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【4565】そーせいG 508【Enerzair Breezhaler(QVM149) 6月承認予定】
■ このスレッドは過去ログ倉庫に格納されています
0665山師さん@トレード中
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2020/06/17(水) 18:00:07.57ID:bg9dIJt60
M1オワッタ・・
0666山師さん@トレード中
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2020/06/17(水) 18:18:23.47ID:4KGDHidD0
>>661
ちょいやめて下さいよぉ…
0668山師さん@トレード中
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2020/06/17(水) 18:55:39.30ID:+zfwX6ARd
皆んなで岐阜さんのYouTubeライブ配信時に
そーせい買えってレスしまくろうぜ!!
0669山師さん@トレード中
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2020/06/17(水) 19:42:40.95ID:PLER8mtcd
ケケケ
0670山師さん@トレード中
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2020/06/17(水) 20:47:02.88ID:QLODQjtJ0
glp1のことだけど、ファイザーのは1日2回、ヘプのは1日一回でいいんだ。
ペプのが採用されれば、ビッグニュースだね
0672山師さん@トレード中
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2020/06/18(木) 06:00:28.34ID:LWw7Z3jY0
次なる飛躍へ。着実な進捗と共に更なる成長の黎明期にて振るい育ちゆく相場。控える材料と共に水準訂正。笑。
成長期。予定されていた業績の急成長と共に更なる成長戦略が進展。順調なR&D・PL等の拡充・拡大の加速。笑。
・・・
※Vectura 2019 Preliminary Results: QVM149 EU Launch is Expected in H2 2020. Vectura will Receive a $5m Milestone Payment Upon Approval of the Product in Europe and a Low-Single Digit Royalty on Net Sales. (3/17)
※EMA CHMP: "Pre-Authorisation Procedure Oral Explanations: QVM149 (indacaterol / Glycopyrronium bromide / mometasone furoate) - Treatment of Asthma and to Reduce Asthma Exacerbations". (3/24 Oral Explanations)
※EMA CHMP: "Recommended Granting a Marketing Authorisation for Atectura Breezhaler (QMF149), Intended for the Treatment of Asthma". (3/31)
※Propeller Health: Propeller Sensor for Breezhaler: "How to Attach Your Sensor for Breezhaler"; "How to Remove Your Sensor for Breezhaler"; "Breezhaler Sensor Technique". (4/9update)
※Novartis Q1 2020 Results: 2020 Expected Pipeline Milestones: "QVM149 Asthma (EU/JP): "CHMP Positive Opinion Anticipated Q2 2020"; "Japan Decision Anticipated H1 2020". (4/28)
※Novartis Q1 2020 Earnings Conference Call: Novartis CEO Vasant Narasimhan: "Ultibro, I think, continues in a very steady way. Hopefully, we'll soon be Launching a Triple in Asthma." (4/28)
※EMA CHMP: "Recommended Granting a Marketing Authorisation for Enerzair Breezhaler, the First Triple Combination Therapy for the Treatment of Asthma which Includes an Optional Smart Electronic Sensor". (4/30)
0673山師さん@トレード中
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2020/06/18(木) 06:00:51.17ID:LWw7Z3jY0
※Sosei Heptares:「Enerzair Breezhaler(QVM149)が喘息治療剤として欧州連合の承認勧告を取得」欧州委員会(EC)はCHMPによる承認勧告を審査し、通常約2ヵ月で承認。承認時に約534百万円のマイルストン受領。(5/1)
※Novartis: "Novartis Receives CHMP Positive Opinion for Enerzair Breezhaler (QVM149), a Potential First-in-class Inhaled LABA/LAMA/ICS Combination for Uncontrolled Asthma". (5/1)
※ATS International Conference 2020, Abstracts: "QVM149 Asthma Phase 3 Results Presentation (IRIDIUM Study, ARGON Study, Japanese Study)": (5/18 Presentation Cancelled; Abstracts Online 5/1up)
※Novartis Spain: "Novartis and the Lovexair Foundation Present MyAVA, the First Virtual Assistant to Control Asthma". Novartis' Commitment to People with Chronic Respiratory Diseases such as Asthma. (5/5)
※厚生労働省:「薬事・食品衛生審議会 医薬品第二部会 (5/28 16:30-19:00: Web会議) 開催のお知らせ」 [審議事項]:医薬品エナジア吸入用カプセル(QVM149)中用量及び高用量の製造販売承認の可否。(5/14)
※Respiratory Medicine: "Fixed-Dose Combination of IND/GLY/MF once-daily Versus Sal/Flu twice-daily Plus Tio once-daily in Patients with Uncontrolled Asthma: A Randomised, Phase IIIb, ARGON Study". (5/26 Published)
※厚生労働省 薬事・食品衛生審議会 医薬品第二部会:「審議:医薬品エナジア吸入用カプセル(QVM149)中用量及び高用量の製造販売承認の可否」結果:承認を了承しました。(5/28開催)
※ミクスOnline:「薬食審・第二部会 新薬6製品の承認了承、3成分配合喘息薬など」承認の可否を審議し、いずれも承認することを了承。順調にいけば6月に正式承認。喘息適応の3成分配合薬は初となる。(5/29)
0674山師さん@トレード中
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2020/06/18(木) 06:01:12.63ID:LWw7Z3jY0
※EC: "EU Approval for Atectura Breezhaler (QMF149)". The European Commission has Approved Atectura Breezhaler as Maintenance Therapy for Asthma for Adults and Adolescents Aged 12 Years and Over. (6/2)
※Novartis: "Novartis Phase IIIb ARGON Study Meets Primary Endpoint in a Comparison of Enerzair Breezhaler (QVM149) Versus a Free Combination of Two Existing Inhaled Treatments in Uncontrolled Asthma". (6/5)
※Sosei Heptares:「コントロール不良な喘息患者を対象とした Enerzair Breezhaler(QVM149)の第Vb 相臨床試験(ARGON試験)において主要評価項目を達成」スイス、日本を含む複数の国でも継続して承認審査が進められています。(6/5)
※厚生労働省:「薬事・食品衛生審議会 薬事分科会 (6/25 15:00-17:00: Web会議) 開催のお知らせ」[報告事項]:医薬品エナジア吸入用カプセル(QVM149)中用量及び高用量の製造販売承認の可否。(6/11up)
・・・
※厚生労働省 薬事・食品衛生審議会 薬事分科会:「報告:医薬品エナジア吸入用カプセル(QVM149)の製造販売承認」(6/25 15:00-17:00: Web会議)
※Novartis Q2 2020 Results: (7/21)
※Sosei Group 2020年12月期第2四半期決算発表 (8月)
・・・
0675山師さん@トレード中
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2020/06/18(木) 06:01:38.74ID:LWw7Z3jY0
※SOSEIの成長相場の動向:下押しでの調整 (2/17新年最高値2217、3/13最安値1051) 相場は順調に推移。笑。
2020/_2/14 (終値2012) ・(2/14安値1972) ※2/13:決算 ※25日・200日線DC(1/22) ※200日線調整下抜け
2020/_2/21 (終値2030) ・(2/21安値2004) ※2/17:決算説明会(2/17最高値2217) ※75日・200日線DC (2/19)
2020/_2/28 (終値1645) ・(2/28安値1590) ※空売りトリガー抵触(2/27) ※52週線調整下抜け
2020/_3/_6 (終値1538) ・(3/_6安値1526) ※13週・52週線DC(3/2) ※6ヶ月・12ヶ月線DC(3/2)
2020/_3/13 (終値1165) ・(3/13最安値1051※)
2020/_3/19 (終値1062) ・(3/19安値1058) ※26週・52週線DC(3/23)
0676山師さん@トレード中
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2020/06/18(木) 06:01:57.07ID:LWw7Z3jY0
2020/_3/27 (終値1288) ・(3/23安値1063) ※3/25:株主総会
2020/_4/_3 (終値1225) ・(4/_3安値1211)
2020/_4/10 (終値1327) ・(4/_6安値1212) ※4/6:Discngine 3decision Selected. ※5日・25日線再GC(4/9)
2020/_4/17 (終値1419) ・(4/13安値1325)
2020/_4/24 (終値1417) ・(4/22安値1345)
2020/_5/_1 (終値1577) ・(4/28安値1436) ※4/30: QVM149欧州承認勧告
2020/_5/_8 (終値1518) ・(5/_8安値1500) ※5/7:Orexia&Inexia進捗 ※6ヶ月・24ヶ月線DC(5/8)
2020/_5/15 (終値1687) ・(5/11安値1500) 5/13:第1四半期決算 ※一目均衡表3役好転(5/15)
0677山師さん@トレード中
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2020/06/18(木) 06:02:30.60ID:LWw7Z3jY0
2020/_5/22 (終値1794) ・(5/18安値1722) ※5日・75日線再GC(5/18) ※9週・13週線再GC(5/19)
2020/_5/29 (終値1764) ・(5/28安値1726) ※25日・75日線再GC(5/26) ※5/28: QVM149日本承認勧告
2020/_6/_5 (終値1853) ・(6/_5安値1719) ※6/5:QVM149 ARGON Study Results.
2020/_6/12 (終値1633) ・(6/12安値1589)
2020/_6/15 (終値1584) (安値1575) ※5日・25日線再DC(6/15)
2020/_6/16 (終値1689) (安値1633)
2020/_6/17 (終値1698) (安値1675)
0678山師さん@トレード中
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2020/06/18(木) 06:02:48.93ID:LWw7Z3jY0
更なる成長の黎明期、3倍圏ステージ踊り場からの再びの2倍圏ステージにて、コロナショックでの調整相場は順調な推移。笑。
今回はパンデミックにて振るいも順調に推移。笑。成長戦略は着実に進捗、次なる成長ステージが楽しみですね。笑。
0679山師さん@トレード中
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2020/06/18(木) 06:03:48.00ID:pRB0TKaH0
ファイザーとの契約では、ヘプタレスはGPCRの構造およびStaRタンパクを提供し、化合物または抗体はファイザーが作るんだよ。
よくリリースを読んでみな。
0680山師さん@トレード中
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2020/06/18(木) 06:10:04.77ID:wM1GxEo9d
読解力のない馬鹿いるねw
0681山師さん@トレード中
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2020/06/18(木) 07:00:49.75ID:LWw7Z3jY0
Article up:
・・・
※Nature: "Molecular basis of β-arrestin coupling to formoterol-bound β1-adrenoceptor". (6/17 Published)
・Nature volume 582, pages384-388(2020); Published: 17 June 2020.
Abstract: 
The β1-adrenoceptor (β1AR) is a G-protein-coupled receptor (GPCR) that couples to the heterotrimeric G protein Gs.
G-protein-mediated signalling is terminated by phosphorylation of the C terminus of the receptor by GPCR kinases (GRKs) and by coupling of β-arrestin 1 (βarr1, also known as arrestin),
which displaces Gs and induces signalling through the MAP kinase pathway2.
The ability of synthetic agonists to induce signalling preferentially through either G proteins or arrestins - known as biased agonism - is important in drug development,
because the therapeutic effect may arise from only one signalling cascade, whereas the other pathway may mediate undesirable side effects.
To understand the molecular basis for arrestin coupling, here we determined the cryo-electron microscopy structure of the β1AR -βarr1 complex in lipid nanodiscs bound to the biased agonist formoterol,
and the crystal structure of formoterol-bound β1AR coupled to the G-protein-mimetic nanobody Nb80.
βarr1 couples to β1AR in a manner distinct to that of Gs coupling to β2AR - the finger loop of βarr1 occupies a narrower cleft on the intracellular surface,
and is closer to transmembrane helix H7 of the receptor when compared with the C-terminal α5 helix of Gs.
The conformation of the finger loop in βarr1 is different from that adopted by the finger loop of visual arrestin when it couples to rhodopsin.
β1AR coupled to βarr1 shows considerable differences in structure compared with β1AR coupled to Nb80, including an inward movement of extracellular loop 3 and the cytoplasmic ends of H5 and H6.
We observe weakened interactions between formoterol and two serine residues in H5 at the orthosteric binding site of β1AR, and find that formoterol has a lower affinity for the β1AR -βarr1 complex than for the β1AR - Gs complex.
The structural differences between these complexes of β1AR provide a foundation for the design of small molecules that could bias signalling in the β-adrenoceptors.
Acknowledgements:
Work in the Christopher G. Tate laboratory was funded by a grant from the European Research Council (EMPSI 339995), Heptares Therapeutics Ltd and core funding from the Medical Research Council (MRC U105197215).
Corresponding author:
Christopher G. Tate.
Competing interests:
Christopher G. Tate is a shareholder, consultant and member of the scientific advisory board of Sosei Heptares, who also partly funded this work.
0682山師さん@トレード中
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2020/06/18(木) 07:30:29.05ID:LWw7Z3jY0
・・・

※AraInfo: "The scientific journal Nature collects the finding of a researcher from the University of Zaragoza to create improved drugs, without side effects". (6/17)
Javier Garcia Nafria, Ramon y Cajal researcher of excellence at BIFI, has collaborated in the discovery to visualize how proteins on the surface of cells work at the molecular level.
"It is a decisive step to understand at the molecular level how certain drugs activate one cellular signaling pathway in preference to another," he says.
The study was carried out on an asthma drug, thanks to the high-resolution cryo-electron microscopy technique, which was absent until recently in Aragon.
-ARAINFO JUNE 17, 2020.
Javier Garcia Nafria, Ramón y Cajal researcher of excellence at the Institute of Biocomputing and Physics of Complex Systems (BIFI) at the University of Zaragoza,
has collaborated in the finding to visualize how proteins work at the molecular level, with the ultimate goal of creating improved drugs, without side effects.
The scientific journal Nature publishes this Wednesday the results obtained thanks to the use of the high-resolution cryo-electron microscopy technique,
whose advances during the last 6 years have led to the Nobel Prize in Chemistry in 2017, and recently installed in BIFI and at the Unizar Advanced Microscopy Laboratory (LMA).
This procedure allows obtaining three-dimensional images of proteins with a high therapeutic value, previously practically unattainable through the available systems.
The results, collected in the article “Molecular basis of β-arrestin coupling to formoterol-bound β1-adrenoceptor”,
have been obtained from a study on an asthma drug, applying this technique developed in part at the MRC Laboratory of Molecular Biology (Cambridge), where Javier Garcia Nafria has worked for eight years.
This research "represents a decisive step in understanding at the molecular level how certain drugs activate one cellular signaling pathway in preference to another, with the ultimate goal of creating improved drugs."
Biochemist Javier Garcia Nafria is one of 14 Ramon y Cajal researchers currently active at the University of Zaragoza, within one of the main programs of excellence in the Spanish State to retain and attract both state and international talent.
Since his arrival at BIFI at the end of 2019, Garcia Nafra has directed the research line “Signal transduction and membrane protein therapies”.
Together with his group, he studies how proteins on the cell surface detect stimuli and transmit information to the cell interior, as well as the modulation of these proteins by drugs.
The group uses a novel technique, high-resolution cryo-electron microscopy, absent so far in Aragon, in which state-of-the-art microscopes and high-performance computing are used to visualize how proteins work at the molecular level.
Its establishment in BIFI has been key since the institute has state-of-the-art biophysical equipment, a computational cluster and a multidisciplinary environment.
In addition, the Advanced Microscopy Laboratory (AML) of Aragon, of which Javier Garcia Nafria is a member, is also used.
0683山師さん@トレード中
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2020/06/18(木) 07:30:45.03ID:LWw7Z3jY0
Results and meaning of the study:
G protein-coupled receptors (GPCRs) are on the surface of cells and mediate intercellular communication in the main organs of the human body.
Furthermore, these receptors are the most successful therapeutic targets, since 35% of the drugs used in the clinic target one of these receptors.
Examples include drugs to treat Parkinson's, schizophrenia, HIV, heart attacks, allergies, or asthma.
Drugs that join GPCRs make up 27% of the drug market, and between 2011-2015 accounted for sales of $ 890 billion.
GPCRs activate intracellular signals based on two routes: G proteins or arrestin.
The drugs currently used activate the two routes to different degrees, that is, while some drugs activate the G protein pathway more, others activate the arrestin pathway more.
This phenomenon is called biased agonism.

A route produces beneficial effects. The other, unwanted:
The problem is that normally only one of the routes provides the beneficial effects of the drug and the other provides unwanted side effects.
An example would be opiates, used as pain relievers (route 1) but also causing addiction (route 2).
Understanding how drugs activate one or the other pathway through the same receptor could help develop better drugs for a large number of diseases.
In this study two three-dimensional structures with quasi-atomic resolution are determined,
one of the adrenergic b1 receptor bound to formoterol (a drug to treat asthma) and arrestin and another structure with the same receptor bound to a molecule (nanobody) that simulates the receptor binding to G proteins.
This study is an important step in understanding at the molecular level how certain drugs activate one route preferably over another, with the ultimate goal of creating improved drugs.

About the researcher:
Javier Garcia Nafria completed his doctorate at York University (United Kingdom, 2011), and then worked for eight years in two laboratories of the MRC Laboratory of Molecular Biology (Cambridge, 2012-2019).
At this stage, he studied proteins responsible for neuronal communication and collaborated with various companies in the development of drugs (AstraZeneca, MRC-T, Heptares Therapeutics).
His work has been published in prestigious magazines such as Nature, Cell or Science.
At the end of 2019, he joined UNIZAR (as Ramon y Cajal) in the Institute of Biocomputing and Physics of Complex Systems (BIFI).
Here he has established a new line of research called "Signal Transduction and Membrane Protein Therapies."

・・・
0684山師さん@トレード中
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2020/06/18(木) 07:33:05.15ID:gaaIt3je0
>>679
IRに一つ目、二つ目、三つ目の候補物質と書いてあるからGLP1が2個はなさそうだけど
0685山師さん@トレード中
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2020/06/18(木) 07:39:30.61ID:wM1GxEo9d
馬鹿ばかり
0686山師さん@トレード中
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2020/06/18(木) 08:14:51.44ID:lLF7B1Ob0
昨日は緑十字星。今日は厳しそうじゃのおー
0687山師さん@トレード中
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2020/06/18(木) 08:20:27.05ID:nWCUo9og0
気配大暴落w
0688山師さん@トレード中
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2020/06/18(木) 08:33:00.27ID:uL/tYCA/0
ならIR出せばいいじゃん
出さないってことは無材料、もしくはデマと同じだろ
ホルダーがウキウキして推測で物言ってるに過ぎないでしょ
0689山師さん@トレード中
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2020/06/18(木) 08:50:06.69ID:0AOwmgi5d
気配大暴騰w
0691山師さん@トレード中
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2020/06/18(木) 09:09:30.13ID:0AOwmgi5d
漏れた
0693山師さん@トレード中
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2020/06/18(木) 09:30:13.77ID:XNafFvR1d
ケケケ
0694山師さん@トレード中
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2020/06/18(木) 10:24:50.98ID:0/lvXGDqd
いやぁ本当ブレないねぇ
上髭からの陰線マイテン雪崩
そーせいさん買い天井は鉄板だねぇ笑
0695山師さん@トレード中
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2020/06/18(木) 10:31:25.33ID:nWCUo9og0
大暴落ww
空売り外資様を舐めんなよ
0697山師さん@トレード中
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2020/06/18(木) 11:36:43.32ID:nWCUo9og0
>>696
空売り外資様を舐めんなよ
0698山師さん@トレード中
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2020/06/18(木) 11:50:25.75ID:TZl9rf3P0
ちょい待って下さいよぉ…
0700山師さん@トレード中
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2020/06/18(木) 12:47:52.92ID:0v8IswxLd
ケケケ
0702山師さん@トレード中
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2020/06/18(木) 15:00:20.90ID:LWw7Z3jY0
・・・
※MRC Laboratory of Molecular Biology Twitter 13時間前:
"Researchers from Chris Tate’s group in Structural Studies Division, and others, have solved the first high-resolution structure of a GPCR-arrestin complex."

※MRC Laboratory of Molecular Biology: Insight on Research: "First High-Resolution Structure of a GPCR-Arrestin Complex". (6/17)
Published on 17 June, 2020.
Understanding minute structural differences in GPCR (G protein-coupled receptor) complexes could lead to the design of more efficacious drugs that have fewer side effects.
Yang Lee, Tony Warne and Rony Nehmé from Chris Tate’s group in the Structural Studies Division, and others, have solved the first high-resolution structure of arrestin coupled to a non-sensory GPCR.
The β1-adrenoceptor (β1AR) is a GPCR activated by the hormone noradrenaline.
What are GPCRs?
G protein-coupled receptors (GPCRs) are integral membrane proteins that transduce chemical signals from the extracellular matrix into the cell.
There are ~800 GPCRs encoded by the human genome and they respond to a diverse array of stimuli such as hormones, neurotransmitters, ions, photons and odorants.
They play an important role in physiology and disease, and represent attractive drug targets.
Ligands that activate GPCRs may push signalling preferentially through either G proteins or arrestins in a phenomenon known as biased agonism.
These different couplings are important in drug development, as the therapeutic effect may arise from only one signalling cascade, while the other pathway may mediate undesirable side effects.
Unfortunately, the molecular basis for this phenomenon is poorly understood. However, there is good evidence that arrestin-biased ligands stabilise different subsets of receptor conformations compared to G protein-biased ligands.
0703山師さん@トレード中
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2020/06/18(木) 15:00:39.43ID:LWw7Z3jY0
GPCRs trigger critical intracellular signalling cascades through coupling with G proteins or arrestins - a process that is called ‘biased agonism’.
A receptor can activate more than one signalling cascade and the one that is activated is determined by what activates it (in this case, either the G protein or the arrestin).
Whichever triggers the receptor is an agonist and it biases the signalling in a particular direction. And certain ligands/drugs can bias this critical signalling towards either G proteins or arrestins.
GPCRs bind to various proteins (and form complexes) and it is quite difficult to catch them in these conformations to discern the differences among these complexes.
A large number of GPCR-G protein complexes have been determined by cryo-EM in recent years.
However, structure determination of a GPCR-arrestin complex presents a greater challenge due to its smaller size, greater flexibility and specific requirements for complex formation.
Published in Nature, the key advance of the work is the comparison of the β1-adrenoceptor with the same ligand, coupled to either arrestin or a G protein mimetic at high enough resolution to observe subtle changes in the receptor.
These minute differences are critical.
The coupling of arrestins to GPCRs is dependent on receptor phosphorylation.
Starting with a thermostabilised form of the β1-adrenoceptor, the scientists engineered the end of the receptor to allow attachment of a synthetic phosphorylated peptide.
This allowed them to produce a sample that was both highly and homogeneously phosphorylated.
The coupling of arrestin to the phosphorylated receptor proved inefficient when performed in detergent.
0704山師さん@トレード中
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2020/06/18(木) 15:00:55.39ID:LWw7Z3jY0
To overcome this, they replaced the detergent that the receptor was purified in with a nanodisc - this is a discoidal lipid bilayer stabilised at its edges by a protein scaffold.
Arrestins are known to interact with elements of the lipid bilayer when coupled to GPCRs. The nanodisc environment provides many of the essential factors.
To further stabilise the receptor-arrestin complex, they engineered arrestin with a mutation known to predispose it to its coupled state as well as introduced an antibody binder that recognises and locks it in said state.
Having optimised the preparation biochemically, the sample was frozen in vitreous ice on cryo-EM grids for imaging on the Titan Krios.
With the help of electron microscopy and high-performance computing resources and expertise at the LMB,
the researchers processed more than 18,000 images collected on the microscopes at the LMB and Diamond Light Source-eBIC in order to solve the structure.
As a proof of concept, this would be highly significant as many drug companies are trying to develop biased drugs to reduce side effects of current medications.
A classic example of this is in pain therapy, where long-term use of opiates leads to chronic constipation, tolerance and addiction.
The work was funded by UKRI MRC, the Wellcome Trust, European Research Council, Department of Biotechnology, Indian Institute of Technology, Kanpur, India, Heptares Therapeutics,
Council of Scientific and Industrial Research, India, BBSRC and the European Synchrotron Radiation Facility.

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0705山師さん@トレード中
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2020/06/18(木) 15:01:14.34ID:LWw7Z3jY0
※European Synchrotron Radiation Facility (ESRF): "First High-Resolution Structure of a GPCR-Arrestin Complex". (6/17)
17-06-2020.
An international team of scientists led by Chris Tate's group at the MRC Laboratory of Molecular Biology (UK),
have solved the first high-resolution structure of arrestin coupled to a non-sensory GPCR, using cryoEM and the MASSIF-1 automated beamline at the ESRF.
The β1-adrenoceptor (β1AR) is a GPCR activated by the hormone noradrenaline.
・・・
The team of scientists used cryo-EM to determine the structure of the receptor-arrestin complex. However, they also needed the structure of the receptor alone bound to formoterol to allow comparisons with other receptor complexes.
The receptor alone is too small for cryo-EM studies so X-ray crystallography, carried out at the the ESRF’s unique fully automated beamline MASSIF-1, was used GPCRs are flexible molecules and crystals tend to vary enormously in their quality.
This means that a large number need to be screened to find the few that provide good data. The full automation of sample mounting and data collection on MASSIF-1 allowed a huge number of crystals to be assessed without human presence.
Coupled to automatic workflows that identify the best areas of crystals and calculate optimised data collection strategies, high quality data could be collected for these challenging samples clearly showing the effect of the bound drug.
“We have used these crystals to develop new algorithms for intelligent data collection because they were so challenging to work with – it is fantastic to see these method developments now supporting important translational research”
says Matthew Bowler (EMBL), scientist co-responsible for the operation of MASSIF-1.
“The automated routines on MASSIF-1 have allowed the researchers to determine a high-resolution structure of the receptor while spending more time on the electron microscopy.
The combination of these two techniques is extremely powerful” adds Didier Nurizzo (ESRF), scientist co-responsible for the operation of MASSIF-1.
As a proof of concept, this work could be highly significant as many drug companies are trying to develop biased drugs to reduce side effects of current medications.
A classic example of this is in pain therapy, where long-term use of opiates leads to chronic constipation, tolerance and addiction.
・・・
0706山師さん@トレード中
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2020/06/18(木) 15:05:21.71ID:LWw7Z3jY0
次なる飛躍へ。着実な進捗と共に更なる成長の黎明期にて振るい育ちゆく相場。控える材料と共に水準訂正。笑。
成長期。予定されていた業績の急成長と共に更なる成長戦略が進展。順調なR&D・PL等の拡充・拡大の加速。笑。
・・・
※Sosei Groupは創立30周年を2020年6月22日に迎える。
※AACR: "Clinical Pharmacology of AZD4635: Integration of PK data from Cancer Patients and Healthy Volunteer Clinical Trials to Provide Dosing Recommendations" (6/22 9:00: Virtual)
※AACR: "Targeting A2aR (AZD4635) in Mouse Pten-Deficient Prostate Cancer" (6/23 9:05-9:15: Virtual)
※薬事・食品衛生審議会 薬事分科会:「報告:医薬品エナジア吸入用カプセル(QVM149)の製造販売承認」(6/25 15:00-17:00: Web会議)
※四季報2020年3集夏号 (四季報先取り新興株50:6/12〜6/25に配信) (四季報6/26発売・更新)
※Novartis Q2 2020 Results: (7/21)
※AstraZeneca Q2 2020 Results: (7/30)
※Sosei Group 2020年12月期第2四半期決算発表 (8月)
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0707山師さん@トレード中
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2020/06/18(木) 15:05:41.85ID:LWw7Z3jY0
※SOSEIの成長相場の動向:再成長期にて、今回のコロナショックでの下押し調整(3/13※最安値1051)は順調に推移しましたね。笑。
2019/12/30 (終値2171) 買残高_7743600 ・(12/16安値2137) ※12/6:IR説明会(広島)
2020/_1/31 (終値1932) 買残高_7134700 ・(1/30安値1825) ※1/15: Presentation
2020/_2/28 (終値1645) 買残高_5606500 ・(2/28安値1590) ※2/13::決算※(2/17:新年最高値2217)
2020/_3/27 (終値1288) 買残高_3487900 ・(3/13最安値1051※) ※3/25::株主総会
2020/_5/_1 (終値1577) 買残高_3389600 ・(4/22安値1345) ※4/30: QVM149欧州承認勧告※5/13:第1四半期決算
2020/_5/29 (終値1818) 買残高_3355400 ・(5/8; 5/11安値1500) ※5/28: QVM149日本承認勧告
0708山師さん@トレード中
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2020/06/18(木) 15:05:56.55ID:LWw7Z3jY0
2020/_6/_5 (終値1853) 買残高_3746400 ・(6/_4安値1716) ※6/5:QVM149 ARGON Study Results.
2020/_6/12 (終値1633) 買残高_3875100 ・(6/12安値1589)
2020/_6/15 (終値1584) 5日線1707.20( -7.22%) 25日線1749.24( -9.45%) 75日線1524.74( +3.89%) (安値1575)
2020/_6/16 (終値1689) 5日線1686.80(+0.13%) 25日線1754.32( -3.72%) 75日線1521.65(+11.00%) (安値1633)
2020/_6/17 (終値1698) 5日線1664.80(+1.99%) 25日線1759.48( -3.49%) 75日線1520.24(+11.69%) (安値1675)
2020/_6/18 (終値1712) 5日線1663.20(+2.93%) 25日線1764.24( -2.96%) 75日線1520.73(+12.58%) (安値1689)
0709山師さん@トレード中
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2020/06/18(木) 15:06:14.30ID:LWw7Z3jY0
更なる成長の黎明期、3倍圏ステージ踊り場からの再びの2倍圏ステージにて、コロナショックでの調整相場は順調な推移。笑。
今回はパンデミックにて信用需給が改善し、振るいも順調に推移しました。笑。次なる成長ステージが楽しみですね。笑。
0710山師さん@トレード中
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2020/06/18(木) 15:11:44.81ID:0v8IswxLd
ホルダーおめ
0712山師さん@トレード中
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2020/06/18(木) 16:55:13.22ID:XfHLvYXta
ちょい待って下さいよぉ…
0713山師さん@トレード中
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2020/06/18(木) 17:41:23.63ID:lLF7B1Ob0
昨日は緑十字線、今日は赤十字線。 明日も厳しそうじゃのおー
0715山師さん@トレード中
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2020/06/18(木) 18:09:35.29ID:xXoVJoWm0
M1オワッタ・・
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