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The Humanicsxian: November 09: Issue 06
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What Does Not Die











In Hampshire in an autumn wood the squirrel I found that came to say hello
In New Hampshire life’s voices went rippling human joys and sorrows and
In Union Square I saw the sun painting the green leaves with photon-paints
Allwhere life is a song written and sung in many a form in many a rainbow
A rainbow it is always allwhere marking the same shape of life-expressions

It is always in units of atoms
Units of photons and of cells
DNAs RNAs and neurons
Always the same rises ee falls
Always it is the song of cells

And the Empire State Building raised a spectacle in Manhattan skyline as
The traffic lit the air in all its expressions in the evening and in Scotland I
Saw heather and hyacinth in Swansea the light and its spread the same
Light the same song written and sung in many a form in many a rainbow
And it is the same that drives us to strive to stretch to reach to risk to rise

It is always magnetic
Always electric and
Chemical and active
Biochemical it is as
It shapes the cell-rise

I saw grace in human faces in Prague in Granada in Dhaka in Rome or in
London Manchester or York and found moss on city brick walls and saw
Butterflies on squeezed in greens of tiny spaces in town gardens and saw
Waters mining for life poetry in silence music in the ferns climbing onto
The trellis of light heard seagulls’ cries as human babies in all-everyday

In everyday momentary miracles
I saw life’s rainbow biochemistry
Unfolding noughts in paperboats
It is always the same song of love
That never dies and forever lives

:Munayem Mayenin: November 07: 2015

|| A Targeted Small Molecule Alleviates Arthritis Symptoms in Mice: Many Opportunities Are Possible in Atomistic-Level Drug Development ||


|| Wednesday: August 30: 2023  || ά. A new molecular discovery helped ameliorate the symptoms of rheumatoid arthritis in mice. The use of small molecules makes drug development increasingly accurate. Their use is currently being investigated in the treatment of cancer. For the first time, researchers have described at the atomic level, how a small molecule, that blocks the cellular secretion of proteins involved in development of disease, binds to its target protein.

Researchers at the University of Helsinki, together with researchers from the United States, have discovered a small molecule, that inhibits the formation in cells of cytokine proteins, that promote inflammation. The mechanism is based on the fact that the small molecule blocks the secretion of cytokines entirely. By inhibiting a target protein, known as Sec61, the researchers successfully alleviated symptoms of rheumatoid arthritis in a mouse model. The finding may, also, have relevance to the treatment of certain cancers.

“For the first time, we were able to describe on the level of atoms how a small molecule, that blocks the cellular secretion of proteins relevant to the development of diseases, such as, cytokines, binds to its target protein. This way, we were able to establish a model for blocking the production of various secreted target proteins with the help of small molecules.” says Research Director Ville Paavilainen from the Institute of Biotechnology, University of Helsinki.

According to Paavilainen, the finding means that, in the future, such drug-like small molecules can be developed with increased accuracy to, specifically prevent, the formation of proteins, associated with various diseases. “The new atom-level knowledge we have produced on the target protein and the small molecule bound to it enables the rational design of novel molecules in drug development.” Paavilainen says.

The researchers used chemical biology to determine how the small molecule, that inhibits the function of the Sec61 protein functions in human cells and affects the functioning of the Sec61 protein channel. Using an animal model of rheumatoid arthritis, the researchers were able to demonstrate that the small molecule alleviated arthritis symptoms without adverse side effects.

The researchers, also, utilised Nobel Prize–winning cryo-electron microscopy to investigate how this small molecule binds to its large target protein. At the same time, the dynamics and interactions of this complex were investigated through atomistic computer simulations carried out on the supercomputers operated by the CSC–IT Centre for Science in Kajaani, central Finland.

Many proteins formed in cells are associated with the onset of diseases. For example, proteins, such as, cytokines, which function as mediators of inflammation, are known to underlie rheumatoid arthritis. Paavilainen’s research group investigates the mechanisms by which various proteins, that affect diseases are secreted in cells.

A range of small molecules have long been the subject of drug development. Most of the drugs currently available are aimed at influencing the secretion of proteins already generated, such as, cytokines. In the research carried out by Paavilainen’s group, the formation of proteins, that contribute to the onset of diseases is entirely blocked.

“Collecting more research knowledge on which proteins are associated with various diseases will enable the development of entirely new kinds of drugs. Of course, further research is needed. Our group will continue working on targeted small molecules.” Paavilainen says.

The Study was carried out in collaboration with Kezar Life Sciences, a United States pharmaceutical company. The company is currently investigating the effectiveness of blocking protein secretion in the treatment of certain solid and easily spreading malignant tumours. The Study was published in the journal Nature Chemical Biology in May.

Publication: Rehan, S., Tranter, D., Sharp, P.P. et al. Signal peptide mimicry primes Sec61 for client-selective inhibition. Nat Chem Biol
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Mutations in Plasma Cells Play a Key Role in Light Chain Amyloidosis Fatal Over-production of Antibodies




|| Tuesday: March 10: 2020 || ά. Bone marrow plasma cells produce antibodies. These comprise two long and two short protein chains. The pathological proliferation of plasma cells can lead to an over-production of the short chains. These associate to fibrils and deposit in organs. The result is fatal organ failure. A research team from the Technical University of Munich:TUM and Heidelberg University has now identified the mutation, behind the disease in a patient. Antibodies are vital for the survival of human beings. They, typically, consist of two longer and, thus, heavier amino acid chains and two lighter ones. In rare cases, the plasma cells multiply excessively, flooding the body with light antibody chains.

In people suffering from light chain amyloidosis or AL amyloidosis, these light chains are deposited as extremely fine fibres, so-called amyloid fibrils, in tissue or in organs. The disease is, often, recognised, only, after the deposits already compromise the function of organs. In many cases AL amyloidosis is fatal. "To date, little was known about the exact cause of this amyloidosis." says Professor Johannes Buchner, of bio-technology at the Technical University of Munich. “Depending on the organ affected, the symptoms vary considerably. Furthermore, each patient produces different types of antibodies. The disease is, thus, difficult to diagnose at an early stage.”

Using various analytical and database-supported methods, the team of scientists succeeded in identifying eleven mutations, caused by the disease in the antibodies of a patient with advanced AL amyloidosis. Further investigations showed that exactly one mutation was responsible for the destabilisation and formation of the disease-causing amyloid fibrils. This mutation causes the unstable light chain to lose its structure after breaking into fragments, which, then, form the deadly amyloid fibrils.

"Our Study shows that mutations, that lead to unstable light chains, are an important factor in the occurrence of amyloidosis." says Ms Pamina Kazman, who carried out the majority of the measurements. "In the long term, we hope that these and other studies will lead to new, earlier diagnostic methods and, possibly, even, new treatment options."

The Paper: Fatal amyloid formation in a patient’s antibody light chain is caused by a single point mutation: Pamina Kazman, Marie-Theres Vielberg, María Daniela Pulido Cendales, Lioba Hunziger, Benedikt Weber, Ute Hegenbart, Martin Zacharias, Rolf Köhler, Stefan Schönland, Michael Groll, Johannes Buchner: Published in eLife online

The research was funded by the German Research Foundation:DFG. The protein structures were determined at the synchrotron radiation sources of the Paul Scherrer Institute in Villigen in Switzerland and the European synchrotron radiation source in Grenoble in France.

::: Caption: 01: PhD student Ms Pamina Kazman examines the folding and stability of antibody domains with the circular dichroism spectrometer of the Chair of Bio-technology; 02: At the Lab: 03: Compared to the normal antibody fragment, left, that of the patient, right, has a significantly larger hydrophobic area, red. Due to its lower stability, this fragment can form the dangerous amyloid fibrils: Image: P Kazman:TUM :::: 10.03.2020

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New Collaboration in Drug Development Offers Hope for the Patients of Alzheimer's Disease



|| February 22: 2019: University of Dundee News || ά. The University of Dundee’s Drug Discovery Unit has announced a partnership with Takeda, Japan’s largest pharmaceutical company, to develop possible new therapeutic treatments for tau pathology, an underlying feature in several forms of neuro-degeneration, including, Alzheimer’s Disease. Tau pathology occurs when the normal cellular protein, tau, misfolds and forms insoluble fibrils. It is found in the brains of sufferers of more than 20 different neuro-degenerative diseases, of which Alzheimer’s Disease is the most common.

Tau pathology is, increasingly, thought to be an important driver of disease progression. Recent studies demonstrate that tau pathology can spread from diseased to healthy cells in a seeding process, which is the focus of this collaboration. Alzheimer’s Disease affects 50 million people worldwide, yet, there are currently no disease-modifying treatments. Numbers of sufferers are expected to increase dramatically in the coming decades, thus, representing a vast and growing unmet medical need. Working in collaboration with Dr Will McEwan at the University of Cambridge and Dr Leo James at the MRC Laboratory of Molecular Biology, the Drug Discovery Unit has identified drug-like molecules, that prevent seeded misfolding of tau.

The partnership with Takeda will accelerate the progression of these drug-like molecules towards clinical development, with the potential to become much-needed therapies in diseases where tau is implicated, including, Alzheimer’s Disease. Dr David Gray, the Head of Innovative Targets at the Drug Discovery Unit, said, “Our mission is to bridge the gap between innovative life science research and drug development in areas of unmet clinical need and Alzheimer’s Disease is at the top of the list.

With support from Medical Research Council we are able to work with leading investigators, such as, Dr Will McEwan in Cambridge and Dr Leo James at the MRC Laboratory of Molecular Biology to deliver programmes, that are ready for industry to take forward. Teaming up with Takeda means we’ll get further, faster, bringing a potential treatment for this debilitating condition one step closer.”

The University of Dundee Drug Discovery Unit  is a fully integrated drug discovery group, established in 2006 to translate world-class biology research into novel drug targets and candidate drugs.  Housed within purpose-built facilities the Unit has the full repertoire of professional, industry-standard expertise and infrastructure required for preclinical small molecule drug discovery and to bridge the gap between academic research and pharmaceutical development.:::ω.

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Neuro-endocrine Tumours: New Comparative Study Conducted to Help Doctors Choose Better Therapies for Their Patients



|| February 18: 2019: University of Geneva News || ά. Which treatment for which patient? Researchers from a cluster of universities formed of Geneva, Bern and Basel, the HUG and Inselpital Bern has performed systematic comparisons between the therapies available for neuro-endocrine tumours in order to offer patients the most appropriate ones. An increasing number of new anti-cancer drugs are made available each year. During the authorisation process, such new drugs, usually, undergo comparisons to one but, only, rarely, to multiple established drugs.

This practice leads to a lack of comparisons between therapies and makes it, increasingly, difficult for physicians to choose the best treatment for their patients. To address this, researchers of these universities have conducted an extensive comparison of all drugs, used in the treatment of neuro-endocrine tumours. Their Study, published in JAMA Oncology, aims of guiding physicians through all available treatment options. Neuro-endocrine tumours can develop anywhere in the body from hormone-producing cells. Their prevalence is increasing and new therapies are regularly beefing up therapeutic options.

“The growing number of new therapies constitutes a great opportunity, obviously. However, the fact that few comparative studies are carried out between these different drugs, creates a dilemma for doctors when it comes to finding the best option for each patient.” says Professor Martin A Walter, at the University of Geneva Faculty of Medicine and the Head of the Nuclear Medicine and Molecular Imaging Division at the HUG, who initiated and co-ordinated this Study.

“Indeed, it is, actually, sufficient to establish the superiority of a new molecule over a single established drug or, even, over a placebo, to obtain approval from the regulatory authorities and enter the market.’’

“In such a situation, a network meta-analysis can be a valuable tool to generate indirect comparisons for therapies, that have not yet been directly compared. They, also, make it possible to use all existing data to identify the most effective treatments.” says Dr Reto Kaderli, the Head of Endocrine Surgery, Department of Visceral Surgery and Medicine, Bern University Hospital and University of Bern. Dr Kaderli is the First Author of the Study.

Swiss researchers collaborated with Cochrane, a global organisation, that aims to facilitating clinical decision-making, through systematic reviews of health interventions and with researchers at McMaster University in Hamilton, Canada, where some of the key methodologies for the analysis of evidence-based medicine have been developed.

“One of the most striking results of our Study is the high and, often, underestimated, efficacy of combination therapies. And, equally, striking was that these combination therapies were under-represented in international guidelines.” says Dr Kaderli. Indeed, studies, combining drugs produced by different pharmaceutical companies are mainly conducted by independent researchers and their results are less taken into account in treatment guidelines than studies conducted by the pharmaceutical industry.

“As a specialist in Nuclear Medicine, however, I am delighted with the promising results of our radioactive therapeutics.” says Professor Walter. Such a step still needs to be taken for surgical options, for which randomised controlled trials in combination with other therapies are still lacking.

“Our work, thus, marks an important step in the search for the best therapeutic option for patients with neuro-endocrine tumours and highlights the need for independent evidence-based medicine.” researchers put forward.:::ω.

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New Research Gains New Insight Into the Workings of An Antibody in Coronavirus-Induced Severe Acute Respiratory Syndrome




|| February 06: 2019: University of Washington News || ά. Studies of human monoclonal antibodies, isolated from survivors of Coronavirus-Induced Severe Acute Respiratory Syndrome:SARS or Middle-East Respiratory Syndrome:MERS are showing surprising immune defense tactics against fatal viruses. Atomic and molecular information about the workings of the highly potent antibodies, may, provide insights to prevent these serious and, sometimes, deadly lung infections. Currently, no vaccine or specific treatment is available for any of the six coronaviruses, that can infect humans. 

Some of these coronaviruses cause, only, common-cold like symptoms but, others provoke lethal pneumonias. Past deadly outbreaks in several countries foreshadow the possibility of coronavirus-mediated pandemics. Additionally, genetic surveillance of coronaviruses in bats and the fact that the MERS coronavirus, naturally, circulates in dromedary camels, suggest that  previous outbreaks, may, not be, unusual incidences. The animal:human species barrier is likely to be crossed again and lead to new emerging coronaviruses in the future.

As part of anticipation and preparation initiatives, infectious disease research groups are trying to develop an anti-coronavirus arsenal. An international research team, headed by the University’s Medicine scientists is among those, attempting to understand how SARS and MERS coronaviruses infect humans and how their presence elicits a response from the immune system. The research group is, particularly, interested in how neutralising antibodies target the coronavirus’ cell-invasion machinery.

Their most recent findings appear in the online edition of Cell, January 31. Coronaviruses have multi-functional surface spikes, that recognise and attach to receptors on the surface of a host cell. They, then, fuse the virus and cellular membranes. They use these trimeric spike glycoproteins as their molecular break-in tool.

The spike glycoprotein densely decorates the surface of coronaviruses.  The numerous projections resemble burrs on a seed-pod.  The spikes are key to the infectivity and pathogenicity of the coronavirus. They are the target of neutralising antibodies and the main focus of sub-unit vaccine design.

Previous studies in the Veesler Lab at the University’s Medicine looked at the structural states, that occur in the coronavirus spike before and after the membrane fusion reaction. The researchers saw large conformational changes in the spike glycoprotein. Details about activation of the membrane fusion cascade, however, remained unclear.

Using cryo-electron microscopy and other powerful technologies, the researchers gained insight into how the neutralising monoclonal antibodies from the SARS and MERS survivors inhibit the viruses at the molecular level. Their findings, also, helped elucidate the unusual nature of coronavirus membrane fusion activation.

The researchers found that both the SARS and the MERS coronavirus antibodies blocked the virus spikes from interacting with the receptors on the host cell membrane.  The SARS coronavirus antibody, also, did something unexpected: it, functionally, mimicked receptor-attachment and induced the spike to undergo conformational changes, leading to membrane fusion.  This trigger seems to be driven by a molecular ratcheting mechanism.

The researchers suggest that the finding is an unprecedented example of functional mimicry, whereby, an antibody activates membrane fusion by recapitulating the action of the receptor.

This study used molecular imaging to characterise the structures of both SARS and MERS coronavirus spike glycoproteins in a complex with their respective antibodies. The researchers, also, provided a blueprint of the carbohydrates, that bedeck the spike glycoproteins, in the context of whole viruses. Coronaviruses use this strategy to mask the vulnerable portion of their fusion apparatus to limit antibody access to it and expose it only to carry out the recognition and infection of host cells.

This study was supported by the National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases, Pew Biomedical Scholars Award, Investigators in the Pathogenesis of Infectious Disease Award from the Burroughs Wellcome Fund, the Netherlands Organisation for Scientific, European Molecular Biology Organisation, Zoonoses Anticipation and Preparedness Initiative, Pasteur Institute, Centre National de la Recherche Scientifique and the LabEx Integrative Biology of Emerging Infectious Diseases, University of Washington Arnold and Mabel Beckman cryoEM Centre and Proteomics Resource and Beamline 5.0.1 at the Advanced Light Source at Lawrence Berkeley National Laboratory.:::ω.

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|| April 06: 2018 || ά. The Humanion was first published on September 24, 2015 and has been run, since that day, on a complete voluntary basis without any 'formal' or 'constituted' manner or form and, it was run on as a Human Enterprise, which is an idea of Humanics, in which, ownership is replaced by belongingship and, thus, in a Humanical Society, no one owns anything but everyone belongs to the whole as the whole belongs to everyone lawfully and equally and, it neither believes in nor makes money but human utilities, needs, aspirations, creativity, imagination and dreams are served without money, where everyone works and creates for all others as all others create and work for all others, thus, bringing in meaning and purpose to life along with it come natural justice, equality and liberty, that establish a true civilisation within the Rule of Law. And in one word, this system of human affairs management is called, Humanics and a society that runs itself in humanics is called a humanical society. Today, we have begun the process of 'constituting' this Human Enterprise, which does not exist in the current system, but the next closest thing to it, that exists in the UK Law is Social Enterprise. Therefore, today, Friday, April 06, 2018, we are beginning Regine Humanics Foundation, that is the 'Agency', that will lead, run, manage and develop everything, that The Humanion has been trying to do.

Regine Humanics Foundation is established by the Thinker, Author, Poet, Novelist, Playwright, Editor of The Humanion, Festival Director of London Poetry Festival and a Humanicsxian: hu: maa: neek: tian: One, that believes in, lives and exists by Humanics, Mr Munayem Mayenin, of London, England, United Kingdom. Mr Mayenin says, ''Humanics is a vision; people, may, call it, utopia, we, call it our Humanicsovicsopia; Humanics. Humanics is our philosophy, our faith, our conviction, our resolution, our way of existing, thinking, being and doing: to seek and try to do so in the determination that all we must do and be is to exist to advance the human condition. People, readers and agencies and organisations, from all across England, Scotland, Northern Ireland, Wales and the whole of the United Kingdom and Australasia, Africa, Asia, Europe, North and South America, from all walks and strata of life, have supported our endeavours, supported The Humanion and The Humanion Team, who volunteered their time to run things, since the beginning of The Humanion and long before that, when other things, that are now part of The Foundation, were developing. Nothing has changed in terms of the nature and value of what we have been seeking to do.''

''But the founding of The Foundation brings it all in a solid foundation so that we can keep on building this 'vision' so that it keeps on going regardless of who come to take the vision-mission of The Foundation forward. The Foundation runs along with time and along with the flowing humanity. This is the dream, this is the vision, this the hope in founding this Foundation. And, in this, we hope and invite all our readers, supporters, well wishers and all agencies and organisations to support our endeavours to build something, a Human Enterprise, which we are in the process of registering as a Social Enterprise, as a Community Interest Company, working for the common good of the one and common humanity. No one makes or takes profit out of The Foundation, which now runs The Humanion and everything else, that is part of it. The Foundation, once registered, will have an Asset Lock, which means that in any event, should The Foundation dissolve itself, all its existing assets shall go to a similar Social Enterprise. Therefore, we invite everyone to support The Foundation, support The Humanion in whatever way they can. And, there are endless number of ways people and organisations can support The Foundation and The Humanion.'' ::: ω.

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