recognising excellence in science, supporting outstanding science, providing scientific advice for policy, education and public engagement and fostering international and global co-operation. Founded on 28 November 1660, it was granted a royal charter by King Charles II as The Royal Society and is the oldest continuously existing scientific academy in the world. The society is governed by its Council, which is chaired by the Society's President, according to a set of statutes and standing orders. The members of Council and the President are elected from and by its Fellows, the basic members of the society, who are themselves elected by existing Fellows. , there are about 1,700 fellows, allowed to use the postnominal title FRS ( Fellow of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Leeuwenhoek Lecture
The Leeuwenhoek Lecture is a prize lecture of the Royal Society to recognize achievement in microbiology. The prize was originally given in 1950 and awarded annually, but from 2006 to 2018 was given triennially. From 2018 it will be awarded biennially. The prize is named after the Dutch microscopist Antonie van Leeuwenhoek and was instituted in 1948 from a bequest from George Gabb. A gift of £2000 is associated with the lecture. Leeuwenhoek Lecturers The following is a list of Leeuwenhoek Lecture award winners along with the title of their lecture: 21st Century * 2022 Sjors Scheres, ''for ground-breaking contributions and innovations in image analysis and reconstruction methods in electron cryo-microscopy, enabling the structure determination of complex macromolecules of fundamental biological and medical importance to atomic resolution'' * 2020 Geoffrey L. Smith, ''for his studies of poxviruses which has had major impact in wider areas, notably vaccine development, biotechnol ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ELife
''eLife'' is a not-for-profit, peer-reviewed, open access, scientific journal for the biomedical and life sciences. It was established at the end of 2012 by the Howard Hughes Medical Institute, Max Planck Society, and Wellcome Trust, following a workshop held in 2010 at the Janelia Farm Research Campus. Together, these organizations provided the initial funding to support the business and publishing operations. In 2016, the organizations committed US$26 million to continue publication of the journal. The current editor-in-chief is Michael Eisen ( University of California, Berkeley). Editorial decisions are made largely by senior editors and members of the board of reviewing editors, all of whom are active scientists working in fields ranging from human genetics and neuroscience to biophysics, epidemiology, and ecology. Business model ''eLife'' is a non-profit organisation, but for long-term sustainability of the service, the journal asks for an article processing charg ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TMEM106B
Transmembrane protein 106B is a protein that is encoded by the ''TMEM106B'' gene. It is found primarily within neurons and oligodendrocytes in the central nervous system with its subcellular location being in lysosomal membranes. TMEM106B helps facilitate important functions for maintaining a healthy lysosome, and therefore certain mutations and polymorphisms can lead to issues with proper lysosomal function. Lysosomes are in charge of clearing out mis-folded proteins and other debris, and thus, play an important role in neurodegenerative diseases that are driven by the accumulation of various mis-folded proteins and aggregates. Due to its impact on lysosomal function, TMEM106B has been investigated and found to be associated to multiple neurodegenerative diseases. Structure Gene In humans,''TMEM106B'' is found on chromosome 7 at positions 12211270 - 12243367, totaling 32097 base pairs. The gene includes 9 exons and can give rise to 2 different isoforms, T185 and S185, whi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Multiple System Atrophy
Multiple system atrophy (MSA) is a rare neurodegenerative disorder characterized by autonomic dysfunction, tremors, slow movement, muscle rigidity, and postural instability (collectively known as parkinsonism) and ataxia. This is caused by progressive degeneration of neurons in several parts of the brain including the basal ganglia, inferior olivary nucleus, and cerebellum. Many people affected by MSA experience dysfunction of the autonomic nervous system, which commonly manifests as orthostatic hypotension, impotence, loss of sweating, dry mouth and urinary retention and incontinence. Palsy of the vocal cords is an important and sometimes initial clinical manifestation of the disorder. A modified form of the alpha-synuclein protein within affected neurons may cause MSA. About 55% of MSA cases occur in men, with those affected first showing symptoms at the age of 50–60 years. MSA often presents with some of the same symptoms as Parkinson's disease. However, those with ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha-synuclein
Alpha-synuclein is a protein that, in humans, is encoded by the ''SNCA'' gene. Alpha-synuclein is a neuronal protein that regulates synaptic vesicle trafficking and subsequent neurotransmitter release. It is abundant in the brain, while smaller amounts are found in the heart, muscle and other tissues. In the brain, alpha-synuclein is found mainly in the axon terminals of presynaptic neurons. Within these terminals, alpha-synuclein interacts with phospholipids and proteins. Presynaptic terminals release chemical messengers, called neurotransmitters, from compartments known as synaptic vesicles. The release of neurotransmitters relays signals between neurons and is critical for normal brain function. The human alpha-synuclein protein is made of 140 amino acids. An alpha-synuclein fragment, known as the non- Abeta component (NAC) of Alzheimer's disease amyloid, originally found in an amyloid-enriched fraction, was shown to be a fragment of its precursor protein, NACP. It was late ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amyloid Beta
Amyloid beta (Aβ or Abeta) denotes peptides of 36–43 amino acids that are the main component of the amyloid plaques found in the brains of people with Alzheimer's disease. The peptides derive from the amyloid precursor protein (APP), which is cleaved by beta secretase and gamma secretase to yield Aβ in a cholesterol-dependent process and substrate presentation. Aβ molecules can aggregate to form flexible soluble oligomers which may exist in several forms. It is now believed that certain misfolded oligomers (known as "seeds") can induce other Aβ molecules to also take the misfolded oligomeric form, leading to a chain reaction akin to a prion infection. The oligomers are toxic to nerve cells. The other protein implicated in Alzheimer's disease, tau protein, also forms such prion-like misfolded oligomers, and there is some evidence that misfolded Aβ can induce tau to misfold. A study has suggested that APP and its amyloid potential is of ancient origins, dating as far ba ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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