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Månsson, A. (2019). Comparing models with one versus multiple myosin-binding sites per actin target zone: The power of simplicity. The Journal of General Physiology, 151(4), 578-592
Open this publication in new window or tab >>Comparing models with one versus multiple myosin-binding sites per actin target zone: The power of simplicity
2019 (English)In: The Journal of General Physiology, ISSN 0022-1295, E-ISSN 1540-7748, Vol. 151, no 4, p. 578-592Article in journal (Refereed) Published
Abstract [en]

Mechanokinetic statistical models describe the mechanisms of muscle contraction on the basis of the average behavior of a large ensemble of actin-myosin motors. Such models often assume that myosin II motor domains bind to regularly spaced, discrete target zones along the actin-based thin filaments and develop force in a series of strain-dependent transitions under the turnover of ATP. The simplest models assume that there is just one myosin-binding site per target zone and a uniform spatial distribution of the myosin motor domains in relation to each site. However, most of the recently developed models assume three myosin-binding sites per target zone, and some models include a spatially explicit 3-D treatment of the myofilament lattice and thereby of the geometry of the actin-myosin contact points. Here, I show that the predictions for steady-state contractile behavior of muscle are very similar whether one or three myosin-binding sites per target zone is assumed, provided that the model responses are appropriately scaled to the number of sites. Comparison of the model predictions for isometrically contracting mammalian muscle cells suggests that each target zone contains three or more myosin-binding sites. Finally, I discuss the strengths and weaknesses of one-site spatially inexplicit models in relation to three-site models, including those that take into account the detailed 3-D geometry of the myofilament lattice. The results of this study suggest that single-site models, with reduced computational cost compared with multisite models, are useful for several purposes, e.g., facilitated molecular mechanistic insights.

Place, publisher, year, edition, pages
Rockefeller University Press, 2019
National Category
Biophysics Biochemistry and Molecular Biology
Research subject
Chemistry, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-81840 (URN)10.1085/jgp.201812301 (DOI)000462865900017 ()30872560 (PubMedID)2-s2.0-85064199288 (Scopus ID)
Available from: 2019-04-12 Created: 2019-04-12 Last updated: 2019-08-29
Lindberg, F. W., Korten, T., Löfstrand, A., Rahman, M. A., Graczyk, M., Månsson, A., . . . Maximov, I. (2019). Design and development of nanoimprint-enabled structures for molecular motor devices. Materials Research Express, 6(2), Article ID 025057.
Open this publication in new window or tab >>Design and development of nanoimprint-enabled structures for molecular motor devices
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2019 (English)In: Materials Research Express, E-ISSN 2053-1591, Vol. 6, no 2, article id 025057Article in journal (Refereed) Published
Abstract [en]

Devices based on molecular motor-driven cytoskeletal filaments, e.g., actin filaments, have been developed both for biosensing and biocomputational applications. Commonly, these devices require nanoscaled tracks for guidance of the actin filaments which has limited the patterning technique to electron beam lithography. Thus, large scale systems become intractable to fabricate at a high throughput within a reasonable time-frame. We have studied the possibility to fabricate molecular motor-based devices using the high throughput, high resolution technique of nanoimprint lithography. Molecular motor-based devices require wide open regions (loading zones) to allow filaments to land for later propulsion into the nanoscale tracks. Such open zones are challenging to fabricate using nanoimprint lithography due to the large amount of material displaced in the process. We found that this challenge can be overcome by introducing nanoscaled pillars inside the loading zones, into which material can be displaced during imprint. By optimising the resist thickness, we were able to decrease the amount of material displaced without suffering from insufficient filling of the stamp. Furthermore, simulations suggest that the shape and positioning of the pillars can be used to tailor the overall cytoskeletal filament transportation direction and behaviour. This is a potentially promising design feature for future applications that however, requires further optimisations before experimental realisation.

Place, publisher, year, edition, pages
Institute of Physics Publishing (IOPP), 2019
Keywords
nanoimprint lithography, molecular motors, actin-myosin, nanostructures, nanofabrication, nanodevice, patterning
National Category
Biochemistry and Molecular Biology
Research subject
Chemistry, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-79598 (URN)10.1088/2053-1591/aaed10 (DOI)000452490000003 ()2-s2.0-85057713106 (Scopus ID)
Funder
EU, Horizon 2020, 732482Swedish Research Council, 2015-05290Swedish Research Council, 2015-0612Swedish Foundation for Strategic Research , RIF14-0090
Available from: 2019-01-18 Created: 2019-01-18 Last updated: 2019-08-29Bibliographically approved
Matusovsky, O. S., Månsson, A., Persson, M., Cheng, Y.-S. & Rassier, D. E. (2019). High-speed AFM reveals subsecond dynamics of cardiac thin filaments upon Ca2+ activation and heavy meromyosin binding. Proceedings of the National Academy of Sciences of the United States of America, 116(33), 16384-16393
Open this publication in new window or tab >>High-speed AFM reveals subsecond dynamics of cardiac thin filaments upon Ca2+ activation and heavy meromyosin binding
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2019 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 116, no 33, p. 16384-16393Article in journal (Refereed) Published
Abstract [en]

High-speed atomic force microscopy (HS-AFM) can be used to study dynamic processes with real-time imaging of molecules within 1- to 5-nm spatial resolution. In the current study, we evaluated the 3-state model of activation of cardiac thin filaments (cTFs) isolated as a complex and deposited on a mica-supported lipid bilayer. We studied this complex for dynamic conformational changes 1) at low and high [Ca2+] (pCa 9.0 and 4.5), and 2) upon myosin binding to the cTF in the nucleotide-free state or in the presence of ATP. HS-AFM was used to directly visualize the tropo-myosin-troponin complex and Ca2+-induced tropomyosin movements accompanied by structural transitions of actin monomers within cTFs. Our data show that cTFs at relaxing or activating conditions are not ultimately in a blocked or activated state, respectively, but rather the combination of states with a prevalence that is dependent on the [Ca2+] and the presence of weakly or strongly bound myosin. The weakly and strongly bound myosin induce similar changes in the structure of cTFs as confirmed by the local dynamical displacement of individual tropomyosin strands in the center of a regulatory unit of cTF at the relaxed and activation conditions. The displacement of tropomyosin at the relaxed conditions had never been visualized directly and explains the ability of myosin binding to TF at the relaxed conditions. Based on the ratios of nonactivated and activated segments within cTFs, we proposed a mechanism of tropomyosin switching from different states that includes both weakly and strongly bound myosin.

Place, publisher, year, edition, pages
National Academy of Sciences, 2019
Keywords
thin filaments, muscle contraction, HS-AFM
National Category
Biophysics Biochemistry and Molecular Biology
Research subject
Chemistry, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-88826 (URN)10.1073/pnas.1903228116 (DOI)000481404300041 ()31358631 (PubMedID)
Available from: 2019-08-29 Created: 2019-08-29 Last updated: 2019-08-29Bibliographically approved
Månsson, A., Persson, M., Shalabi, N. & Rassier, D. E. (2019). Nonlinear Actomyosin Elasticity in Muscle?. Biophysical Journal, 116(2), 330-346
Open this publication in new window or tab >>Nonlinear Actomyosin Elasticity in Muscle?
2019 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 116, no 2, p. 330-346Article in journal (Refereed) Published
Abstract [en]

Cyclic interactions between myosin II motor domains and actin filaments that are powered by turnover of ATP underlie muscle contraction and have key roles in motility of nonmuscle cells. The elastic characteristics of actin-myosin cross-bridges are central in the force-generating process, and disturbances in these properties may lead to disease. Although the prevailing paradigm is that the cross-bridge elasticity is linear (Hookean), recent single-molecule studies suggest otherwise. Despite convincing evidence for substantial nonlinearity of the cross-bridge elasticity in the single-molecule work, this finding has had limited influence on muscle physiology and physiology of other ordered cellular actin-myosin ensembles. Here, we use a biophysical modeling approach to close the gap between single molecules and physiology. The model is used for analysis of available experimental results in the light of possible nonlinearity of the cross-bridge elasticity. We consider results obtained both under rigor conditions (in the absence of ATP) and during active muscle contraction. Our results suggest that a wide range of experimental findings from mechanical experiments on muscle cells are consistent with nonlinear actin-myosin elasticity similar to that previously found in single molecules. Indeed, the introduction of nonlinear cross-bridge elasticity into the model improves the reproduction of key experimental results and eliminates the need for force dependence of the ATP-induced detachment rate, consistent with observations in other single-molecule studies. The findings have significant implications for the understanding of key features of actin-myosin-based production of force and motion in living cells, particularly in muscle, and for the interpretation of experimental results that rely on stiffness measurements on cells or myofibrils.

Place, publisher, year, edition, pages
Cell Press, 2019
National Category
Biophysics
Research subject
Chemistry, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-80278 (URN)10.1016/j.bpj.2018.12.004 (DOI)000456327100015 ()30606448 (PubMedID)2-s2.0-85059232890 (Scopus ID)
Available from: 2019-02-07 Created: 2019-02-07 Last updated: 2019-08-29Bibliographically approved
Danielsson, T., Schreyer, H., Woksepp, H., Johansson, T., Bergman, P., Månsson, A. & Carlsson, J. (2019). Two-peaked increase of serum myosin heavy chain-α after triathlon suggests heart muscle cell death. BMJ Open Sport & Exercise Medicine, 5, Article ID e000486.
Open this publication in new window or tab >>Two-peaked increase of serum myosin heavy chain-α after triathlon suggests heart muscle cell death
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2019 (English)In: BMJ Open Sport & Exercise Medicine, ISSN 2055-7647, Vol. 5, article id e000486Article in journal (Refereed) Published
Abstract [en]

Objective It has been suggested that the mechanism behind cardiac troponin elevation after strenuous exercise is passage through a cell membrane with changed permeability rather than myocardial cell death. We hypothesised that an increase of cardiac specific myosin heavy chain-alpha (MHC-α; 224 kDa compared with cardiac troponin T’s (cTnT) 37 kDa) could hardly be explained by passage through a cell membrane.

Methods Blood samples were collected from 56 athletes (15 female, age 42.5±9.7, range 24–70 years) before, directly after and on days 1–8 after an Ironman. Biomarkers (C reactive protein (CRP), cTnT, creatinekinase (CK), MHC-α, myoglobin (MG), creatinine (C) and N-terminal prohormone of brain natriuretic peptide (NTproBNP) were measured.

Results The course of MHC-α concentration (μg/L) was 1.33±0.53 (before), 2.57±0.78 (directly after), 1.51±0.53 (day 1), 2.74±0.55 (day 4) and 1.83±0.76 (day 6). Other biomarkers showed a one-peaked increase with maximal values either directly after the race or at day 1: cTnT 76 ±80 ng/L (12–440; reference<15), NT-proBNP 776±684 ng/L (92–4700; ref.<300), CK 68±55 μkat/L (5–280; ref.<1.9), MG 2088±2350 μg/L (130–17 000; ref.<72) and creatinine 100±20 μmol/L (74–161; ref.<100), CRP 49±23 mg/L(15–119; ref.<5).

Conclusion MHC-α exhibited a two-peaked increase which could represent a first release from the cytosolic pool and later from cell necrosis. This is the first investigation of MHC-α plasma concentration afterexercise.

Place, publisher, year, edition, pages
BMJ Publishing Group Ltd, 2019
Keywords
cardiovascular medicine, physiology, sports and exercise medicine
National Category
Sport and Fitness Sciences Cardiac and Cardiovascular Systems
Research subject
Social Sciences, Sport Science
Identifiers
urn:nbn:se:lnu:diva-79922 (URN)10.1136/ bmjsem-2018-000486 (DOI)30740234 (PubMedID)2-s2.0-85060492223 (Scopus ID)
Available from: 2019-01-25 Created: 2019-01-25 Last updated: 2019-05-23Bibliographically approved
Rahman, M. A., Ušaj, M., Rassier, D. E. & Månsson, A. (2018). Blebbistatin Effects Expose Hidden Secrets in the Force-Generating Cycle of Actin and Myosin. Paper presented at Biophysical-Society Thematic Meeting on Single-Cell Biophysics - Mearurement, Modulation, and Modeling, JUN, 2017, Natl Taiwan Univ, Acad Sinica, Inst Atom & Mol Sci, Taipei, TAIWAN. Biophysical Journal, 115(2), 386-397
Open this publication in new window or tab >>Blebbistatin Effects Expose Hidden Secrets in the Force-Generating Cycle of Actin and Myosin
2018 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 115, no 2, p. 386-397Article in journal (Refereed) Published
Abstract [en]

Cyclic interactions between myosin II motors and actin filaments driven by ATP turnover underlie muscle contraction and have key roles in the motility of nonmuscle cells. A remaining enigma in the understanding of this interaction is the relationship between the force-generating structural change and the release of the ATP-hydrolysis product, inorganic phosphate (Pi), from the active site of myosin. Here, we use the small molecular compound blebbistatin to probe otherwise hidden states and transitions in this process. Different hypotheses for the Pi release mechanism are tested by interpreting experimental results from in vitro motility assays and isolated muscle fibers in terms of mechanokinetic actomyosin models. The data fit with ideas that actomyosin force generation is preceded by Pi release, which in turn is preceded by two serial transitions after/coincident with cross-bridge attachment. Blebbistatin changes the rate limitation of the cycle from the first to the second of these transitions, uncovering functional roles of an otherwise short-lived pre-power stroke state that has been implicated by structural data.

Place, publisher, year, edition, pages
Rockville, MD: Biophysical Society, 2018
National Category
Biophysics
Research subject
Chemistry, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-77397 (URN)10.1016/j.bpj.2018.05.037 (DOI)000438958800024 ()30021113 (PubMedID)2-s2.0-85048935566 (Scopus ID)
Conference
Biophysical-Society Thematic Meeting on Single-Cell Biophysics - Mearurement, Modulation, and Modeling, JUN, 2017, Natl Taiwan Univ, Acad Sinica, Inst Atom & Mol Sci, Taipei, TAIWAN
Available from: 2018-08-29 Created: 2018-08-29 Last updated: 2019-08-29Bibliographically approved
Månsson, A. & Ušaj, M. (2018). Challenges in TIRF-Microscopy Based Single Molecule ATPase and Binding Assays for Myosin and Actin. In: Biophysical Journal Supplement 1: . Paper presented at Biophysical Society 62nd Annual Meeting, February 17-21, 2018, San Francisco. (pp. 211a-211a). , 114(3), Article ID 1062-Plat.
Open this publication in new window or tab >>Challenges in TIRF-Microscopy Based Single Molecule ATPase and Binding Assays for Myosin and Actin
2018 (English)In: Biophysical Journal Supplement 1, 2018, Vol. 114, no 3, p. 211a-211a, article id 1062-PlatConference paper, Oral presentation with published abstract (Refereed)
Abstract [en]

Total internal reflection fluorescence (TIRF) microscopy has permitted visualization of myosin and actin mechanochemistry on a single-molecule level. It has, for instance, been possible to study complex phenomena such as temporal relationship between ATP turnover and the force producing transition. However, despite quite large number of studies using fluorescent ATP analogs, several challenges remain in the interpretation of TIRF data in terms of ATP binding to the active site of myosin. We here present improvements in assay conditions for more reliable detection of ATP on-time (i.e. dwell time) at the active site(s) of myosin using approaches to suppress fluorophore blinking events related to the photophysics of the fluorescent probe. We also suggest assay designs for analysis of myosin-binding to actin filaments on a surface in the presence of nucleotide. The experiments were performed using a custom built TIRF microscopy platform and fluorescent Alexa Fluor 647 ATP (Alexa-ATP) whose turnover to Alexa Fluor 647 ADP (Alexa-ADP) and inorganic phosphate (Pi) by myosin and actomyosin occurs by a similar mechanism as for unlabeled ATP. Using this system we present solutions for improved single molecule assays for actin and myosin with emphasis on the use of reducing and oxidizing agents (trolox/trolox-quinone; TTQ) in assay buffers to suppress photo-blinking while maintaining long-lasting fluorescence signals. The cumulative frequency distribution of dwell-time events exhibited more than one exponential phase both in the presence and absence of TTQ. The relative amplitude of the slowest phase increased appreciably in the presence of TTQ as well as the overall half-time.

National Category
Biophysics
Research subject
Chemistry, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-75776 (URN)10.1016/j.bpj.2017.11.1180 (DOI)
Conference
Biophysical Society 62nd Annual Meeting, February 17-21, 2018, San Francisco.
Available from: 2018-06-14 Created: 2018-06-14 Last updated: 2018-06-15Bibliographically approved
Rahman, M. A., Salhotra, A. & Månsson, A. (2018). Comparative analysis of widely used methods to remove nonfunctional myosin heads for the in vitro motility assay. Journal of Muscle Research and Cell Motility, 39(5-6), 175-187
Open this publication in new window or tab >>Comparative analysis of widely used methods to remove nonfunctional myosin heads for the in vitro motility assay
2018 (English)In: Journal of Muscle Research and Cell Motility, ISSN 0142-4319, E-ISSN 1573-2657, Vol. 39, no 5-6, p. 175-187Article in journal (Refereed) Published
Abstract [en]

The in vitro motility assay allows studies of muscle contraction through observation of actin filament propulsion by surface-adsorbed myosin motors or motor fragments isolated from muscle. A possible problem is that motility may be compromised by nonfunctional, "dead", motors, obtained in the isolation process. Here we investigate the effects on motile function of two approaches designed to eliminate the effects of these dead motors. We first tested the removal of heavy meromyosin (HMM) molecules with ATP-insensitive "dead" heads by pelleting them with actin filaments, using ultracentrifugation in the presence of 1 mM MgATP ("affinity purification"). Alternatively we incubated motility assay flow cells, after HMM surface adsorption, with non-fluorescent "blocking actin" (1 µM) to block the dead heads. Both affinity purification and use of blocking actin increased the fraction of motile filaments compared to control conditions. However, affinity purification significantly reduced the actin sliding speed in five out of seven experiments on silanized surfaces and in one out of four experiments on nitrocellulose surfaces. Similar effects on velocity were not observed with the use of blocking actin. However, a reduced speed was also seen (without affinity purification) if HMM or myosin subfragment 1 was mixed with 1 mM MgATP before and during surface adsorption. We conclude that affinity purification can produce unexpected effects that may complicate the interpretation of in vitro motility assays and other experiments with surface adsorbed HMM, e.g. single molecule mechanics experiments. The presence of MgATP during incubation with myosin motor fragments is critical for the complicating effects.

Place, publisher, year, edition, pages
Springer, 2018
Keywords
Affinity purification, Blocking actin, Cross-bridge cycle, In vitro motility assay, Molecular motor, Myosin
National Category
Cell Biology
Research subject
Natural Science, Cell and Organism Biology
Identifiers
urn:nbn:se:lnu:diva-82905 (URN)10.1007/s10974-019-09505-1 (DOI)000466555500004 ()30850933 (PubMedID)
Available from: 2019-05-23 Created: 2019-05-23 Last updated: 2019-08-12Bibliographically approved
Lindberg, F. W., Norrby, M., Rahman, M. A., Salhotra, A., Takatsuki, H., Jeppesen, S., . . . Månsson, A. (2018). Controlled Surface Silanization for Actin-Myosin and Biocompatibility of New Polymer Resists. Langmuir, 34(30), 8777-8784
Open this publication in new window or tab >>Controlled Surface Silanization for Actin-Myosin and Biocompatibility of New Polymer Resists
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2018 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 34, no 30, p. 8777-8784Article in journal (Refereed) Published
Abstract [en]

Molecular motor-based nanodevices require organized cytoskeletal filament guiding along motility-promoting tracks, confined by motility-inhibiting walls. One way to enhance motility quality on the tracks, particularly in terms of filament velocity but also the fraction of motile filaments, is to optimize the surface hydrophobicity. We have investigated the potential to achieve this for the actin myosin II motor system on trimethylchlorosilane (TMCS)-derivatized SiO2 surfaces to be used as channel floors in nanodevices. We have also investigated the ability to supress motility on two new polymer resists, TU7 (for nanoimprint lithography) and CSAR 62 (for electron beam and deep UV lithography), to be used as channel walls. We developed a chemical-vapor deposition tool for silanizing SiO2 surfaces in a controlled environment to achieve different surface hydrophobicities (measured by water contact angle). In contrast to previous work, we were able to fabricate a wide range of contact angles by varying the silanization time and chamber pressure using only one type of silane. This resulted in a significant improvement of the silanization procedure, producing a predictable contact angle on the surface and thereby predictable quality of the heavy meromyosin (HMM)-driven actin motility with regard to velocity. We observed a high degree of correlation between the filament sliding velocity and contact angle in the range 10-86 degrees, expanding the previously studied range. We found that the sliding velocity on TU7 surfaces was superior to that on CSAR 62 surfaces despite similar contact angles. In addition, we were able to suppress the motility on both TU7 and CSAR 62 by plasma oxygen treatment before silanization. These results are discussed in relation to previously proposed surface adsorption mechanisms of HMM and their relationship to the water contact angle. Additionally, the results are considered for the development of actin-myosin based nanodevices with superior performance with respect to actin-myosin functionality.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2018
National Category
Biophysics Biochemistry and Molecular Biology
Research subject
Chemistry, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-77391 (URN)10.1021/acs.langmuir.8b01415 (DOI)000440768400007 ()29969272 (PubMedID)2-s2.0-85049637573 (Scopus ID)
Available from: 2018-08-30 Created: 2018-08-30 Last updated: 2019-08-29Bibliographically approved
Månsson, A., Ušaj, M., Moretto, L. & Rassier, D. E. (2018). Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?. International Journal of Molecular Sciences, 19(7), Article ID 1863.
Open this publication in new window or tab >>Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?
2018 (English)In: International Journal of Molecular Sciences, ISSN 1422-0067, E-ISSN 1422-0067, Vol. 19, no 7, article id 1863Article, review/survey (Refereed) Published
Abstract [en]

In muscle, but not in single-molecule mechanics studies, actin, myosin and accessory proteins are incorporated into a highly ordered myofilament lattice. In view of this difference we compare results from single-molecule studies and muscle mechanics and analyze to what degree data from the two types of studies agree with each other. There is reasonable correspondence in estimates of the cross-bridge power-stroke distance (7-13 nm), cross-bridge stiffness (similar to 2 pN/nm) and average isometric force per cross-bridge (6-9 pN). Furthermore, models defined on the basis of single-molecule mechanics and solution biochemistry give good fits to experimental data from muscle. This suggests that the ordered myofilament lattice, accessory proteins and emergent effects of the sarcomere organization have only minor modulatory roles. However, such factors may be of greater importance under e.g., disease conditions. We also identify areas where single-molecule and muscle data are conflicting: (1) whether force generation is an Eyring or Kramers process with just one major power-stroke or several sub-strokes; (2) whether the myofilaments and the cross-bridges have Hookean or non-linear elasticity; (3) if individual myosin heads slip between actin sites under certain conditions, e.g.,in lengthening; or (4) if the two heads of myosin cooperate.

Place, publisher, year, edition, pages
MDPI, 2018
Keywords
optical tweezers, optical traps, muscle fiber, myofibril, myosin, actin, cross-bridge, mechanochemical model
National Category
Biophysics Biochemistry and Molecular Biology
Research subject
Chemistry, Biochemistry
Identifiers
urn:nbn:se:lnu:diva-77732 (URN)10.3390/ijms19071863 (DOI)000442807400042 ()29941816 (PubMedID)2-s2.0-85049149996 (Scopus ID)
Available from: 2018-09-13 Created: 2018-09-13 Last updated: 2019-08-29Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0002-5889-7792

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