Borja Ibarra

Dr. Borja Ibarra


Research Focus & Metrics

Academic Career Length

27Years (2000-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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7 May 2004 in Proceedings of the National Academy of Sciences
Verified
Journal Article
Closed access
PDF file
III. L. Ivanovska
I. L. Ivanovska
PAPedro Pablo Cardenas Alzate
Pedro Pablo Cardenas Alzate
BIBorja Ibarra
Borja Ibarra
GSG. Sgalari
G. Sgalari
FMF. C. MacKintosh
F. C. MacKintosh
GWG. J. L. Wuite
G. J. L. Wuite
The shell of bacteriophages protects the viral DNA during host-to-host transfer and serves as a high-pressure container storing energy for DNA injection into a host bacterium. Here, we probe the mechanical properties of nanometer-sized bacteriophage φ29 shells by applying point forces. We show that empty shells withstand nanonewton forces while being indented up to 30% of their height. The elastic response varies across the surface, reflecting the arrangement of shell proteins. The measured Young's modulus (≈1.8 GPa) is comparable with that of hard plastic. We also observe fatigue and breakage of capsids after probing them repetitively. These results illustrate the mechanoprotection that viral shells provide and also suggest design principles for nanotechnology.

1 January 2002 in Journal of Molecular Biology
Verified
Journal Article
Closed access
AGAlicia Guasch
Alicia Guasch
JPJoan Pous
Joan Pous
BIBorja Ibarra
Borja Ibarra
FGF. Xavier Gomis-Rüth
F. Xavier Gomis-Rüth
José M. ValpuestaJosé M. Valpuesta
José M. Valpuesta
MCMiquel Coll
Miquel Coll

6 August 2009 in The EMBO Journal
Verified
Journal Article
Open access
PDF file
BIBorja Ibarra
Borja Ibarra
YCYann R Chemla
Yann R Chemla
SPSergey Plyasunov
Sergey Plyasunov
SSSteven B Smith
Steven B Smith
JLJosé M Lázaro
José M Lázaro
CBCarlos Bustamante
Carlos Bustamante
EMBO Press is an editorially independent publishing platform for the development of EMBO scientific publications.

9 May 2012 in Proceedings of the National Academy of Sciences
Verified
Journal Article
Closed access
JMJosé A. Morin
José A. Morin
FCFrancisco J. Cao-García
Francisco J. Cao-García
JLJosé M. Lázaro
José M. Lázaro
J. Ricardo Arias-GonzalezJ. Ricardo Arias-Gonzalez
J. Ricardo Arias-Gonzalez
José M. ValpuestaJosé M. Valpuesta
José M. Valpuesta
BIBorja Ibarra
Borja Ibarra
Duplication of double-stranded DNA (dsDNA) requires a fine-tuned coordination between the DNA replication and unwinding reactions. Using optical tweezers, we probed the coupling dynamics between these two activities when they are simultaneously carried out by individual Phi29 DNA polymerase molecules replicating a dsDNA hairpin. We used the wild-type and an unwinding deficient polymerase variant and found that mechanical tension applied on the DNA and the DNA sequence modulate in different ways the replication, unwinding rates, and pause kinetics of each polymerase. However, incorporation of pause kinetics in a model to quantify the unwinding reaction reveals that both polymerases destabilize the fork with the same active mechanism and offers insights into the topological strategies that could be used by the Phi29 DNA polymerase and other DNA replication systems to couple unwinding and replication reactions.

22 November 2019 in Nature Communications
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Journal Article
Open access
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JEJavier Espadas
Javier Espadas
DPDiana Pendin
Diana Pendin
RBRebeca Bocanegra
Rebeca Bocanegra
AEArtur Escalada
Artur Escalada
GMGiulia Misticoni
Giulia Misticoni
ADAndrea Daga
Andrea Daga
The endoplasmic reticulum (ER) is a continuous cell-wide membrane network. Network formation has been associated with proteins producing membrane curvature and fusion, such as reticulons and atlastin. Regulated network fragmentation, occurring in different physiological contexts, is less understood. Here we find that the ER has an embedded fragmentation mechanism based upon the ability of reticulon to produce fission of elongating network branches. In Drosophila, Rtnl1-facilitated fission is counterbalanced by atlastin-driven fusion, with the prevalence of Rtnl1 leading to ER fragmentation. Ectopic expression of Drosophila reticulon in COS-7 cells reveals individual fission events in dynamic ER tubules. Consistently, in vitro analyses show that reticulon produces velocity-dependent constriction of lipid nanotubes leading to stochastic fission via a hemifission mechanism. Fission occurs at elongation rates and pulling force ranges intrinsic to the ER, thus suggesting a principle whereby the dynamic balance between fusion and fission controlling organelle morphology depends on membrane motility.

1 May 2000 in Journal of Molecular Biology
Verified
Journal Article
Closed access
BIBorja Ibarra
Borja Ibarra
JCJose Caston
Jose Caston
ÓLÓscar Llorca
Óscar Llorca
MVMikel Valle
Mikel Valle
José M. ValpuestaJosé M. Valpuesta
José M. Valpuesta
JCJosé L Carrascosa
José L Carrascosa