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#rex1e
analanaisdying · 25 days
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Strong believer that what ur eating is just as important as how much u r.
Because 100cals of fruit is not gonna make u fat but 100cals of Doritos will.
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cs-kang · 1 year
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it’s so weird not to feel my arms touching my waist anymore. can’t wait to have that same feeling when my thighs stop touching
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ask-the-toy-box · 1 year
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speekygeeky · 2 years
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Join Rex-1 and more on a brand new episode of @speekygeeky original deep dive series TMNT NECA “Which Figures do We Want?” https://youtu.be/r0D9J35lxGw
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clickonmedotexe · 2 years
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"REX1E 1'M DO1NG TH1S BECAUSE Y0U D1DNT INV1TE ME 2 THE WEDD1NG WHY W0ULDNT YOU INVITE ME THAT'2 THE CRU3LEST TH1NG Y♡U COULD D0 2 SOMEONE"
"Drop the act, whore. You'll come whether I want you there or not, won’t you. Don't you have your boytoy to fuck or something? More arms to rip off?"
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kittyzsemetery · 16 days
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guys turns out i dont have superpowers like some rex1es and cannot do 50k steps while f@sting
i omad 330c and now ill do the 50k, im at 20k rn and after eating i have so much more energy and im moving at a normal/fast pace again🪶
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starvingofc · 1 year
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moving out of my junk@ rex1e era…. i badly want a low body fat %
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abstraxidesign · 3 years
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Get carried away by the electric revolution! The RE-X1 electric car from Kreisel in action in our wrapping project. Fot.Harald Illmer #rex1 #baumschlager #electricrx #kreiselrex1 #kreisel #electriccar #wrapdesign #carwrap #electricmotorsport #LIVERYDESIGN #kreiselelectric https://www.instagram.com/p/CK1XITXj1AX/?igshid=13nt2kpuizptv
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specialsockdrawer · 4 years
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Rex1-060_r
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analanaisdying · 2 months
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If you’re asking yourself rn if you should eat that, even if it’s just a tiny thing, the answer is no. The second you pick it up you’ll lose all control and binge.
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tamimuniverse · 3 years
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qfwagseg
http://piafimages.org/rex1/v-ideo-Metz-lequip-fr-01.html http://piafimages.org/rex1/v-ideo-Metz-lequip-fr-02.html http://piafimages.org/rex1/v-ideo-Metz-lequip-fr-03.html http://piafimages.org/rex1/v-ideo-Reims-foot-xfr-01.html http://piafimages.org/rex1/v-ideo-Reims-foot-xfr-02.html http://piafimages.org/rex1/v-ideo-Reims-foot-xfr-03.html
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vitalykuzmin · 5 years
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Нелетальное оружие для защиты от дронов REX 1 REX 1 anti-drone gun #rex1 #antidrone #zala #kalashnikov #антидрон #калашников https://t.co/Kd6IIptDcW
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uzladets · 3 years
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Škoda elektriskā rallija mašīna ir debitējusi sacensībās Elektriskā rallija sporta automašīna ŠKODA RE-X1 Kreisel autosporta pasaulē savā pirmajā oficiālajā uznācienā, kas notika Austrijā Rallye Weiz sacensībās, sacenšoties ar iekšdedzes dzinēju automašīnām, ieguva trešo vietu kopvērtējumā. Saite profila aprakstā. #Škoda #elektrisks #rallijs #debija #sacensības #rex1 #kreisel #Austrija #RallyeWeiz #automašīna #elektroauto #elektromobilis #electric #rally #debut #race #Austria #car #electricvehicle #electriccar #ev #bev — view on Instagram https://ift.tt/3ldgd4L
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quickyblog · 3 years
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Skoda RE-X1 Kreisel एक ऑल-इलेक्ट्रिक रैली कार है https://tinyurl.com/yz4appes #kreisel #rex1 #skoda #एक #ऑटो_समाचार #ऑलइलकटरक #कर #कारैंडबाइक #रल #समाचार #स्कोडा #स्कोडा_ऑटो #स्कोडा_फ़ेबिया #स्कोडा_मोटरस्पोर्ट #स्कोडा_री-x1_क्रेज़ेल #ह
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tokka · 4 years
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#CenicientaVideo #LasTortugasNinja
"El Más Brillante de Nueva York" ( 'New York's Shiniest' ) #VHS #199x Cortesía de @poacherscorner.wav
#REX1 #TMNT
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sciencespies · 5 years
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Study unveils the intricate way two proteins interact to promote cell movement, metastasis
https://sciencespies.com/biology/study-unveils-the-intricate-way-two-proteins-interact-to-promote-cell-movement-metastasis/
Study unveils the intricate way two proteins interact to promote cell movement, metastasis
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The cryo-EM 3D reconstruction (left) of the protein P-Rex1 bound to Gβγ and the proteinmodel (right) showing that Gβγ (top; blue and green) binds to a compact, multi-domain surfaceon P-Rex1 (bottom; yellow, magenta, teal and gold). Credit: Jennifer Cash, U-M LifeSciences Institute.
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When cells in our bodies need to move—to attack an infection or heal a wound, for example—cellular proteins send and receive a cascade of signals that directs the cells to the right place at the right time. It’s a process cancer cells can hijack to spread to new tissues and organs.
Now, a team of researchers led by the University of Michigan Life Sciences Institute has shed light on a key driver of this process. The findings, scheduled to publish Oct. 16 in Science Advances, offer important insights into cell migration not only under normal health conditions, but also in breast, prostate and other types of cancers.
The researchers specifically probed a protein called P-Rex1 (phosphatidylinositol 3,4,5-triphosphate-dependent Rac exchanger 1), which is activated when it binds another protein, Gbg. Despite the discovery of P-Rex1 more than 15 years ago, precisely how the two proteins interact and how this interaction leads to cell movement has remained poorly understood.
Using a combination of structural biology and biochemistry techniques, the researchers have revealed the structure of P-Rex1 bound to Gbg, providing a snapshot of how this intricate activation process unfolds.
“Knowing the structure of this protein complex provides mechanistic details that allow us to understand how it is regulated,” said Jennifer Cash, LSI researcher and lead author of the study. “And when we understand how it’s regulated, we can start to think about how to modify that regulation and inhibit P-Rex1 signaling in cancers.”
The team found that Gbg binds to an extensive surface on P-Rex1 comprised of several different protein domains. Previous studies offered conflicting arguments about which domain (or domains) bound Gbg. But this latest study was able to resolve the conflict by taking a bigger-picture view of the protein, using newer technologies.
“We wanted to look at the enzyme as a whole—and to do that, we really needed to move into cryo-EM,” said John Tesmer, professor of biological sciences at Purdue University and one of the study’s senior authors.
Cryo-EM, or cryo-electron microscopy, enables researchers to study proteins that cannot be visualized using other structural biology techniques—such as the complex, interwoven structure of P-Rex1. The process involves freezing proteins in a thin layer of water and then using electrons to capture images of their shape. Hundreds of thousands of images are then averaged to create a 3-D structure.
Beyond clarifying how Gbg binds to and activates P-Rex1, these new findings stand as an important touchstone in the development of cryo-EM, said Michael Cianfrocco, LSI assistant professor and senior author of the study.
The majority of structures determined with cryo-EM are larger, symmetric molecules. The results for P-Rex1, in contrast, represent a high-resolution structure of the smallest asymmetric protein achieved through cryo-EM to date. Furthermore, a large domain in P-Rex1 has a structure or fold that had not previously been identified in any other mammalian protein, requiring the team to build it piece by piece—a difficult task with cryo-EM data.
“Cryo-EM is still a relatively new field, and people are really interested in knowing how far its limits can be pushed,” said Cianfrocco, who is also an assistant professor of biological chemistry at the U-M Medical School.
The Science Advances papers is titled “Cryo-electron microscopy structure and analysis of the P-Rex1-Gbg signaling scaffold.”
Explore further
Realization of new image-based structure analysis method for 3-D structural analysis of biology
More information: “Cryo–electron microscopy structure and analysis of the P-Rex1–Gβγ signaling scaffold” Science Advances (2019). advances.sciencemag.org/content/5/10/eaax8855
Provided by University of Michigan
Citation: Study unveils the intricate way two proteins interact to promote cell movement, metastasis (2019, October 16) retrieved 16 October 2019 from https://phys.org/news/2019-10-unveils-intricate-proteins-interact-cell.html
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