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Article ; Online: Parallel transmission in a synthetic nerve.

Hoskin, Charlotte E G / Schild, Vanessa Restrepo / Vinals, Javier / Bayley, Hagan

2022 Volume 14, Issue 6, Page(s) 650–657

Abstract: Bioelectronic devices that are tetherless and soft are promising developments in medicine, robotics and chemical computing. Here, we describe bioinspired synthetic neurons, composed entirely of soft, flexible biomaterials, capable of rapid ... ...

Abstract	Bioelectronic devices that are tetherless and soft are promising developments in medicine, robotics and chemical computing. Here, we describe bioinspired synthetic neurons, composed entirely of soft, flexible biomaterials, capable of rapid electrochemical signal transmission over centimetre distances. Like natural cells, our synthetic neurons release neurotransmitters from their terminals, which initiate downstream reactions. The components of the neurons are nanolitre aqueous droplets and hydrogel fibres, connected through lipid bilayers. Transmission is powered at these interfaces by light-driven proton pumps and mediated by ion-conducting protein pores. By bundling multiple neurons into a synthetic nerve, we have shown that distinct signals can propagate simultaneously along parallel axons, thereby transmitting spatiotemporal information. Synthetic nerves might play roles in next-generation implants, soft machines and computing devices.
MeSH term(s)	Hydrogels ; Lipid Bilayers ; Neurons ; Robotics ; Water
Chemical Substances	Hydrogels ; Lipid Bilayers ; Water (059QF0KO0R)
Language	English
Publishing date	2022-04-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2464596-5
ISSN	1755-4349 ; 1755-4330
ISSN (online)	1755-4349
ISSN	1755-4330
DOI	10.1038/s41557-022-00916-1
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Article ; Online: Structure and RAF family kinase isoform selectivity of type II RAF inhibitors tovorafenib and naporafenib.

Tkacik, Emre / Li, Kunhua / Gonzalez-Del Pino, Gonzalo / Ha, Byung Hak / Vinals, Javier / Park, Eunyoung / Beyett, Tyler S / Eck, Michael J

The Journal of biological chemistry

2023 Volume 299, Issue 5, Page(s) 104634

Abstract: Upon activation by RAS, RAF family kinases initiate signaling through the MAP kinase cascade to control cell growth, proliferation, and differentiation. Among RAF isoforms (ARAF, BRAF, and CRAF), oncogenic mutations are by far most frequent in BRAF. The ... ...

Abstract	Upon activation by RAS, RAF family kinases initiate signaling through the MAP kinase cascade to control cell growth, proliferation, and differentiation. Among RAF isoforms (ARAF, BRAF, and CRAF), oncogenic mutations are by far most frequent in BRAF. The BRAF
MeSH term(s)	Humans ; Cell Line, Tumor ; Crystallography, X-Ray ; MAP Kinase Signaling System ; Melanoma/drug therapy ; Models, Molecular ; Molecular Structure ; Mutation ; Protein Isoforms/chemistry ; Protein Isoforms/metabolism ; Protein Kinase Inhibitors/chemistry ; Protein Kinase Inhibitors/pharmacology ; Proto-Oncogene Proteins B-raf/chemistry ; Proto-Oncogene Proteins B-raf/genetics ; Proto-Oncogene Proteins B-raf/metabolism
Chemical Substances	naporafenib (15JL80DG6H) ; Protein Isoforms ; Protein Kinase Inhibitors ; Proto-Oncogene Proteins B-raf (EC 2.7.11.1) ; tovorafenib (ZN90E4027M)
Language	English
Publishing date	2023-03-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.104634
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Article ; Online: Two states of a light-sensitive membrane protein captured at room temperature using thin-film sample mounts.

Axford, Danny / Judge, Peter J / Bada Juarez, Juan F / Kwan, Tristan O C / Birch, James / Vinals, Javier / Watts, Anthony / Moraes, Isabel

Acta crystallographica. Section D, Structural biology

2022 Volume 78, Issue Pt 1, Page(s) 52–58

Abstract: Room-temperature diffraction methods are highly desirable for dynamic studies of biological macromolecules, since they allow high-resolution structural data to be collected as proteins undergo conformational changes. For crystals grown in lipidic cubic ... ...

Abstract	Room-temperature diffraction methods are highly desirable for dynamic studies of biological macromolecules, since they allow high-resolution structural data to be collected as proteins undergo conformational changes. For crystals grown in lipidic cubic phase (LCP), an extruder is commonly used to pass a stream of microcrystals through the X-ray beam; however, the sample quantities required for this method may be difficult to produce for many membrane proteins. A more sample-efficient environment was created using two layers of low X-ray transmittance polymer films to mount crystals of the archaerhodopsin-3 (AR3) photoreceptor and room-temperature diffraction data were acquired. By using transparent and opaque polymer films, two structures, one corresponding to the desensitized, dark-adapted (DA) state and the other to the ground or light-adapted (LA) state, were solved to better than 1.9 Å resolution. All of the key structural features of AR3 were resolved, including the retinal chromophore, which is present as the 13-cis isomer in the DA state and as the all-trans isomer in the LA state. The film-sandwich sample environment enables diffraction data to be recorded at room temperature in both illuminated and dark conditions, which more closely approximate those in vivo. This simple approach is applicable to a wide range of membrane proteins crystallized in LCP and light-sensitive samples in general at synchrotron and laboratory X-ray sources.
MeSH term(s)	Archaeal Proteins ; Crystallization ; Crystallography, X-Ray ; Halorubrum/chemistry ; Isomerism ; Light ; Lipids/chemistry ; Membrane Proteins/chemistry ; Photoreceptors, Microbial ; Polymers ; Proton Pumps ; Retina/chemistry ; Temperature ; X-Ray Diffraction/methods ; X-Rays
Chemical Substances	Archaeal Proteins ; Lipids ; Membrane Proteins ; Photoreceptors, Microbial ; Polymers ; Proton Pumps ; archaerhodopsin protein, Archaea
Language	English
Publishing date	2022-01-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	2968623-4
ISSN	2059-7983 ; 0907-4449
ISSN (online)	2059-7983
ISSN	0907-4449
DOI	10.1107/S2059798321011220
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Article ; Online: Highlights from the Faraday discussion on photoinduced processes in nucleic acids and proteins.

Segarra-Martí, Javier / Ramakrishnan, Remya / Vinals, Javier / Hughes, Ashley J

Chemical communications (Cambridge, England)

2018 Volume 54, Issue 34, Page(s) 4207–4215

Language	English
Publishing date	2018-04-24
Publishing country	England
Document type	Journal Article
ZDB-ID	1472881-3
ISSN	1364-548X ; 1359-7345 ; 0009-241X
ISSN (online)	1364-548X
ISSN	1359-7345 ; 0009-241X
DOI	10.1039/c8cc90123f
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Article: Analysis of Serum Proteome after Treatment of Osteoporosis with Anabolic or Antiresorptive Drugs.

Del Real, Alvaro / Ciordia, Sergio / Sañudo, Carolina / Garcia-Ibarbia, Carmen / Roa-Bautista, Adriel / Ocejo-Viñals, Javier G / Corrales, Fernando / Riancho, Jose A

Metabolites

2022 Volume 12, Issue 5

Abstract: The aim of the study was to explore new markers in serum proteome associated with the response to antiosteoporosis drugs, namely teriparatide and denosumab. We obtained serum samples from 14 patients with osteoporosis, both at baseline and after 6 months ...

Abstract	The aim of the study was to explore new markers in serum proteome associated with the response to antiosteoporosis drugs, namely teriparatide and denosumab. We obtained serum samples from 14 patients with osteoporosis, both at baseline and after 6 months of treatment with teriparatide (n = 10) or denosumab (n = 4). Samples were analyzed by nanoliquid chromatography coupled to high-resolution mass spectrometry on a QTOF 5600 (SCIEX) apparatus. The spectrometry data were analyzed with Mascot against the UniProtKB base and then several quality-control filters were applied for the identification of peptides (false discovery rate, FDR q < 0.02) and their quantification (FDR q < 0.05). In the group treated with teriparatide, 28 proteins were identified with significant differences before and after treatment. A pathway analysis by using the Reactome database revealed significant enrichment in the Insulin Like Growth Factor 1 (IGF-I) (FDR q 4 × 10−2) and innate immune system (FDR q 2 × 10−3) pathways. Among patients treated with denosumab, we observed significant differences in the levels of 10 proteins, which were also enriched in the pathways related to the innate immune system (FDR q 3 × 10−2). These results suggest that the innate immune system may be involved in the response to antiosteoporosis drugs.
Language	English
Publishing date	2022-04-28
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2662251-8
ISSN	2218-1989
ISSN	2218-1989
DOI	10.3390/metabo12050399
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Article: A versatile approach to high-density microcrystals in lipidic cubic phase for room-temperature serial crystallography.

Journal of applied crystallography

2023 Volume 56, Issue Pt 5, Page(s) 1361–1370

Abstract: Serial crystallography has emerged as an important tool for structural studies of integral membrane proteins. The ability to collect data from micrometre-sized weakly diffracting crystals at room temperature with minimal radiation damage has opened many ... ...

Abstract	Serial crystallography has emerged as an important tool for structural studies of integral membrane proteins. The ability to collect data from micrometre-sized weakly diffracting crystals at room temperature with minimal radiation damage has opened many new opportunities in time-resolved studies and drug discovery. However, the production of integral membrane protein microcrystals in lipidic cubic phase at the desired crystal density and quantity is challenging. This paper introduces VIALS (versatile approach to high-density microcrystals in lipidic cubic phase for serial crystallography), a simple, fast and efficient method for preparing hundreds of microlitres of high-density microcrystals suitable for serial X-ray diffraction experiments at both synchrotron and free-electron laser sources. The method is also of great benefit for rational structure-based drug design as it facilitates
Language	English
Publishing date	2023-08-18
Publishing country	United States
Document type	Journal Article
ZDB-ID	2020879-0
ISSN	1600-5767 ; 0021-8898
ISSN (online)	1600-5767
ISSN	0021-8898
DOI	10.1107/S1600576723006428
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Article ; Online: Detergent-free Lipodisq Nanoparticles Facilitate High-Resolution Mass Spectrometry of Folded Integral Membrane Proteins.

Hoi, Kin Kuan / Bada Juarez, Juan Francisco / Judge, Peter J / Yen, Hsin-Yung / Wu, Di / Vinals, Javier / Taylor, Garrick F / Watts, Anthony / Robinson, Carol V

Nano letters

2021 Volume 21, Issue 7, Page(s) 2824–2831

Abstract: Integral membrane proteins pose considerable challenges to mass spectrometry (MS) owing to the complexity and diversity of the components in their native environment. Here, we use native MS to study the post-translational maturation of bacteriorhodopsin ( ...

Abstract	Integral membrane proteins pose considerable challenges to mass spectrometry (MS) owing to the complexity and diversity of the components in their native environment. Here, we use native MS to study the post-translational maturation of bacteriorhodopsin (bR) and archaerhodopsin-3 (AR3), using both octyl-glucoside detergent micelles and lipid-based nanoparticles. A lower collision energy was required to obtain well-resolved spectra for proteins in styrene-maleic acid copolymer (SMA) Lipodisqs than in membrane scaffold protein (MSP) Nanodiscs. By comparing spectra of membrane proteins prepared using the different membrane mimetics, we found that SMA may favor selective solubilization of correctly folded proteins and better preserve native lipid interactions than other membrane mimetics. Our spectra reveal the correlation between the post-translation modifications (PTMs), lipid-interactions, and protein-folding states of bR, providing insights into the process of maturation of the photoreceptor proteins.
MeSH term(s)	Lipid Bilayers ; Lipids ; Mass Spectrometry ; Membrane Proteins ; Micelles ; Nanoparticles
Chemical Substances	Lipid Bilayers ; Lipids ; Membrane Proteins ; Micelles
Language	English
Publishing date	2021-03-31
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1530-6992
ISSN (online)	1530-6992
DOI	10.1021/acs.nanolett.0c04911
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Article ; Online: Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization.

Bada Juarez, Juan F / Judge, Peter J / Adam, Suliman / Axford, Danny / Vinals, Javier / Birch, James / Kwan, Tristan O C / Hoi, Kin Kuan / Yen, Hsin-Yung / Vial, Anthony / Milhiet, Pierre-Emmanuel / Robinson, Carol V / Schapiro, Igor / Moraes, Isabel / Watts, Anthony

Nature communications

2021 Volume 12, Issue 1, Page(s) 629

Abstract: Many transmembrane receptors have a desensitized state, in which they are unable to respond to external stimuli. The family of microbial rhodopsin proteins includes one such group of receptors, whose inactive or dark-adapted (DA) state is established in ... ...

Abstract	Many transmembrane receptors have a desensitized state, in which they are unable to respond to external stimuli. The family of microbial rhodopsin proteins includes one such group of receptors, whose inactive or dark-adapted (DA) state is established in the prolonged absence of light. Here, we present high-resolution crystal structures of the ground (light-adapted) and DA states of Archaerhodopsin-3 (AR3), solved to 1.1 Å and 1.3 Å resolution respectively. We observe significant differences between the two states in the dynamics of water molecules that are coupled via H-bonds to the retinal Schiff Base. Supporting QM/MM calculations reveal how the DA state permits a thermodynamic equilibrium between retinal isomers to be established, and how this same change is prevented in the ground state in the absence of light. We suggest that the different arrangement of internal water networks in AR3 is responsible for the faster photocycle kinetics compared to homologs.
MeSH term(s)	Archaeal Proteins/metabolism ; Crystallography, X-Ray ; Electrons ; Hydrogen Bonding ; Isomerism ; Lipids/chemistry ; Membrane Transport Proteins/chemistry ; Membrane Transport Proteins/metabolism ; Molecular Conformation ; Protein Processing, Post-Translational ; Protons ; Retinaldehyde/chemistry ; Retinaldehyde/metabolism ; Water/chemistry
Chemical Substances	Archaeal Proteins ; Lipids ; Membrane Transport Proteins ; Protons ; archaerhodopsin protein, Archaea ; Water (059QF0KO0R) ; Retinaldehyde (RR725D715M)
Language	English
Publishing date	2021-01-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-020-20596-0
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Article ; Online: Comparison of the anti-inflammatory effect of aripiprazole and risperidone in 75 drug-naïve first episode psychosis individuals: A 3 months randomized study.

Juncal-Ruiz, María / Riesco-Dávila, Laura / Ortiz-García de la Foz, Víctor / Martínez-Garcia, Obdulia / Ramírez-Bonilla, Mariluz / Ocejo-Viñals, Javier Gonzalo / Leza, Juan Carlos / López-Hoyos, Marcos / Crespo-Facorro, Benedicto

Schizophrenia research

2018 Volume 202, Page(s) 226–233

Abstract: Introduction: Evidence about the anti-inflammatory properties of antipsychotics has grown. However, no previous studies have compared the immunomodulatory effect of risperidone and aripiprazole.: Objectives: The main aim of the present work is to ... ...

Abstract	Introduction: Evidence about the anti-inflammatory properties of antipsychotics has grown. However, no previous studies have compared the immunomodulatory effect of risperidone and aripiprazole. Objectives: The main aim of the present work is to compare the anti-inflammatory effect of risperidone and aripiprazole on a large array of serum cytokines at 3 months following the onset of treatment. Methods: This is a prospective, randomized, open-label study. Patients were randomly assigned to risperidone or aripiprazole. From this randomization, 75 patients and 75 healthy volunteers that matched with the selected patients were picked for entry in this study. Serum concentrations of 21 cytokines/chemokines were measured at baseline and 3 months following the initiation of antipsychotic medication. Results: Those patients who were randomly assigned to risperidone had higher levels of IL-8 (p = 0.000) and MIP-1β (p = 0.007) than healthy volunteers at baseline, whereas no differences were found between patients initially assigned to aripiprazole and healthy volunteers. Three months following the onset of medication several cytokines decreased significantly: IL-8, MIP-1β, Fractalkine, TNF-α, IL-7, IL-13, IL-17α, IL-23, IL-21 (all ps < 0.01). No differences were found in the percentages of change between both treatments. The effect size of the two antipsychotics was similar, except for TNF-α, IL-13, IL-17α and Fractalkine, in which aripiprazole seems to have a greater effect size than risperidone, whereas risperidone seems to have a greater effect size than aripiprazole on MIP-1β. Conclusions: This is the first study that has compared the immunomodulatory effect of risperidone and aripiprazole, finding that the anti-inflammatory effect of both treatments was similar.
MeSH term(s)	Adult ; Anti-Inflammatory Agents/therapeutic use ; Antipsychotic Agents/therapeutic use ; Aripiprazole/therapeutic use ; Biomarkers/blood ; Cytokines/blood ; Female ; Humans ; Longitudinal Studies ; Male ; Psychotic Disorders/blood ; Psychotic Disorders/drug therapy ; Psychotic Disorders/immunology ; Risperidone/therapeutic use ; Treatment Outcome
Chemical Substances	Anti-Inflammatory Agents ; Antipsychotic Agents ; Biomarkers ; Cytokines ; Aripiprazole (82VFR53I78) ; Risperidone (L6UH7ZF8HC)
Language	English
Publishing date	2018-06-23
Publishing country	Netherlands
Document type	Comparative Study ; Journal Article ; Randomized Controlled Trial ; Research Support, Non-U.S. Gov't
ZDB-ID	639422-x
ISSN	1573-2509 ; 0920-9964
ISSN (online)	1573-2509
ISSN	0920-9964
DOI	10.1016/j.schres.2018.06.039
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Zs.A 2351: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Protein-templated gold nanoparticle synthesis: protein organization, controlled gold sequestration, and unexpected reaction products.

Dalton transactions (Cambridge, England : 2003)

2017 Volume 46, Issue 47, Page(s) 16465–16473

Abstract: Emerging applications that exploit the properties of nanoparticles for biotechnology require that the nanoparticles be biocompatible or support biological recognition. These types of particles can be produced through syntheses that involve biologically ... ...

Abstract	Emerging applications that exploit the properties of nanoparticles for biotechnology require that the nanoparticles be biocompatible or support biological recognition. These types of particles can be produced through syntheses that involve biologically relevant molecules (proteins or natural extracts, for example). Many of the protocols that rely on these molecules are performed without a clear understanding of the mechanism by which the materials are produced. We have investigated a previously described reaction in which gold nanoparticles are produced from the reaction of chloroauric acid and proteins in solution. We find that modifications to the starting conditions can alter the product from the expected solution-suspended colloids to a product where colloids are formed within a solid, fibrous protein structure. We have interrogated this synthesis, exploiting the change in products to better understand this reaction. We have evaluated the kinetics and products for 7 different proteins over a range of concentrations and temperatures. The key factor that controls the synthetic outcome (colloid or fiber) is the concentration of the protein relative to the gold concentration. We find that the observed fibrous structures are more likely to form at low protein concentrations and when hydrophilic proteins are used. An analysis of the reaction kinetics shows that AuNP formation occurs faster at lower protein (fiber-forming) concentrations than at higher protein (colloid-forming) concentrations. These results contradict traditional expectations for reaction kinetics and protein-fiber formation and are instructive of the manner in which proteins template gold nanoparticle production.
MeSH term(s)	Animals ; Chemistry Techniques, Synthetic ; Gold/chemistry ; Kinetics ; Metal Nanoparticles/chemistry ; Nanotechnology/methods ; Proteins/chemistry
Chemical Substances	Proteins ; Gold (7440-57-5)
Language	English
Publishing date	2017-12-21
Publishing country	England
Document type	Journal Article
ZDB-ID	1472887-4
ISSN	1477-9234 ; 1364-5447 ; 0300-9246 ; 1477-9226
ISSN (online)	1477-9234 ; 1364-5447
ISSN	0300-9246 ; 1477-9226
DOI	10.1039/c7dt03275g
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