---
_id: '1611'
abstract:
- lang: eng
text: Biosensors for signaling molecules allow the study of physiological processes
by bringing together the fields of protein engineering, fluorescence imaging,
and cell biology. Construction of genetically encoded biosensors generally relies
on the availability of a binding "core" that is both specific and stable,
which can then be combined with fluorescent molecules to create a sensor. However,
binding proteins with the desired properties are often not available in nature
and substantial improvement to sensors can be required, particularly with regard
to their durability. Ancestral protein reconstruction is a powerful protein-engineering
tool able to generate highly stable and functional proteins. In this work, we
sought to establish the utility of ancestral protein reconstruction to biosensor
development, beginning with the construction of an l-arginine biosensor. l-arginine,
as the immediate precursor to nitric oxide, is an important molecule in many physiological
contexts including brain function. Using a combination of ancestral reconstruction
and circular permutation, we constructed a Förster resonance energy transfer (FRET)
biosensor for l-arginine (cpFLIPR). cpFLIPR displays high sensitivity and specificity,
with a Kd of ∼14 μM and a maximal dynamic range of 35%. Importantly, cpFLIPR was
highly robust, enabling accurate l-arginine measurement at physiological temperatures.
We established that cpFLIPR is compatible with two-photon excitation fluorescence
microscopy and report l-arginine concentrations in brain tissue.
author:
- first_name: Jason
full_name: Whitfield, Jason
last_name: Whitfield
- first_name: William
full_name: Zhang, William
last_name: Zhang
- first_name: Michel
full_name: Herde, Michel
last_name: Herde
- first_name: Ben
full_name: Clifton, Ben
last_name: Clifton
- first_name: Johanna
full_name: Radziejewski, Johanna
last_name: Radziejewski
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
- first_name: Christian
full_name: Henneberger, Christian
last_name: Henneberger
- first_name: Colin
full_name: Jackson, Colin
last_name: Jackson
citation:
ama: Whitfield J, Zhang W, Herde M, et al. Construction of a robust and sensitive
arginine biosensor through ancestral protein reconstruction. Protein Science.
2015;24(9):1412-1422. doi:10.1002/pro.2721
apa: Whitfield, J., Zhang, W., Herde, M., Clifton, B., Radziejewski, J., Janovjak,
H. L., … Jackson, C. (2015). Construction of a robust and sensitive arginine biosensor
through ancestral protein reconstruction. Protein Science. Wiley. https://doi.org/10.1002/pro.2721
chicago: Whitfield, Jason, William Zhang, Michel Herde, Ben Clifton, Johanna Radziejewski,
Harald L Janovjak, Christian Henneberger, and Colin Jackson. “Construction of
a Robust and Sensitive Arginine Biosensor through Ancestral Protein Reconstruction.”
Protein Science. Wiley, 2015. https://doi.org/10.1002/pro.2721.
ieee: J. Whitfield et al., “Construction of a robust and sensitive arginine
biosensor through ancestral protein reconstruction,” Protein Science, vol.
24, no. 9. Wiley, pp. 1412–1422, 2015.
ista: Whitfield J, Zhang W, Herde M, Clifton B, Radziejewski J, Janovjak HL, Henneberger
C, Jackson C. 2015. Construction of a robust and sensitive arginine biosensor
through ancestral protein reconstruction. Protein Science. 24(9), 1412–1422.
mla: Whitfield, Jason, et al. “Construction of a Robust and Sensitive Arginine Biosensor
through Ancestral Protein Reconstruction.” Protein Science, vol. 24, no.
9, Wiley, 2015, pp. 1412–22, doi:10.1002/pro.2721.
short: J. Whitfield, W. Zhang, M. Herde, B. Clifton, J. Radziejewski, H.L. Janovjak,
C. Henneberger, C. Jackson, Protein Science 24 (2015) 1412–1422.
date_created: 2018-12-11T11:53:01Z
date_published: 2015-09-01T00:00:00Z
date_updated: 2021-01-12T06:52:00Z
day: '01'
department:
- _id: HaJa
doi: 10.1002/pro.2721
external_id:
pmid:
- '26061224'
intvolume: ' 24'
issue: '9'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4570536/
month: '09'
oa: 1
oa_version: Submitted Version
page: 1412 - 1422
pmid: 1
project:
- _id: 255BFFFA-B435-11E9-9278-68D0E5697425
grant_number: RGY0084/2012
name: In situ real-time imaging of neurotransmitter signaling using designer optical
sensors (HFSP Young Investigator)
publication: Protein Science
publication_status: published
publisher: Wiley
publist_id: '5555'
quality_controlled: '1'
scopus_import: 1
status: public
title: Construction of a robust and sensitive arginine biosensor through ancestral
protein reconstruction
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 24
year: '2015'
...
---
_id: '1867'
abstract:
- lang: eng
text: Cultured mammalian cells essential are model systems in basic biology research,
production platforms of proteins for medical use, and testbeds in synthetic biology.
Flavin cofactors, in particular flavin mononucleotide (FMN) and flavin adenine
dinucleotide (FAD), are critical for cellular redox reactions and sense light
in naturally occurring photoreceptors and optogenetic tools. Here, we quantified
flavin contents of commonly used mammalian cell lines. We first compared three
procedures for extraction of free and noncovalently protein-bound flavins and
verified extraction using fluorescence spectroscopy. For separation, two CE methods
with different BGEs were established, and detection was performed by LED-induced
fluorescence with limit of detections (LODs 0.5-3.8 nM). We found that riboflavin
(RF), FMN, and FAD contents varied significantly between cell lines. RF (3.1-14
amol/cell) and FAD (2.2-17.0 amol/cell) were the predominant flavins, while FMN
(0.46-3.4 amol/cell) was found at markedly lower levels. Observed flavin contents
agree with those previously extracted from mammalian tissues, yet reduced forms
of RF were detected that were not described previously. Quantification of flavins
in mammalian cell lines will allow a better understanding of cellular redox reactions
and optogenetic tools.
author:
- first_name: Jens
full_name: Hühner, Jens
last_name: Hühner
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Christian
full_name: Neusüß, Christian
last_name: Neusüß
- first_name: Michael
full_name: Lämmerhofer, Michael
last_name: Lämmerhofer
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
citation:
ama: Hühner J, Inglés Prieto Á, Neusüß C, Lämmerhofer M, Janovjak HL. Quantification
of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian
model cells by CE with LED-induced fluorescence detection. Electrophoresis.
2015;36(4):518-525. doi:10.1002/elps.201400451
apa: Hühner, J., Inglés Prieto, Á., Neusüß, C., Lämmerhofer, M., & Janovjak,
H. L. (2015). Quantification of riboflavin, flavin mononucleotide, and flavin
adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence
detection. Electrophoresis. Wiley. https://doi.org/10.1002/elps.201400451
chicago: Hühner, Jens, Álvaro Inglés Prieto, Christian Neusüß, Michael Lämmerhofer,
and Harald L Janovjak. “Quantification of Riboflavin, Flavin Mononucleotide, and
Flavin Adenine Dinucleotide in Mammalian Model Cells by CE with LED-Induced Fluorescence
Detection.” Electrophoresis. Wiley, 2015. https://doi.org/10.1002/elps.201400451.
ieee: J. Hühner, Á. Inglés Prieto, C. Neusüß, M. Lämmerhofer, and H. L. Janovjak,
“Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide
in mammalian model cells by CE with LED-induced fluorescence detection,” Electrophoresis,
vol. 36, no. 4. Wiley, pp. 518–525, 2015.
ista: Hühner J, Inglés Prieto Á, Neusüß C, Lämmerhofer M, Janovjak HL. 2015. Quantification
of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian
model cells by CE with LED-induced fluorescence detection. Electrophoresis. 36(4),
518–525.
mla: Hühner, Jens, et al. “Quantification of Riboflavin, Flavin Mononucleotide,
and Flavin Adenine Dinucleotide in Mammalian Model Cells by CE with LED-Induced
Fluorescence Detection.” Electrophoresis, vol. 36, no. 4, Wiley, 2015,
pp. 518–25, doi:10.1002/elps.201400451.
short: J. Hühner, Á. Inglés Prieto, C. Neusüß, M. Lämmerhofer, H.L. Janovjak, Electrophoresis
36 (2015) 518–525.
date_created: 2018-12-11T11:54:26Z
date_published: 2015-02-01T00:00:00Z
date_updated: 2021-01-12T06:53:43Z
day: '01'
department:
- _id: HaJa
doi: 10.1002/elps.201400451
ec_funded: 1
intvolume: ' 36'
issue: '4'
language:
- iso: eng
month: '02'
oa_version: None
page: 518 - 525
project:
- _id: 25548C20-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '303564'
name: Microbial Ion Channels for Synthetic Neurobiology
- _id: 255BFFFA-B435-11E9-9278-68D0E5697425
grant_number: RGY0084/2012
name: In situ real-time imaging of neurotransmitter signaling using designer optical
sensors (HFSP Young Investigator)
publication: Electrophoresis
publication_status: published
publisher: Wiley
publist_id: '5230'
pubrep_id: '836'
quality_controlled: '1'
scopus_import: 1
status: public
title: Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide
in mammalian model cells by CE with LED-induced fluorescence detection
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 36
year: '2015'
...
---
_id: '1678'
abstract:
- lang: eng
text: High-throughput live-cell screens are intricate elements of systems biology
studies and drug discovery pipelines. Here, we demonstrate an optogenetics-assisted
method that avoids the need for chemical activators and reporters, reduces the
number of operational steps and increases information content in a cell-based
small-molecule screen against human protein kinases, including an orphan receptor
tyrosine kinase. This blueprint for all-optical screening can be adapted to many
drug targets and cellular processes.
acknowledgement: 'This work was supported by grants from the European Union Seventh
Framework Programme (CIG-303564 to H.J. and ERC-StG-311166 to S.M.B.N.), the Human
Frontier Science Program (RGY0084_2012 to H.J.) and the Herzfelder Foundation (to
M.G.). A.I.-P. was supported by a Ramon Areces fellowship, and E.R. by the graduate
program MolecularDrugTargets (Austrian Science Fund (FWF): W 1232) and a FemTech
fellowship (3580812 Austrian Research Promotion Agency).'
author:
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Eva
full_name: Gschaider-Reichhart, Eva
id: 3FEE232A-F248-11E8-B48F-1D18A9856A87
last_name: Gschaider-Reichhart
orcid: 0000-0002-7218-7738
- first_name: Markus
full_name: Muellner, Markus
last_name: Muellner
- first_name: Matthias
full_name: Nowak, Matthias
id: 30845DAA-F248-11E8-B48F-1D18A9856A87
last_name: Nowak
- first_name: Sebastian
full_name: Nijman, Sebastian
last_name: Nijman
- first_name: Michael
full_name: Grusch, Michael
last_name: Grusch
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
citation:
ama: Inglés Prieto Á, Gschaider-Reichhart E, Muellner M, et al. Light-assisted small-molecule
screening against protein kinases. Nature Chemical Biology. 2015;11(12):952-954.
doi:10.1038/nchembio.1933
apa: Inglés Prieto, Á., Gschaider-Reichhart, E., Muellner, M., Nowak, M., Nijman,
S., Grusch, M., & Janovjak, H. L. (2015). Light-assisted small-molecule screening
against protein kinases. Nature Chemical Biology. Nature Publishing Group.
https://doi.org/10.1038/nchembio.1933
chicago: Inglés Prieto, Álvaro, Eva Gschaider-Reichhart, Markus Muellner, Matthias
Nowak, Sebastian Nijman, Michael Grusch, and Harald L Janovjak. “Light-Assisted
Small-Molecule Screening against Protein Kinases.” Nature Chemical Biology.
Nature Publishing Group, 2015. https://doi.org/10.1038/nchembio.1933.
ieee: Á. Inglés Prieto et al., “Light-assisted small-molecule screening against
protein kinases,” Nature Chemical Biology, vol. 11, no. 12. Nature Publishing
Group, pp. 952–954, 2015.
ista: Inglés Prieto Á, Gschaider-Reichhart E, Muellner M, Nowak M, Nijman S, Grusch
M, Janovjak HL. 2015. Light-assisted small-molecule screening against protein
kinases. Nature Chemical Biology. 11(12), 952–954.
mla: Inglés Prieto, Álvaro, et al. “Light-Assisted Small-Molecule Screening against
Protein Kinases.” Nature Chemical Biology, vol. 11, no. 12, Nature Publishing
Group, 2015, pp. 952–54, doi:10.1038/nchembio.1933.
short: Á. Inglés Prieto, E. Gschaider-Reichhart, M. Muellner, M. Nowak, S. Nijman,
M. Grusch, H.L. Janovjak, Nature Chemical Biology 11 (2015) 952–954.
date_created: 2018-12-11T11:53:25Z
date_published: 2015-10-12T00:00:00Z
date_updated: 2023-09-07T12:49:09Z
day: '12'
ddc:
- '571'
department:
- _id: HaJa
- _id: LifeSc
doi: 10.1038/nchembio.1933
ec_funded: 1
file:
- access_level: open_access
checksum: e9fb251dfcb7cd209b83f17867e61321
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:10:51Z
date_updated: 2020-07-14T12:45:12Z
file_id: '4842'
file_name: IST-2017-837-v1+1_ingles-prieto.pdf
file_size: 1308364
relation: main_file
file_date_updated: 2020-07-14T12:45:12Z
has_accepted_license: '1'
intvolume: ' 11'
issue: '12'
language:
- iso: eng
month: '10'
oa: 1
oa_version: Submitted Version
page: 952 - 954
project:
- _id: 25548C20-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '303564'
name: Microbial Ion Channels for Synthetic Neurobiology
- _id: 255BFFFA-B435-11E9-9278-68D0E5697425
grant_number: RGY0084/2012
name: In situ real-time imaging of neurotransmitter signaling using designer optical
sensors (HFSP Young Investigator)
- _id: 255A6082-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: W1232-B24
name: Molecular Drug Targets
publication: Nature Chemical Biology
publication_status: published
publisher: Nature Publishing Group
publist_id: '5471'
pubrep_id: '837'
quality_controlled: '1'
related_material:
record:
- id: '418'
relation: dissertation_contains
status: public
scopus_import: 1
status: public
title: Light-assisted small-molecule screening against protein kinases
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 11
year: '2015'
...
---
_id: '1844'
abstract:
- lang: eng
text: 'Local protein interactions ("molecular context" effects) dictate
amino acid replacements and can be described in terms of site-specific, energetic
preferences for any different amino acid. It has been recently debated whether
these preferences remain approximately constant during evolution or whether, due
to coevolution of sites, they change strongly. Such research highlights an unresolved
and fundamental issue with far-reaching implications for phylogenetic analysis
and molecular evolution modeling. Here, we take advantage of the recent availability
of phenotypically supported laboratory resurrections of Precambrian thioredoxins
and β-lactamases to experimentally address the change of site-specific amino acid
preferences over long geological timescales. Extensive mutational analyses support
the notion that evolutionary adjustment to a new amino acid may occur, but to
a large extent this is insufficient to erase the primitive preference for amino
acid replacements. Generally, site-specific amino acid preferences appear to remain
conserved throughout evolutionary history despite local sequence divergence. We
show such preference conservation to be readily understandable in molecular terms
and we provide crystallographic evidence for an intriguing structural-switch mechanism:
Energetic preference for an ancestral amino acid in a modern protein can be linked
to reorganization upon mutation to the ancestral local structure around the mutated
site. Finally, we point out that site-specific preference conservation naturally
leads to one plausible evolutionary explanation for the existence of intragenic
global suppressor mutations.'
author:
- first_name: Valeria
full_name: Risso, Valeria
last_name: Risso
- first_name: Fadia
full_name: Manssour Triedo, Fadia
last_name: Manssour Triedo
- first_name: Asuncion
full_name: Delgado Delgado, Asuncion
last_name: Delgado Delgado
- first_name: Rocio
full_name: Arco, Rocio
last_name: Arco
- first_name: Alicia
full_name: Barroso Deljesús, Alicia
last_name: Barroso Deljesús
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Raquel
full_name: Godoy Ruiz, Raquel
last_name: Godoy Ruiz
- first_name: Josè
full_name: Gavira, Josè
last_name: Gavira
- first_name: Eric
full_name: Gaucher, Eric
last_name: Gaucher
- first_name: Beatriz
full_name: Ibarra Molero, Beatriz
last_name: Ibarra Molero
- first_name: Jose
full_name: Sánchez Ruiz, Jose
last_name: Sánchez Ruiz
citation:
ama: Risso V, Manssour Triedo F, Delgado Delgado A, et al. Mutational studies on
resurrected ancestral proteins reveal conservation of site-specific amino acid
preferences throughout evolutionary history. Molecular Biology and Evolution.
2014;32(2):440-455. doi:10.1093/molbev/msu312
apa: Risso, V., Manssour Triedo, F., Delgado Delgado, A., Arco, R., Barroso Deljesús,
A., Inglés Prieto, Á., … Sánchez Ruiz, J. (2014). Mutational studies on resurrected
ancestral proteins reveal conservation of site-specific amino acid preferences
throughout evolutionary history. Molecular Biology and Evolution. Oxford
University Press. https://doi.org/10.1093/molbev/msu312
chicago: Risso, Valeria, Fadia Manssour Triedo, Asuncion Delgado Delgado, Rocio
Arco, Alicia Barroso Deljesús, Álvaro Inglés Prieto, Raquel Godoy Ruiz, et al.
“Mutational Studies on Resurrected Ancestral Proteins Reveal Conservation of Site-Specific
Amino Acid Preferences throughout Evolutionary History.” Molecular Biology
and Evolution. Oxford University Press, 2014. https://doi.org/10.1093/molbev/msu312.
ieee: V. Risso et al., “Mutational studies on resurrected ancestral proteins
reveal conservation of site-specific amino acid preferences throughout evolutionary
history,” Molecular Biology and Evolution, vol. 32, no. 2. Oxford University
Press, pp. 440–455, 2014.
ista: Risso V, Manssour Triedo F, Delgado Delgado A, Arco R, Barroso Deljesús A,
Inglés Prieto Á, Godoy Ruiz R, Gavira J, Gaucher E, Ibarra Molero B, Sánchez Ruiz
J. 2014. Mutational studies on resurrected ancestral proteins reveal conservation
of site-specific amino acid preferences throughout evolutionary history. Molecular
Biology and Evolution. 32(2), 440–455.
mla: Risso, Valeria, et al. “Mutational Studies on Resurrected Ancestral Proteins
Reveal Conservation of Site-Specific Amino Acid Preferences throughout Evolutionary
History.” Molecular Biology and Evolution, vol. 32, no. 2, Oxford University
Press, 2014, pp. 440–55, doi:10.1093/molbev/msu312.
short: V. Risso, F. Manssour Triedo, A. Delgado Delgado, R. Arco, A. Barroso Deljesús,
Á. Inglés Prieto, R. Godoy Ruiz, J. Gavira, E. Gaucher, B. Ibarra Molero, J. Sánchez
Ruiz, Molecular Biology and Evolution 32 (2014) 440–455.
date_created: 2018-12-11T11:54:19Z
date_published: 2014-11-12T00:00:00Z
date_updated: 2021-01-12T06:53:34Z
day: '12'
ddc:
- '571'
department:
- _id: HaJa
doi: 10.1093/molbev/msu312
file:
- access_level: open_access
checksum: 06215318e66be8f3e0c33abb07e9d3da
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:16:56Z
date_updated: 2020-07-14T12:45:19Z
file_id: '5247'
file_name: IST-2016-430-v1+1_Mol_Biol_Evol-2015-Risso-440-55.pdf
file_size: 1545246
relation: main_file
file_date_updated: 2020-07-14T12:45:19Z
has_accepted_license: '1'
intvolume: ' 32'
issue: '2'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '11'
oa: 1
oa_version: Published Version
page: 440 - 455
publication: Molecular Biology and Evolution
publication_status: published
publisher: Oxford University Press
publist_id: '5257'
pubrep_id: '430'
quality_controlled: '1'
scopus_import: 1
status: public
title: Mutational studies on resurrected ancestral proteins reveal conservation of
site-specific amino acid preferences throughout evolutionary history
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 4435EBFC-F248-11E8-B48F-1D18A9856A87
volume: 32
year: '2014'
...
---
_id: '2032'
abstract:
- lang: eng
text: As light-based control of fundamental signaling pathways is becoming a reality,
the field of optogenetics is rapidly moving beyond neuroscience. We have recently
developed receptor tyrosine kinases that are activated by light and control cell
proliferation, epithelial–mesenchymal transition, and angiogenic sprouting—cell
behaviors central to cancer progression.
article_number: e964045
author:
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Eva
full_name: Gschaider-Reichhart, Eva
id: 3FEE232A-F248-11E8-B48F-1D18A9856A87
last_name: Gschaider-Reichhart
orcid: 0000-0002-7218-7738
- first_name: Karin
full_name: Schelch, Karin
last_name: Schelch
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
- first_name: Michael
full_name: Grusch, Michael
last_name: Grusch
citation:
ama: 'Inglés Prieto Á, Gschaider-Reichhart E, Schelch K, Janovjak HL, Grusch M.
The optogenetic promise for oncology: Episode I. Molecular and Cellular Oncology.
2014;1(4). doi:10.4161/23723548.2014.964045'
apa: 'Inglés Prieto, Á., Gschaider-Reichhart, E., Schelch, K., Janovjak, H. L.,
& Grusch, M. (2014). The optogenetic promise for oncology: Episode I. Molecular
and Cellular Oncology. Taylor & Francis. https://doi.org/10.4161/23723548.2014.964045'
chicago: 'Inglés Prieto, Álvaro, Eva Gschaider-Reichhart, Karin Schelch, Harald
L Janovjak, and Michael Grusch. “The Optogenetic Promise for Oncology: Episode
I.” Molecular and Cellular Oncology. Taylor & Francis, 2014. https://doi.org/10.4161/23723548.2014.964045.'
ieee: 'Á. Inglés Prieto, E. Gschaider-Reichhart, K. Schelch, H. L. Janovjak, and
M. Grusch, “The optogenetic promise for oncology: Episode I,” Molecular and
Cellular Oncology, vol. 1, no. 4. Taylor & Francis, 2014.'
ista: 'Inglés Prieto Á, Gschaider-Reichhart E, Schelch K, Janovjak HL, Grusch M.
2014. The optogenetic promise for oncology: Episode I. Molecular and Cellular
Oncology. 1(4), e964045.'
mla: 'Inglés Prieto, Álvaro, et al. “The Optogenetic Promise for Oncology: Episode
I.” Molecular and Cellular Oncology, vol. 1, no. 4, e964045, Taylor &
Francis, 2014, doi:10.4161/23723548.2014.964045.'
short: Á. Inglés Prieto, E. Gschaider-Reichhart, K. Schelch, H.L. Janovjak, M. Grusch,
Molecular and Cellular Oncology 1 (2014).
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title: 'The optogenetic promise for oncology: Episode I'
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