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Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН
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Каталог диссертаций ИБФ СО РАН
Труды сотрудников ИБФ СО РАН
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1.

Вид документа : Статья из сборника (однотомник)
Шифр издания :
Автор(ы) : Illarionova V.A., Illarionov B.A., Bondar V.S., Vysotski E.S., Blinks J.R.
Заглавие : Removal of essential ligand in N-terminal calcium binding domain of obelin does not inactivate the photoprotein or reduce its calcium sensitivity, but dramatically alters the kinetics of the luminescent reaction
Место публикации : BIOLUMINESCENCE AND CHEMILUMINESCENCE: MOLECULAR REPORTING WITH PHOTONS: JOHN WILEY & SONS LTD, 1997. - 9th International Symposium on Bioluminescence and Chemiluminescence (OCT, 1996, WOODS HOLE, MA). - С. 431-434. - 4. - ISBN 0-471-97502-8
Примечания : Cited References: 0
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2.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Natashin P.V., Song L..., Zhou Y.G., van Berkel WJH, Liu Z.J., Vysotski E.S.
Заглавие : Oxygen Activation of Apo-obelin-Coelenterazine Complex
Колич.характеристики :7 с
Место публикации : ChemBioChem: WILEY-V C H VERLAG GMBH, 2013. - Vol. 14, Is. 6. - С. 739-745. - ISSN 1439-4227, DOI 10.1002/cbic.201300002
Примечания : Cited References: 46. - The work was supported by grants from the RFBR 12-04-91153, and NSFC 31270795 and 31021062, by the Russian Federation Government Program "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of the Russian Federation "Leading Science School" (grant 1044.2012.2). E.V.E. was supported by a Wageningen University Sandwich PhD Fellowship Program.
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
JELLYFISH CLYTIA-GREGARIA
CRYSTAL-STRUCTURE
CA2+-DISCHARGED PHOTOPROTEIN
ANGSTROM RESOLUTION
RECOMBINANT OBELIN
MOLECULAR-OXYGEN
AEQUORIN
CALCIUM
BIOLUMINESCENCE
Ключевые слова (''Своб.индексиров.''): aequorin--coelenterazine--luminescence--photoprotein--protein folding
Аннотация: Ca2+-regulated photoproteins use a noncovalently bound 2-hydroperoxycoelenterazine ligand to emit light in response to Ca2+ binding. To better understand the mechanism of formation of active photoprotein from apoprotein, coelenterazine and molecular oxygen, we investigated the spectral properties of the anaerobic apo-obelincoelenterazine complex and the kinetics of its conversion into active photoprotein after exposure to air. Our studies suggest that coelenterazine bound within the anaerobic complex might be a mixture of N7-protonated and C2() anionic forms, and that oxygen shifts the equilibrium in favor of the C2() anion as a result of peroxy anion formation. Proton removal from N7 and further protonation of peroxy anion and the resulting formation of 2-hydroperoxycoelenterazine in obelin might occur with the assistance of His175. It is proposed that this conserved His residue might play a key role both in formation of active photoprotein and in Ca2+-triggering of the bioluminescence reaction.
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3.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Markova S.V., Frank L.A., Visser AJWG, van Berkel WJH, Vysotski E.S.
Заглавие : Bioluminescent and spectroscopic properties of His-Trp-Tyr triad mutants of obelin and aequorin
Колич.характеристики :9 с
Место публикации : Photochem. Photobiol. Sci.: ROYAL SOC CHEMISTRY, 2013. - Vol. 12, Is. 6. - С. 1016-1024. - ISSN 1474-905X, DOI 10.1039/c3pp00002h
Примечания : Cited References: 46. - The work was supported by RFBR grant 12-04-00131, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" (grant 1044.2012.2). E.V.E. was supported by Wageningen University Sandwich PhD-Fellowship Program.
Предметные рубрики: CA2+-REGULATED PHOTOPROTEINS
CA2+-BINDING PHOTOPROTEIN
SEQUENCE-ANALYSIS
CRYSTAL-STRUCTURE
VIOLET BIOLUMINESCENCE
ANGSTROM RESOLUTION
MNEMIOPSIS-LEIDYI
LIGHT-EMISSION
W92F OBELIN
CLONING
Аннотация: Ca2+-regulated photoproteins are responsible for the bioluminescence of a variety of marine organisms, mostly coelenterates. The photoproteins consist of a single polypeptide chain to which an imidazopyrazinone derivative (2-hydroperoxycoelenterazine) is tightly bound. According to photoprotein spatial structures the side chains of His175, Trp179, and Tyr190 in obelin and His169, Trp173, Tyr184 in aequorin are at distances that allow hydrogen bonding with the peroxide and carbonyl groups of the 2-hydroperoxycoelenterazine ligand. We replaced these amino acids in both photoproteins by residues with different hydrogen bond donor-acceptor capacity. All mutants exhibited luciferase-like bioluminescence activity, hardly present in the wild-type photoproteins, and showed low or no photoprotein activity, except for aeqH169Q (24% of wild-type activity), obeW179Y (23%), obeW179F (67%), obeY190F (14%), and aeqY184F (22%). The results clearly support the supposition made from photoprotein spatial structures that the hydrogen bond network formed by His-Trp-Tyr triad participates in stabilizing the 2-hydroperoxy adduct of coelenterazine. These residues are also essential for the positioning of the 2-hydroperoxycoelenterazine intermediate, light emitting reaction, and for the formation of active photoprotein. In addition, we demonstrate that although the positions of His-Trp-Tyr residues in aequorin and obelin spatial structures are almost identical the substitution effects might be noticeably different.
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4.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Eremeeva E.V., Vysotski E.S., Westphal A.H., van Mierlo CPM, van Berkel WJH
Заглавие : Ligand binding and conformational states of the photoprotein obelin
Колич.характеристики :7 с
Место публикации : FEBS Lett.: ELSEVIER SCIENCE BV, 2012. - Vol. 586, Is. 23. - С. 4173-4179. - ISSN 0014-5793, DOI 10.1016/j.febslet.2012.10.015
Примечания : Cited References: 24. - The work was supported by RFBR grant 12-04-00131, by the Program of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.058), by the Program "Molecular and Cellular Biology" of RAS. The Wageningen University Sandwich PhD-Fellowship Program supported E.V.E.
Предметные рубрики: RECOMBINANT OBELIN
CRYSTAL-STRUCTURE
LIGHT-EMISSION
APO-AEQUORIN
BIOLUMINESCENCE
COELENTERAZINE
LUMINESCENCE
STABILITY
ANGSTROM
PROTEINS
Ключевые слова (''Своб.индексиров.''): bioluminescence--coelenterazine--photoprotein--thermostability
Аннотация: Many proteins require a non-covalently bound ligand to be functional. How ligand binding affects protein conformation is often unknown. Here we address thermal unfolding of the free and ligand-bound forms of photoprotein obelin. Fluorescence and far-UV circular dichroism ( CD) data show that the various ligand-dependent conformational states of obelin differ significantly in stability against thermal unfolding. Binding of coelenterazine and calcium considerably stabilizes obelin. In solution, all obelin structures are similar, except for apo-obelin without calcium. This latter protein is an ensemble of conformational states, the populations of which alter upon increasing temperature. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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5.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Liu Z.J., Stepanyuk G.A., Vysotski E.S., Lee J..., Markova S.V., Malikova N.P., Wang B.C.
Заглавие : Crystal structure of obelin after Ca2+-triggered bioluminescence suggests neutral coelenteramide as the primary excited state
Колич.характеристики :6 с
Место публикации : Proc. Natl. Acad. Sci. U. S. A.: NATL ACAD SCIENCES, 2006. - Vol. 103, Is. 8. - С. 2570-2575. - ISSN 0027-8424, DOI 10.1073/pnas.0511142103
Примечания : Cited References: 51
Предметные рубрики: X-RAY-DIFFRACTION
ANGSTROM RESOLUTION
CA2+-REGULATED PHOTOPROTEINS
AEQUORIN BIOLUMINESCENCE
VIOLET BIOLUMINESCENCE
W92F OBELIN
PROTEIN
LUCIFERASE
LIGHT
PROGRAM
Ключевые слова (''Своб.индексиров.''): coelenterazine--photoprotein--ef hand--luciferase--aequorin
Аннотация: The crystal structure at 1.93-angstrom resolution is determined for the Ca2+-discharged obelin containing three bound calcium ions as well as the product of the bioluminescence reaction, coelenteramide. This finding extends the series of available spatial structures of the ligand-dependent conformations of the protein to four, the obelin itself, and those after the bioluminescence reaction with or without bound Ca2+ and/or coelenteramide. Among these structures, global conformational changes are small, typical of the class of "calcium signal modulators" within the EF-hand protein superfamily. Nevertheless, in the active site there are significant repositions of two residues. The His-175 imidazole ring flips becoming almost perpendicular to the original orientation corroborating the crucial importance of this residue for triggering bioluminescence. Tyr-138 hydrogen bonded to the coelenterazine N1-atom in unreacted obelin is moved away from the binding cavity after reaction. However, this Tyr is displaced by a water molecule from within the cavity, which now forms a hydrogen bond to the same atom, the amide N of coelenteramide. From this observation, a reaction scheme is proposed that would result in the neutral coelenteramide as the primary excited state product in photoprotein bioluminescence. From such a higher energy state it is now energetically feasible to account for the shorter wavelength bioluminescence spectra obtained from some photoprotein mutants or to populate the lower energy state of the phenolate anion to yield the blue bioluminescence ordinarily observed from native photoproteins.
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6.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Purtov K.V., Petunin A.I., Burov A.E., Puzyr A.P., Bondar V.S.
Заглавие : Nanodiamonds as Carriers for Address Delivery of Biologically Active Substances
Колич.характеристики :6 с
Коллективы :
Место публикации : Nanoscale Res. Lett.: SPRINGER, 2010. - Vol. 5, Is. 3. - С. 631-636. - ISSN 1931-7573, DOI 10.1007/s11671-010-9526-0
Примечания : Cited References: 24. - This work was supported by the Program # 27 for Basic Research of the Presidium of RAS (project 3.6.3).
Предметные рубрики: ANTICANCER DRUGS
NANOPARTICLES
ADSORPTION
PARTICLES
PROTEINS
Ключевые слова (''Своб.индексиров.''): nanodiamonds--ligand--protein immobilization--nanocarrier--targeted delivery
Аннотация: Surface of detonation nanodiamonds was functionalized for the covalent attachment of immunoglobulin, and simultaneously bovine serum albumin and Rabbit Anti-Mouse Antibody. The nanodiamond-IgG(I125) and RAM-nanodiamond-BSA(I125) complexes are stable in blood serum and the immobilized proteins retain their biological activity. It was shown that the RAM-nanodiamond-BSA(I125) complex is able to bind to the target antigen immobilized on the Sepharose 6B matrix through antibody-antigen interaction. The idea can be extended to use nanodiamonds as carriers for delivery of bioactive substances (i.e., drugs) to various targets in vivo.
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7.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Gibson B.G., Lee J.
Заглавие : Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates
Место публикации : Biochemistry. - 1995. - Vol. 34, Is. 10. - С. 3300-3309. - ISSN 00062960 (ISSN)
Ключевые слова (''Своб.индексиров.''): luciferase--recombinant protein--article--ligand binding--nonhuman--priority journal--protein isolation--protein protein interaction--protein stability--vibrionaceae--bacterial proteins--binding sites--carrier proteins--circular dichroism--flavin mononucleotide--fluorescence polarization--genes, bacterial--kinetics--ligands--luciferase--luminescence--molecular sequence data--photobacterium--recombinant proteins--spectrophotometry--support, u.s. gov't, p.h.s.--photobacterium leiognathi--vibrionaceae
Аннотация: Ligand binding and luciferase interaction properties of the recombinant protein corresponding to the lumazine protein gene (EMBL X56534) of Photobacterium leiognathi have been determined by fluorescence dynamics, circular dichroism, gel filtration, and SDS-PAGE. Scatchard analysis of a fluorescence titration shows that the apoprotein possess one binding site, and at 30В°C the KdS (?M) are as follows: 6,7-dimethyl-8-ribityllumazine, 0.26; riboflavin, 0.53; and much more weakly bound FMN, 30. All holoproteins are highly fluorescent and have absorption spectra distinct from each other and from the free ligands. The longest wavelength absorption maxima are, respectively (nm, 2В°C), 420,463, and 458. Ligand binding produces no change in the far-UV circular dichroism; all have mean residual ellipticity at 210 nm of -6500 deg cm2 dmol-1, the same as the native protein. However, in the bioluminescence reaction only the lumazine holoprotein shows a bioluminescence effect. Fluorescence emission anisotropy decay was used to establish that none of these holoproteins complexed with native luciferase and that the lumazine protein alone formed a 1:1 complex with the luciferase hydroxyflavin fluorescent transient and the luciferase peroxyflavin intermediates, revealed by a dominant channel of anisotropy loss, with rotational correlation time of 2.5 ns, and attributed to excitation transfer from the luciferase flavin donor to the acceptor, the lumazine ligand. The complex stability was sufficient to allow its isolation by FPLC gel filtration and verification by SDS-PAGE. These methods also confirmed the absence of interaction of the holoflavoproteins.
Scopus
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8.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Lee J.
Заглавие : Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1
Место публикации : European Journal of Biochemistry. - 1997. - Vol. 245, Is. 3. - С. 790-796. - ISSN 00142956 (ISSN)
Ключевые слова (''Своб.индексиров.''): anisotropy--lumazine protein--photobacterium--thioredoxin reductase--time-resolved fluorescence--cytochrome--flavoprotein--article--bioluminescence--nonhuman--priority journal--protein analysis--protein purification--sea--vibrio--amino acid sequence--bacterial proteins--cytochromes--flavoproteins--molecular sequence data--sequence alignment--vibrio--azotobacter--bacteria (microorganisms)--escherichia coli--haemophilus--haemophilus influenza--murinae--negibacteria--photobacterium--photobacterium leiognathi--pseudomonas--uncultured marine bacterium--vibrio fischeri
Аннотация: Several flavoproteins and cytochromes that occur as major components in extracts of the yellow bioluminescence Y1 strain of the murine bacterium Vibrio fischeri have been purified and characterized with respect to their mass (SDS/PAGE) and matrix-assisted laser-desorption/ionization MS), chromatographic properties, N-terminal sequence, and spectroscopy (absorption, fluorescence emission and anisotropy decay). The investigated proteins were as follows: yellow fluorescence protein (YFP) with bound riboflavin, FMN or 6,7-dimethyl-8-ribityllumazine; a blue fluorescence protein (BFP) with bound 6,7-dimethyl-8-ribityllumazine, riboflavin, or 6- methyl-7-oxo-ribityllumazine; thioredoxin reductase with FAD as ligand; and two c-type diheme cytochromes, c551 and c554. We present evidence that the riboflavin-bound YFP has an N-terminal sequence corresponding to that published for the dimeric YFP. We show that an equilibrium replacement of the riboflavin can be made with excess lumazine derivative and that lumazine- bound YFP has different bioluminescence properties to those of the lumazine protein from Photobacterium leiognathi. BFP is a different protein again, and in the bacterial lysate it occurs in multiple forms, ligated to either riboflavin, lumazine, or t he 7-oxolumazine derivative. The N-terminal sequence for BFP-shows similarities to those of the YFP proteins and to lumazine protein and riboflavin synthase from Photobacterium. BFP in any form has no bioluminescence or riboflavin-synthase activity. A 70-kDa fluorescent flavoprotein with FAD as ligand has an N-terminal sequence highly similar to those of thioredoxin reductases from Haemophilus influenza and Escherichia coli. Cytochrome contaminations in previous preparations of YFP have been removed and an identified as the two c-type cytochromes c551 and c554. Both inhibit the NADH-induced bioluminescence in the reductase/luciferase system with the luciferase from P. leiognathi and V. fischeri. The N-terminal amino acid sequence of the cytochrome (c551) corresponds to a diheme cytochrome c4. The spectral properties of c554 are similar to those of other c5 cytochromes, and both c554 and c551 have absorption spectra similar to those of the respective cytochromes from the gram-negative bacteria Pseudomonas and Azotobacter.
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9.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Gibson B.G., Lee J...
Заглавие : Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1
Колич.характеристики :6 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 1996. - Vol. 35, Is. 25. - С. 8413-8418. - ISSN 0006-2960, DOI 10.1021/bi952691v
Примечания : Cited References: 24
Предметные рубрики: LUMAZINE PROTEIN
LUMINOUS BACTERIUM
STRAIN Y-1
BIOLUMINESCENCE
EMISSION
PURIFICATION
TRANSIENT
LIGHT
Аннотация: Time-resolved fluorescence was used to directly measure the energy transfer rate constant in the protein-protein complex involved in the yellow bioluminescence of Vibrio fischeri, strain Y1. In this reaction the putative donor is the fluorescent transient intermediate, luciferase hydroxyflavin, which exhibits a major fluorescence lifetime of the bound flavin of 10 ns. On addition of the acceptor, the V. fischeri yellow fluorescence protein containing either FMN or riboflavin as ligand, a rapid decay time, 0.25 ns, becomes predominant. The same results are observed using rec-luciferase from Photobacterium leiognathi to produce the donor. Because of favorable spectral separation in this system, this rapid decay rate of 4 ns(-1), can be directly equated to the energy transfer rate. This rate is ten times higher than the rate previously observed in the Photobacterium luciferase hydroxyflavin-lumazine protein, donor-acceptor system, derived from emission anisotropy measurements. This ten-times ratio is close to the ratio of spectral overlaps of the donor fluorescence with the acceptor absorption, between these two systems, so it is concluded that the topology of the protein complexes in both cases, must be very similar. Energy transfer is also monitored by the loss of steady-state fluorescence intensity at 460 nm of the donor, on addition of the acceptor protein. A fluorescence titration indicates that luciferase hydroxyflavin and the yellow protein complex with a 1:1 stoichiometry with a K-d of 0.7 mu M (0 degrees C). These parameters account for the bioluminescence spectral shifting effects observed in these reactions.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petrushkov V.N., Gibson B.G., Visser AJWG, Lee J...
Заглавие : Purification and ligand exchange protocols for antenna proteins from bioluminescent bacteria
Колич.характеристики :17 с
Место публикации : Methods Enzymol.: ACADEMIC PRESS INC, 2000. - Vol. 305. - P164-180. - ISSN 0076-6879
Примечания : Cited References: 18
Предметные рубрики: YELLOW FLUORESCENT PROTEIN
FISCHERI STRAIN Y-1
AMINO-ACID-SEQUENCE
VIBRIO-FISCHERI
PHOTOBACTERIUM-LEIOGNATHI
RIBOFLAVIN PROTEIN
LUMINOUS BACTERIUM
LUMAZINE PROTEIN
FMN
Y1
WOS
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova L. P., Stepanyuk G. A., Eremeeva E. V., Vysotski E. S.
Заглавие : Role of certain amino acid residues of the coelenterazine-binding cavity in bioluminescence of light-sensitive Ca2+-regulated photoprotein berovin
Место публикации : Photochem. Photobiol. Sci. - 2016. - Vol. 15, Is. 5. - С. 691-704. - ISSN 1474905X (ISSN) , DOI 10.1039/c6pp00050a
Аннотация: Bright bioluminescence of ctenophores is caused by Ca2+-regulated photoproteins. Although these photoproteins are functionally identical to and share many properties of cnidarian photoproteins, like aequorin and obelin, and retain the same spatial architecture, they are extremely sensitive to light, i.e. lose the ability to bioluminesce on exposure to light over the entire absorption spectrum. In addition, the degree of identity of their amino acid sequences with those of cnidarian photoproteins is only 29.4%. This suggests that the residues involved in bioluminescence of ctenophore and cnidarian photoproteins significantly differ. Here we describe the bioluminescent properties of berovin mutants with substitution of the residues located in the photoprotein internal cavity. Since the spatial structure of berovin bound with a substrate is not determined yet, to identify these residues we have modeled it with an accommodated substrate using the structures of some cnidarian Ca2+-regulated photoproteins with bound coelenterazine or coelenteramide as templates in order to obtain an adequate sampling and to take into account all possible conformers and variants for ligand-protein docking. Based on the impact of substitutions on the bioluminescent properties and model structures we speculate that within the internal cavity of ctenophore photoproteins, coelenterazine is bound as a 2-peroxy anion adduct which is stabilized owing to Coulomb interaction with a positively charged guanidinium group of Arg41 paired with Tyr204. In this case, the bioluminescence reaction is triggered by only calcium-induced conformational changes leading to the disturbance of charge-charge interaction. © 2016 The Royal Society of Chemistry and Owner Societies.
Scopus,
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WOS
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Zhou, Yali, Daver, Henrik, Trapkov, Boris, Wu, Lijie, Wu, Meng, Harpsoe, Kasper, Gentry, Patrick R., Liu, Kaiwen, Larionova, Marina, Liu, Junlin, Chen, N.a., Brauner-Osborne, Hans, Gloriam, David E., Hua, Tian, Liu, Zhi-Jie
Заглавие : Molecular insights into ligand recognition and G protein coupling of the neuromodulatory orphan receptor GPR139
Колич.характеристики :4 с
Коллективы : CAS Strategic Priority Research Program [XDB37030104]; National Science Fund for Distinguished Young ScholarsNational Natural Science Foundation of China (NSFC)National Science Fund for Distinguished Young Scholars [32022038]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31930060, 31870744]; Shanghai Rising-Star Program [20QA1406500]; Lundbeck FoundationLundbeckfonden [R355-2020-949, R163-2013-16327]; Novo Nordisk FoundationNovo Nordisk FoundationNovocure Limited [NNF18OC0031226]; Independent Research Fund Denmark | Natural Sciences [8021-00173B]; Carlsberg FoundationCarlsberg Foundation [CF20-0248]
Место публикации : Cell Res.: SPRINGERNATURE, 2021. - Article in press. - ISSN 1001-0602, DOI 10.1038/s41422-021-00591-w. - ISSN 1748-7838(eISSN)
Примечания : Cited References:16. - This work was supported by the CAS Strategic Priority Research Program XDB37030104 (Z.-J.L.), the National Science Fund for Distinguished Young Scholars 32022038 (T.H.), the National Natural Science Foundation of China grants 31930060 (Z.-J.L.) and 31870744 (T.H.), and the Shanghai Rising-Star Program 20QA1406500 (T. H.), the Lundbeck Foundation R163-2013-16327 (D.E.G.), the Novo Nordisk Foundation NNF18OC0031226 (D.E.G.) and Independent Research Fund Denmark | Natural Sciences 8021-00173B (D.E.G.), the Lundbeck Foundation R355-2020-949 (B.T.) and the Carlsberg Foundation CF20-0248 (H.B.-O.). D.E.G. is a member of the Integrative Structural Biology at the University of Copenhagen (ISBUC). The cryo-EM data were collected at the Bio-Electron Microscopy Facility, ShanghaiTech University, with the assistance of Q.-Q. Sun, D.-D. Liu, Z.-H. Zhang and Y.-H. Liu. We thank the Assay Core, the assistance of F.-F. Zhou and Q.-W. Tan and the Cell Expression, Cloning and Purification Core Facilities of iHuman Institute for their support.
Предметные рубрики: DISCOVERY
PEPTIDES
ALPHA
WOS
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