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Human Behavior

Wonder Woman 1984: 5 Ways Cheetah Is A Sympathetic Character (& 5 Ways Shes The Worst) – Screen Rant

Cheetah is the latest to join the ranks of DCEU villains - but is she a truly bad person, or do fans feel sympathy for her?

In a change from the norm, the DCEU brought a story where the traditional aspects of good versus bad were subverted. Wonder Woman 1984 might have received mixed reviews, but the characters were well executed asthe audience is inclined to feel sympathetic even for the villains.

RELATED:Wonder Woman 1984: 10 Questions About Steve Trevor, Answered

Barbara Ann Minerva was presented as a person with low self-esteem who happened to get her wish fulfilled before this twisted her into becoming the Cheetah. Due to this backstory, there are many aspects of Barbara thatare sympathetic and relatable. Still, that doesnt mean it absolves her from blame for the bad things she did, which need to be pointed out as well.

After wishing for the natural abilities Diana possessed, Barbara found herself a confident, strong, and charming woman. Unlike Diana, though, Barbara became arrogant over these attributes and became the opposite of Diana in personality.

It proved that Barbara had an inherent darkness to her that Diana didnt and that the Dreamstone might have just pushed this aspect of Barbara out in the open. She didnt appreciate how the Dreamstone gave her the confidence she lacked, instead deciding that being charming and sought-after was the only important thing.

The DCEU version of Barbara is very different from the comic book Cheetah, who was a nasty piece of work from the beginning. The movie Barbara couldnt catch a break, as she was always overlooked and underappreciatedin life.

She knew more than her fair share in her line of work and was a pleasant person to be around in general, yet her lack of confidence led to people ignoring Barbara altogether. This is something thats relatable to many people, as Barbara developed a severe inferiority complex.

It would be incorrect to claim that Diana was a completely good person, seeing as she did have several selfish moments herself. However, she decided to do the right thing eventually, while Barbara actively worked against Diana in order to preserve her own wish.

She could have accepted that it wasnt her place to benefit from the Dreamstone when millions suffered but decided to side with Maxwell Lord to take Diana down. Due to her actions, the world came very close to being irreparably plunged into chaos.

To be fair, while Barbara did deliver a beatdown to Diana, she didnt go all-out and eliminate her opponent altogether. Due to her former friendship, Barbara retained a sense of attachment to Diana that allowed her to show mercy after shed won.

RELATED:The Suicide Squad: 5 Characters Most Likely To Die (& 5 With The Best Chance Of Survival)

Had she been completely evil, Barbara would have finished the job right then and there to prevent Diana from doing anything in the future. Her decision to let Diana live is an indication that Barbara did have an appreciation for the kindness Diana had shown her.

Despite becoming an apex predator, perhaps the worst thing Barbara did in the movie was to twist Dianas sentiments. When she became worse and embraced her evil side, Barbara claimed that Diana never understood her and wanted to stop her from being happy.

Its clear that Diana genuinely did want to be Barbaras friend when they first met and her kindness toward her had nothing to do with pity. By throwing Dianas good nature right in her face, Barbara cut herself from the one person that hadnt belittled her.

There are movies similar to Wonder Woman 1984 where characters have to deal with heavy themes and this one brought up the issue of harassment. Its a shame that Barbara had to lose her faith in people so quickly after gaining her newfound powers, as a man harassed her to no end.

It was the recollection of this event that ultimately caused her to reach murderous lengths when she later savagely attacked the man. Its entirely possible that Barbara wouldve turned out like Diana had she not had to suffer such abuse.

By the end of the story, everyones wishes were renounced when Maxwell Lord gave up his powers. This left Barbara back into her old form after her corruption into the Cheetah. Rather than display any measure of repentance, she only seemed sad about losing her powers.

Even Maxwell Lord made his regret known, but Barbara didnt feel the same way since she didnt approach Diana later on when things were back to normal. It appears as if she might have remained in her bitter way and continued being a darker personality afterward.

Barbara had never had any connections to understand how human behavior worked, being easily manipulated even by cheesy behavior from Maxwell Lord as she had never felt desirable beforehand. It was after she realized she might lose the Dreamstone wish that she became a baddie.

RELATED:10 Things About Wonder Woman You Need To Remember Before WW84

This situation was the result of Barbara being manipulated by Maxwell Lord rather than her being an evil person from the start. All in all, it wasnt her fault that she was thrust into such a scenario, not when she had no clue where it was all headed.

Barbara sealed her transition into becoming the Cheetah when she wished to become an apex predator. She still had a chance to renounce her wish and do right, especially since she was in such close proximity to Maxwell Lord, but dived completely into her dark side.

By giving in, the Cheetah entered the list of DCEU villains, one who had the best shot at avoiding this status. Had Lord been successful in stealing the life force of the people in the world, Cheetah would have been just as culpable since she was the one protecting Lord at the time.

Watching Barbara feel important was one of the best moments of Wonder Woman 1984, as she finally achieved her wish of being accepted. At the heart of it, all she ever wanted was to be considered a person worthy of notice and thats really not a bad thing.

Despite Barbara going to terrible lengths in the pursuit of such a wish, one can sympathize with where she was coming from as acceptance is an intrinsic part of a person. Had she received this feeling earlier, the Cheetah might never have come about.

NEXT:Man Of Steel: 10 Reasons It's Better Than You Remember

Next Lilo & Stitch: The Main Characters Ranked, By Likability

Saim Cheeda is an entertainment writer covering all of Film, TV, Gaming and Books. He's been a writer for Valnet since 2017, contributing 500+ articles for The Gamer, The Things, Game Rant, Comic Book Resources and Screen Rant. Apart from freelance writing, Saim is a lifestyle blogger, co-owning the blog 3 States Apart.http://3statesapart.com

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Wonder Woman 1984: 5 Ways Cheetah Is A Sympathetic Character (& 5 Ways Shes The Worst) - Screen Rant

Human Behavior

Around Town: Negativity kills – VVdailypress.com

By Pat Orr| For the Victorville Daily Press

I spend a great deal of space ruminating about political decisions, laws and the people who make them. This tends to skew my perspective to the negative. As a moderately conservative person in a state run by ultra-liberals, my view of most state government decisions is not rosy. I told my editor if this pandemic ever receded, I would like to do more local stories with a positive slant. Those are hard to come by when everyone is locked up and not circulating.

I overheard my WFL (wife for life) talking with her sister-in-law on the phone the other day. They observed that both I and her brother were doggedly negative, while they saw themselves as most always seeing the brighter, more positive side of an issue or problem. I countered with No I am just a realist. My WFL laughed. Wait I protested, I am positive. I am positive that things are terrible.

This exchange led me to the ugly realization that 2020 and all that year put us through has forever changed the attitude from sweet to sour for a great many on this planet. Add to the pandemic worries strife over race, riots, several contested elections, personal and business financial woes, and the result is a tough time to stay cheery. I decided to investigate this further. Is there a downside to being a pessimist besides being a drag at parties?

As it happens, like every other human behavior, there are academics studying the issue. Also, as it happens, your emotional well-being and health can be affected by the way you feel about life and what it presents you daily.

University of North Carolina Psychologist Dr. Barbara L. Fredrickson found that All emotions whether positive or negative are adaptive in the right circumstances. The key seems to be in finding a balance between the two.

Research has found a link between an upbeat positive mental state and lower blood pressure, reduced risk of heart disease, healthier weight and longer life. Fredrickson, and others, have found a link indicating that those who savor positive emotions activate new reward pathways deep in the brain and help produce lower levels of a stress hormone.

To reinforce the validity of these findings, Martin Seligman at the University of Pennsylvania looked at the flip side of the equation by doing extensive research on individuals aged 25 to 65 who were rated as pessimists those who routinely have a dark view of events both personal and public. Seligman found that the pessimists' health deteriorated far more rapidly as they aged.

Researchers at Yale and the University of Colorado found pessimism to be associated with weakened immune response to tumors and infection in their own studies. That could have a profound impact on how one should approach contracting any new disease or infection, like COVID-19. There is proof that staying positive helps you beat your health challenges.

Research aside, how do you set about remaking your attitude? Well, naturally, there is quite a large industry willing to teach you how to think positively. Norman Vincent Peale wrote a top selling self-help tome in 1952 that became the signpost of a new era in self-awareness. Subsequently, there has been intensive work by psychologists and physiologists into the science behind staying positive. There is also a great deal of guru-like fakery in the field, too.

In reviewing the current literature (and there is a lot of it), I found some useful tips.

Find an activity that calms and centers you. It may be walking, taking a bike ride, meditating, doing a crossword puzzle or using an adult coloring book (no kidding, they are big now). The motto here is, When the mind ceases, the soul is allowed to speak. Find a way to get away from your thoughts.

Practice the advice from the Disney movie Frozen and sing Let it go over and over. Holding onto negative thoughts and replaying them in your head continually reinforces a dark view toward new situations and issues.

Separate fact from fiction. Surprisingly, negative self-talk those things we beat ourselves up over promote a negative outlook on life. I am always going to be fat. I am too weak to quit smoking. I will never get a good job. An attitude change can often produce surprisingly successful results in the I can never category.

Get a pet. If you are a regular reader of this column, you may remember how I extolled the virtues of having a dog as a friend, companion and psychological counselor. In 2020, the adoption rate for dogs increased by over 30%. Last year, Australian researchers studying the link between pet ownership and mental health found that loneliness decreased in the group that got a dog by 40%.

Dogs also made their owners get out and be more active as a side benefit. Any pet you are comfortable interacting with will work. A parrot, gerbil or bunny are examples. You may need to be more persistent to strike up a long-term conversation with most cats, but they still nuzzle, and that is the whole point.

Help others. Find a way to volunteer. Nothing brings an upbeat attitude into your life faster than helping someone else in need. Volunteering causes the one you are helping to be optimistic and it may just infect you.

Learn something new or indulge a passion. Finding a new hobby or learning a new skill is a way to feel good about achieving something. A sense of achievement is important. For some, just planning and scheduling your day, then ticking off items as you complete them is enough to brighten an attitude. It feels good to finish something you set out to do, no matter how simple the task. You may need to force yourself to remember how good it feels to just feel good about the day you have had.

One of my friends shared her plan over Facebook recently, declaring she would do these two things to make her day go better: Will not watch the news and will not get on the bathroom scale.

Whatever it takes for you, work to make 2021 a positive year. It will be good for your health!

Contact Pat Orr at avreviewopinion@gmail.com.

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Around Town: Negativity kills - VVdailypress.com

Cell Biology

IsoPlexis secures $135M to boost its single-cell protein analysis tech – FierceBiotech

As single-cell analysis technologies continue their rapid developmentpromising a cells-eye view of protein interactions and signalingIsoPlexis hopes to establish itself as a provider of next-generation biology tools with $135 million in new financing.

Backed by Perceptive Advisors, the companys series D round includes $85 million in equity securities plus a $50 million credit facility, alongside support from Ally Bridge Group, funds managed by BlackRock and other investors.

IsoPlexis immediate plans are to expand its global sales and customer support teams, increase its commercial capacity and grow its R&D staff as it builds out its product development strategy, according to co-founder and CEO Sean Mackay.

Last November, the company debuted its IsoSpark instrument, with a tabletop footprint that aims to provide single-cell proteomics capabilities to large and small laboratories alike. IsoPlexis said it plans to begin shipments this month.

The major use of proceeds is to be able to meet the demand in the right places, for cancer immunology, cell and gene therapy and COVID, Mackay said in an interview with Fierce Medtech.

The second use of proceeds is really around the product road map, where we have in-licensed things to interrogate more aspects of single-cell biology, which includes the phospho-proteome, he added, referring to the bodys wide range of secreted proteins used to transmit messages to other cells and coordinate immune responses.

RELATED: Mission Bio raises $70M to scale single-cell cancer R&D platform

Using antibody-based proteomic barcodes, IsoPlexis hardware can tag and analyze hundreds of individual cells at once and classify each by the range of functional proteins they release.

This can help predict how certain patients may respond to checkpoint inhibitor-based cancer therapies or develop drug resistanceor give a better understanding of how the immune system may react or overreact to the coronavirus that causes COVID-19, including through a partnership with researchers at Yale University.

RELATED: Merck joins Seattle consortium to uncover COVID-19's molecular workings

Weve come out with papers showing that if you can measure more of these proteins concurrently with each single cell, you can start to resolve and treat the aberrant signaling pathways that were engaged, Mackay said.

What we hope to do is continue to popularize the need to look at the phospho-proteome, because the early data is so promising, he added. I think our platform opens up some new modalities to be able to answer critical questions about truly networked intracellular biology and how to interact with targeted inhibitors.

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IsoPlexis secures $135M to boost its single-cell protein analysis tech - FierceBiotech

Cell Biology

IsoPlexis Announces $135 Million Financing Led by Perceptive Advisors – PRNewswire

BRANFORD, Conn., Jan. 7, 2021 /PRNewswire/--IsoPlexis, the leader in single-cell functional proteomics, today announced a $135 million Series D financing comprised of $85 million in equity securities and a $50 million credit facility. The round was led by Perceptive Advisors with participation from other new investors, Ally Bridge Group and funds and accounts managed by BlackRock, as well as other existing investors. IsoPlexis will use the proceeds from this financing to expand its global commercial and R&D teams, increase operational capacity to satisfy growing demand, and accelerate its next generation single-cell biology product development roadmap.

"We believe the future of advanced medicines will rely upon deeper access toin vivobiology for the development of new therapies and are excited to back the team at IsoPlexis," said Sam Chawla of Perceptive Advisors.

Michael Altman, of Perceptive Advisors continued, "IsoPlexis' unique technology is giving researchers this access through the convergence of dynamic proteomics and single cell biology. We are delighted to support IsoPlexis and their vision to accelerate the development of personalized therapeutics to significantly impact human health."

IsoPlexis' complete end-to-end solutions are empowered by breakthrough and proprietarysingle-cell functional proteomic technology, proteomic barcode chips, that allow researchers to phenotype each immune cell by the range of its functional proteins for the first time. Housed in its software enabled IsoLight and IsoSpark detection systems, IsoPlexis provides new and accessible layers of biological data at the single-cell level and the ability to interrogate the secreted proteome, the phosphoproteome, and the metabolome from single cells for the first time. This has allowed researchers to connect more deeply to in vivo biology and predict complex responses to therapies and disease in cancer immunotherapy, cell and gene therapy, COVID-19, autoimmune disease, and many other areas.

"We are grateful to our new and existing investors for their support of our vision," said Sean Mackay, Chief Executive Officer and Co-founder of IsoPlexis. "With more than 100 systems placed and a strong team of over 200 employees, we have laid an incredibly strong foundation for future growth at the convergence of single-cell biology, proteomics, and multi-omics. Welook forward to deploying this capital to accelerate our commercial efforts as we work to leverage our powerful biology to impact the future of advanced medicines."

About IsoPlexis

IsoPlexis is a life science technology company building solutions to accelerate the development of curative medicines and personalized therapeutics. Our award-winning single-cell proteomics systems reveal unique biological activity in small subsets of cells, allowing researchers to connect more directly to in-vivo biology and develop more precise and personalized therapies. Our integrated systems named as a top innovation or design by the Scientist Magazine, Fierce, BIG Innovation and Red Dot, among others are used globally to advance the field of single-cell biology into new 'omic possibilities as our customers generate solutions to overcome the challenges of complex diseases and therapeutics. Ourproducts have been adopted by researchers around the world, including 15 of the top 15 global pharmaceutical companies and by approximately 45% of comprehensive cancer centers. Visithttp://www.isoplexis.com to learn more.

Investor Contact:Carrie Mendivil[emailprotected]

Media Contact:Jon Chen, VP of Marketing[emailprotected]

SOURCE IsoPlexis

Single Cell Proteomics | The Superhuman Cell Company | IsoPlexis

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IsoPlexis Announces $135 Million Financing Led by Perceptive Advisors - PRNewswire

Cell Biology

GHz-Class NMR Opens New Scientific Research Window for Discoveries and Novel Insights in Functional Structural Biology and Disease Biology – Business…

BILLERICA, Mass.--(BUSINESS WIRE)--Bruker Corporation (Nasdaq: BRKR) today announced that three world-leading institutions are now accelerating their research into functional structural biology and human disease with new Bruker ultra-high field nuclear magnetic resonance (NMR) spectrometers installed in 2020. Novel GHz-class NMR technology enables advanced research to obtain structural, functional and binding information of intrinsically disordered proteins (IDPs), and of partially structured proteins with key intrinsically disordered regions (IDRs), at atomic resolution under near-physiological conditions. For example, these new technological and methods capabilities now accelerate research into viral-host interactions and viral replication, as well as into proteins that are linked to neurodegenerative diseases.

The recent installation of a 1.2 GHz NMR spectrometer at the Max Planck Institute for Biophysical Chemistry in Goettingen, has already enabled their research teams to deliver new insights into the SARS-CoV-2 nucleocapsid (N) protein, and it is set to aid the deeper molecular understanding of Parkinsons and Alzheimers diseases.

Bruker's 1.2 GHz NMR magnets utilize a novel hybrid technology with high-temperature superconductor (HTS) inserts in low-temperature superconductor outer sections. The Ascend 1.2 GHz magnets are stable, homogenous, standard-bore (54 mm) magnets suitable for high-resolution and solid-state NMR.

Using ultra-high field NMR, scientists at the Max Planck Institute (MPI) and the German Center for Neurodegenerative Diseases (DZNE) have shown that the SARS-CoV-2 N protein and host ribonucleic acids (RNA) jointly condense into tiny droplets akin to membraneless organelles, when the virus enters a host cell. This fast liquid-liquid phase separation (LLPS) inside the cytoplasm of the host cell is a characteristic capability of IDPs and IDRs, and sheds new light on how the virus replicates, and offers new targets for drug development.

Professor Christian Griesinger, Director and Scientific Member at the Max Planck Institute for Biophysical Chemistry in Goettingen, commented: The new 1.2 GHz spectrometer will allow us to characterize droplets and oligomers of IDPs that are key markers in diseases such as COVID-19, neurodegenerative diseases and cancer, and which cannot be studied using crystallography or cryo-EM.

Dr. Markus Zweckstetter, Professor at the University of Goettingen and Group Leader at the German Center for Neurodegenerative Diseases, added: Our first experiments after the installation of the new ultra-high field NMR system have focused on the SARS-CoV-2 nucleocapsid N-protein that is of key relevance for viral-host interactions and viral replication biology. The liquid-like properties of viral replication machineries in combination with the many intrinsically disordered regions of the N-protein make this research ideally suited for GHz-class NMR.

Dr. Falko Busse, President of the Bruker BioSpin Group stated: The fourth quarter acceptance at the Max Planck Institute follows installations of two 1.2 GHz NMRs at CERM (University of Florence) and at ETH Zuerich earlier in 2020. We are proud to provide enabling technology for pushing the boundaries in functional structural biology and advanced materials science.

Dr. Busse continued: We are also pleased that in December 2020, we have received an order for a second Swiss 1.2 GHz system from a consortium of the University of Zuerich, ETH Zuerich and the Biozentrum of the University of Basel. For 2021, we anticipate the installation of 4-5 GHz-class NMRs, as we have used 2020 to ramp our capacity.

About Bruker Corporation (Nasdaq: BRKR)

Bruker is enabling scientists to make breakthrough discoveries and develop new applications that improve the quality of human life. Brukers high-performance scientific instruments and high-value analytical and diagnostic solutions enable scientists to explore life and materials at molecular, cellular and microscopic levels. In close cooperation with our customers, Bruker is enabling innovation, improved productivity and customer success in life science molecular research, in applied and pharma applications, in microscopy and nanoanalysis, and in industrial applications, as well as in cell biology, preclinical imaging, clinical phenomics and proteomics research and clinical microbiology. For more information, please visit: http://www.bruker.com

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GHz-Class NMR Opens New Scientific Research Window for Discoveries and Novel Insights in Functional Structural Biology and Disease Biology - Business...

Cell Biology

Global Cell Biology Cloud Computing Market Revenue Analysis Report with Future Business Scope and New Investment Plans for the Next Five Years -…

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Cell Biology

BlueRock Therapeutics in Collaboration with Memorial Sloan Kettering Cancer Center Receives IND Clearance for DA01 in Parkinson’s Disease – BioSpace

CAMBRIDGE, Mass., Jan. 7, 2021 /PRNewswire/ -- BlueRock Therapeutics, a preclinical stage biopharmaceutical company and wholly-owned subsidiary of BayerAG,in collaboration withMemorialSloan Kettering Cancer Center(MSK), announcedtodaythat the U.S. Food and Drug Administration (FDA) has clearedtheirInvestigational New Drug (IND) application toproceedwith aPhase 1(Ph1)study in patients with advanced Parkinson's disease (PD).This is the first trial in the United States to study pluripotent stem cell-derived dopaminergic neurons in patients with Parkinson's disease.Under the IND, BlueRockand MSK willexecute aPh1 clinical trial to evaluate the safety, tolerability andpreliminaryefficacyof DA01 in patients with PD.

"This is a big step for the stem cell field to finally test a truly "off-the-shelf" dopamine neuron product in human PD patients," said Lorenz Studer, MD, scientific co-founder of BlueRock and Director, Center for Stem Cell Biology at MSK. "We are also grateful for the visionary support by NYSTEM, the NY state-sponsored stem cell program that supported the earlier stages of this project."

"This trial is the culmination of a decade of arduous collaborative work that is based on very rigorous science. It is an important milestone on the road towards regenerative brain repair," said Viviane Tabar, MD, founding investigator of BlueRock and Chair of MSK's Department of Neurosurgery. "It is a real privilege and very exciting to be able to participate in both the bench science and the actual surgical intervention, here at MSK. Our collaborators at Weill Cornell Neurology will also be an integral part of the trial."

"Today, thereisno disease-modifying treatment for Parkinson's. Through this trial and those to follow, we hope to change that,"stated EmileNuwaysir, Ph.D., President and Chief Executive Officer of BlueRock. "Our therapy is intended to replace the midbrain dopaminergic neurons lost in the degenerative condition to rebuild the neural circuit, and thereby restore motor controlto Parkinson's patients. This could shift the treatment paradigm for millions ofPD patients, as well as demonstrate for the first time that degenerative disease is, in principle, reversible. We believe this would represent an enormous step forthe PD community worldwide, and formedicine."

The trial plans to enroll ten patients starting with a first clinical site at Weill Cornell Medicinein the initial open-label study. The primary objective of thePh1study is to assess the safety and tolerability of DA01 cell transplantation at one-year post-transplant. The secondary objectives of the study are to assess the evidence of transplanted cell survival and motor effects at one- and two-years post-transplant, to evaluate continued safety and tolerability at two years, and to assess feasibility of transplantation.

About Parkinson's DiseaseParkinson's disease is a progressive neurodegenerative disorder caused by nerve cell damage in the brain, leading to decreased dopamine levels. The worsening of motor and non-motor symptoms is caused by the loss of dopamine-producing neurons. At diagnosis, it is estimated that patients have already lost 60-80% of their dopaminergic neurons.Parkinson's disease often starts with a tremor in one hand. Other symptoms are rigidity, cramping and dyskinesias. Parkinson's disease is the second most common neurodegenerative disorder, impacting more than 7.5 million people, including 1.3 million people in North America.

About BlueRock TherapeuticsBlueRock Therapeutics is a leading engineered cell therapy company with a mission to develop regenerative medicines for intractable diseases. BlueRock Therapeutics' cell+gene platform harnesses the power of cells to create new medicines for neurology, cardiology and immunology indications. BlueRock Therapeutics' cell differentiation technology recapitulates the cell's developmental biology to produce authentic cell therapies, which are further engineered for additional function. Utilizing these cell therapies to replace damaged or degenerated tissue brings the potential to restore or regenerate lost function. BlueRock Therapeutics was founded in 2016 by Versant Ventures and Bayer AG and capitalized with one of the largest-ever Series A financings in biotech history by Bayer AG (through its Leaps by Bayer unit) and Versant Ventures. The company was fully acquired by Bayer in 2019. BlueRock Therapeutics' culture is defined by scientific innovation, the highest ethical standards and an urgency to bring transformative treatments to all who would benefit. For more information, visit bluerocktx.com.

About BayerBayer is a global enterprise with core competencies in the life science fields of health care and nutrition. Its products and services are designed to benefit people by supporting efforts to overcome the major challenges presented by a growing and aging global population. At the same time, the Group aims to increase its earning power and create value through innovation and growth. Bayer is committed to the principles of sustainable development, and the Bayer brand stands for trust, reliability and quality throughout the world. In fiscal 2019, the Group employed around 104,000 people and had sales of 43.5 billion euros. Capital expenditures amounted to 2.9 billion euros, R&D expenses to 5.3 billion euros. For more information, visit bayer.com.

DisclosuresDr. Studer has intellectual property rights and interests and financial interests related to BlueRock. Dr. Tabar has financial interests related to BlueRock. Researchers at Memorial Sloan Kettering Cancer Center, including Dr. Studer, developed stem cell-derived dopaminergic neurons for the treatment of neurodegenerative diseases, and MSK licensed this intellectual property to BlueRock. MSK has institutional financial interests related to this intellectual property and BlueRock.

Forward-Looking StatementsCertain statements in this press release are forward-looking within the meaning of the Private Securities Litigation Reform Act of 1995. These statements may be identified by the use of forward-looking words such as "anticipate," "believe," "forecast," "estimate" and "intend," among others. These forward-looking statements are based on BlueRock's current expectations and actual results could differ materially. There are a number of factors that could cause actual events to differ materially from those indicated by such forward-looking statements. These factors include, but are not limited to, the timing of our clinical trial for DA01; our results regarding the safety, tolerance and efficacy of DA01 cell transplantation for patients with Parkinson's disease; and ongoing FDA and other regulatory requirements regarding the development of DA01. As with any pharmaceutical under development, there are significant risks in the development, regulatory approval and commercialization of new products. Except as expressly required by law, BlueRock does not undertake an obligation to update or revise any forward-looking statement. All of the Company's forward-looking statements are expressly qualified by all such risk factors and other cautionary statements. The information set forth herein speaks only as of the date hereof.

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BlueRock Therapeutics in Collaboration with Memorial Sloan Kettering Cancer Center Receives IND Clearance for DA01 in Parkinson's Disease - BioSpace

Cell Biology

Study monitors spatial shifts of liver gene expression in relationship to the circadian clock – News-Medical.net

Nothing in biology is static. Biological processes fluctuate over time, and if we are to put together an accurate picture of cells, tissues, organs etc., we have to take into account their temporal patterns. In fact, this effort has given rise to an entire field of study known as "chronobiology".

The liver is a prime example. Everything we eat or drink is eventually processed there to separate nutrients from waste and regulate the body's metabolic balance. In fact, the liver as a whole is extensively time-regulated, and this pattern is orchestrated by the so-called circadian clock, our body's internal metronome, as well as biochemical signals and eating rhythms.

But the liver is actually divided into small repeating units called "lobules", in which distinct zones perform different functions. This intricate spatial organization is known as "liver zonation". For example, the breakdown of sugars during digestion takes place preferentially on one side of the lobule, the so-called central zone, while the production of glucose while we rest from stores such as fat, occurs on the other side of the liver, at the portal side.

So far, liver zonation has only been studied statically, looking into what each zone does independently of time, and vice-versa. And given how central the liver is in mammalian physiology, the two research approaches have to join efforts to understand how temporal and spatial liver programs interact.

In a first ever study, scientists at EPFL and the Weizmann Institute of Science, led by Professors Felix Naef at EPFL's School of Life Sciences and Shalev Itzkovitz at the Weizmann, have been able to monitor the spatial shifts of gene expression within liver lobules in relationship to the circadian clock. Studying this link is a focus of Naef's research, which has previously uncovered connections between the circadian clock and the liver's proteins, our cell cycles, and even the 3D structure of chromatin, the tightly packaged DNA in the cell nucleus.

The study came out of a EPFL-Weizmann joint grant from the Rothschild Caesarea Foundation.

By exploiting the ability to analyze liver tissue in every individual cell, the researchers studied approximately 5000 genes in liver cells at several timepoints throughout the 24-hour day. They then statistically classified the space-time patterns they uncovered with a model that can capture both spatial and temporal variations in the levels of messenger RNA (mRNA), a marker of gene expression.

The study revealed that many of the liver's genes seem to be both zonated and rhythmic, meaning that they are regulated by both their location in the liver and the time of the day. These dually regulated genes are mostly linked to key functions of the liver, e.g. the metabolism of lipids, carbohydrates, and amino acids, but also include a few genes that have never been associated with metabolism, e.g. genes related to chaperone proteins, which help other biomolecules change their 3D structure or even assemble and disassemble.

The work reveals a richness of space-time gene expression dynamics of the liver, and shows how compartmentalization of liver function in both space and time is hallmark of metabolic activity in the mammalian liver."

Felix Naef, EPFL's School of Life Sciences

Source:

Journal reference:

Droin, C., et al. (2021) Space-time logic of liver gene expression at sub-lobular scale. Nature Metabolism. doi.org/10.1038/s42255-020-00323-1.

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Study monitors spatial shifts of liver gene expression in relationship to the circadian clock - News-Medical.net

Cell Biology

Researchers determine the atomic structure of protein that helps coronavirus to evade immune cells – News-Medical.net

A team of HIV researchers, cellular biologists, and biophysicists who banded together to support COVID-19 science determined the atomic structure of a coronavirus protein thought to help the pathogen evade and dampen response from human immune cells.

The structural map - which is now published in the journal PNAS, but has been open-access for the scientific community since August - has laid the groundwork for new antiviral treatments tailored specifically to SARS-CoV-2, and enabled further investigations into how the newly emerged virus ravages the human body.

Using X-ray crystallography, we built an atomic model of ORF8, and it highlighted two unique regions: one that is only present in SARS-CoV-2 and its immediate bat ancestor, and one that is absent from any other coronavirus. These regions stabilize the protein - which is a secreted protein, not bound to the membrane like the virus's characteristic spike proteins - and create new intermolecular interfaces. We, and others in the research community, believe these interfaces are involved in reactions that somehow make SARS-CoV-2 more pathogenic than the strains it evolved from."

James Hurley, Lead Author, Professor, UC Berkeley, Former Faculty Scientist, Lawrence Berkeley National Laboratory (Berkeley Lab)

Generating protein structure maps is always labor intensive, as scientists have to engineer bacteria that can pump out large quantities of the molecule, manipulate the molecules into a pure crystalline form, and then take many, many X-ray diffraction images of the crystals. These images - produced as X-ray beams bounce off atoms in the crystals and pass through gaps in the lattice, generating a pattern of spots - are combined and analyzed via special software to determine the location of every individual atom. This painstaking process can take years, depending on the complexity of the protein.

For many proteins, the process of building a map is helped along by comparing the unsolved molecule's structure to other proteins with similar amino acid sequences that have already been mapped, allowing scientists to make informed guesses about how the protein folds into its 3D shape.

But for ORF8, the team had to start from scratch. ORF8's amino acid sequence is so unlike any other protein that scientists had no reference for its overall shape, and it is the 3D shape of a protein that determines its function.

Hurley and his UC Berkeley colleagues, experienced in structural analysis of HIV proteins, worked with Marc Allaire, a biophysicist and crystallography expert at the Berkeley Center for Structural Biology, located at Berkeley Lab's Advanced Light Source (ALS). Together, the team worked in overdrive for six months - Hurley's lab generated crystal samples and passed them to Allaire, who would use the ALS's X-ray beamlines to take the diffraction images. It took hundreds of crystals with multiple versions of the protein and thousands of diffraction images analyzed by special computer algorithms to puzzle together ORF8's structure.

"Coronaviruses mutate differently than viruses like influenza or HIV, which quickly accumulate many little changes through a process called hypermutation. In coronaviruses, big chunks of nucleic acids sometimes move around through recombination," explained Hurley. When this happens, big, new regions of proteins can appear.

Genetic analyses conducted very early in the SARS-CoV-2 pandemic revealed that this new strain had evolved from a coronavirus that infects bats, and that a significant recombination mutation had occurred in the area of the genome that codes for a protein, called ORF7, found in many coronaviruses. The new form of ORF7, named ORF8, quickly gained the attention of virologists and epidemiologists because significant genetic divergence events like the one seen for ORF8 are often the cause of a new strain's virulence.

"Basically, this mutation caused the protein to double in size, and the stuff that doubled was not related to any known fold," added Hurley. "There's a core of about half of it that's related to a known fold type in a solved structure from earlier coronaviruses, but the other half was completely new."

Like so many scientists working on COVID-19 research, Hurley and his colleagues opted to share their findings before the data could be published in a peer-reviewed journal, allowing others to begin impactful follow-up studies months earlier than the traditional publication process would have allowed. As Allaire explained, the all-hands-on-deck crisis caused by the pandemic shifted everyone in the research community into a pragmatic mindset. Rather than worrying about who accomplished something first, or sticking to the confines of their specific areas of study, scientists shared data early and often, and took on new projects when they had the resources and expertise needed.

In this case, Hurley's UC Berkeley co-authors had the viral protein and crystallography expertise, and Allaire, a longtime collaborator, was right up the hill, also with crystallography expertise and, critically, a beamline that was still operational. The ALS had received special funding from the CARES Act to remain operational for COVID-19 investigations. The team knew from reviewing the SARS-CoV-2 genomic analysis posted in January that ORF8 was an important piece of the (then much hazier) pandemic puzzle, so they set to work.

The authors have since all moved on to other projects, satisfied that they laid the groundwork for other groups to study ORF8 in more detail. (Currently, there are several investigations underway focused on how ORF8 interacts with cell receptors and how it interacts with antibodies, as infected individuals appear to produce antibodies that bind to ORF8 in addition to antibodies specific to the virus's surface proteins.)

"When we started this, other projects had been put on hold, and we had this unique opportunity to hunker down and solve an urgent problem," said Allaire, who is part of Berkeley Lab's Molecular Biophysics and Integrated Bioimaging Division. "We worked very closely, with a lot of back and forth, until we got it right. It really has been one of the best collaborations of my career."

Source:

Journal reference:

Flower, T.G., et al. (2021) Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein. Proceedings of the National Academy of Sciences. doi.org/10.1073/pnas.2021785118.

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Researchers determine the atomic structure of protein that helps coronavirus to evade immune cells - News-Medical.net

Cell Biology

Researchers investigate protein phosphatase to identify new treatments for cancer, other diseases – News-Medical.Net

The abundant presence of an enzyme known as low molecular weight protein tyrosine phosphatase (LMWPTP) in tumor cells has long been considered an indicator of cancer aggressiveness and metastatic potential. It is also known to perform important functions in cells under normal conditions, participating in both the proliferation process and the regulation of intracellular systems. Research continues on its role in cancer progression.

In Brazil, a group of researchers at the University of Campinas's In Vitro Bioassay and Signal Transduction Laboratory led by Professor Carmen Verssima Ferreira-Halder are studying the possibility of inhibiting this protein phosphatase to create novel opportunities for monitoring and treatment of cancer and other diseases.

We believe inhibition of LMWPTP could contribute to the treatment of several diseases. In our case, the focus is on cancer, but research shows it's also associated with autoimmune diseases and diabetes, among others."

Carmen Verssima Ferreira-Halder, Professor, In Vitro Bioassay and Signal Transduction Laboratory, University of Campinas

Ferreira-Halder was principal investigator for the Thematic Project "Low molecular weight protein tyrosine phosphatase in colorectal cancer: from the bench to product generation", supported by FAPESP and completed in June 2020.The phosphatase favors the action of intratumor proteins that help tumors divide, migrate and establish metastasis. "For this reason we say it's a 'hub', in the sense that it controls several processes which together make tumor cells resistant to treatment and able to migrate and establish metastasis," she said.

A review article by the group published in Cellular and Molecular Life Sciences outlines 14 years of research on LMWPTP and its contribution to cancer treatment. "Our group was one of the first to show that this enzyme contributes to chemotherapy resistance in leukemia cells," Ferreira-Halder said. "We also found that the more advanced the stage of the tumor, the larger the amount of the enzyme.

With these discoveries as a basis, research conducted in collaboration with the group led by Professor Maikel Peppelenbosch at Erasmus University Medical Center in Rotterdam [Erasmus MC, Netherlands] validated the significance of LMWPTP to other types of cancer, such as prostate, colorectal and stomach cancer. This research showed us that LMWPTP not only weakens the response to chemotherapy drugs but is also associated with a greater capacity for metastasis."

The review article, whose first author is Alessandra Valria de Sousa Faria, also discusses the available substances that inhibit LMWPTP and the characteristics that make it difficult for drugs to be designed against it. Ferreira-Halder believes it is not yet possible to speak of treatment based on inhibition of LMWPTP, but the strategy can be used for other purposes.

"Our initial aim is to use this enzyme as a biomarker for the purpose of monitoring treatment, and also to use it to classify patients in terms of the severity of disease. In my view this can be done in a relatively short time," she said. "As for treatment, a lot more work remains to be done. Professor Nunzio Bottini at the University of California San Diego [USA] has filed for a patent on a highly effective inhibitor that can be administered orally. Actually he and his group have synthesized several inhibitors, but they have only published one. Maybe we're in for a surprise and a drug will be developed faster. Who knows?"

The main challenges to be faced in developing inhibitors are specificity the drug must act specifically on LMWPTP, which is part of a family of some 100 highly similar phosphatases and stability, so that the drug remains active in the organism. "Until Bottini and his group filed their patent application, all inhibitors acted on several members of the family," Ferreira-Halder said.

Some of the substances mentioned in the review were developed for other purposes but also inhibit LMWPTP and could be used to treat cancer, according to Faria, who recently defended her doctoral thesis on how LMWPTP affects platelets, small cell fragments in the bloodstream that play a key role in clotting.

Faria's research on LMWPTP began with its role in colorectal cancer and platelet reaction in this microenvironment. "As our investigation of platelet biology progressed, we realized how much more knowledge of the enzyme's action on platelets was needed," she said.

The first part of the study consisted of verifying the action of LMWPTP and the protein tyrosine phosphatase 1B (PTP1B) on platelets, with regard to both metabolism and function. The second focused on the influence of platelets on the expression of LMWPTP in cells.

"The goal was to find out to what extent tumor cells may 'educate' platelets to support certain events, such as metastasis, for example, and conversely how far platelets 'educate' tumor cells to assure their survival and proliferation," Faria explained.

For Ferreira-Halder, the relationship appears to be two-way. "However, the action of tumor cells probably predominates. They practically program platelets to work in their favor," she said.

Ferreira-Halder and her group have collaborated with Peppelenbosch's since 2004, but work on the Thematic Project completed in June began only 2016, she recalled, adding that experiments conducted by Emanuella Maria Barreto Fonseca and Cludia de Lourdes Soraggi at Peppelenbosch's laboratory provided a vitally important foundation for the initial hypotheses. Fonseca was supported by a postdoctoral fellowship from FAPESP. Soraggi was able to attend an overseas training course thanks to support from the University of Campinas (UNICAMP) via its Executive Vice Rectorship for International Relations.

"In our Thematic Project research, we were able to investigate the action of this phosphatase from various angles and validate the hypothesis of its role in other tumors besides chronic myeloid leukemia," Ferreira-Halder said. "We wanted to uncover the mechanism of its action, and we now have a great deal of information about this action not just inside but also outside the tumor, because we set out to see if LMWPTP also influenced the tumor's microenvironment external to the cancer cells."

Other research interests for the group during the project included: extracellular vesicles (nanometer-sized structures that play an important role in intercellular communication), with Stefano Piatto Clerici supported by FAPESP showing that LMWPTP regulates these vesicles; platelets, studied by Faria, also with a scholarship from FAPESP; and the TGF-beta signaling pathway, which is involved in many cellular processes such as proliferation and differentiation and was studied by Helon Guimares Cordeiro.

The network of collaborators continued to expand, adding an expert in platelet biology (Sheila Siqueira Andrade at PlateInnove Biotech), and a hematologist and an oncologist at Erasmus MC (Moniek de Maat and Gwenny Fuhler respectively).

According to Ferreira-Halder, the Thematic Project has so far spawned 15 publications (eight articles and two book chapters, as well as five articles under peer review), and several other research fronts. A new project in the same line of research is currently being designed.

Source:

Journal reference:

Faria, A.V. S., et al. (2020) Low molecular weight protein tyrosine phosphatase as signaling hub of cancer hallmarks. Cellular and Molecular Life Sciences. doi.org/10.1007/s00018-020-03657-x.

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