J. Valpuesta

发表

José-Jesús Fernández, J. Valpuesta, 2015 .

Large Terminase Conformational Change Induced by Connector Binding in Bacteriophage T7*

J. Carrascosa, J. Valpuesta, M. I. Dauden, 2013, The Journal of Biological Chemistry.

Mechanical identities of RNA and DNA double helices unveiled at the single-molecule level.

E. Herrero-Galán, J. Carrascosa, J. Valpuesta, 2013, Journal of the American Chemical Society.

Sequential Action of ATP-dependent Subunit Conformational Change and Interaction between Helical Protrusions in the Closure of the Built-in Lid of Group II Chaperonins*

K. Maki, K. Kuwajima, M. Yohda, 2008, Journal of Biological Chemistry.

Encyclopedia of life sciences

Peter Delves, William F. Bynum, Gerry Melino, 2009 .

Engineering protein assemblies with allosteric control via monomer fold-switching

V. Muñoz, G. Rivas, J. M. Sanchez-Ruiz, 2019, Nature Communications.

Structure of the Hsp110:Hsc70 nucleotide exchange machine.

Borries Demeler, Jorge Cuellar, Oscar Llorca, 2008, Molecular cell.

Excluded Volume Effects on the Refolding and Assembly of an Oligomeric Protein

A. Muga, J. Carrascosa, J. Valpuesta, 2001, The Journal of Biological Chemistry.

Mechanical stability of low-humidity single DNA molecules.

J. Carrascosa, J. Valpuesta, J. R. Arias-Gonzalez, 2012, Biopolymers.

Structure and thermal denaturation of crystalline and noncrystalline cytochrome oxidase as studied by infrared spectroscopy.

F. Goñi, J. Valpuesta, J. Castresana, 1994, Biochemistry.

GroEL under Heat-Shock

A. Muga, J. Carrascosa, J. Valpuesta, 1998, The Journal of Biological Chemistry.

Size-selective recognition of gold nanoparticles by a molecular chaperone

M. Maeda, M. Yohda, J. Valpuesta, 2010 .

Structure and Non-Structure of Centrosomal Proteins

I. Vernos, R. Méndez-Giráldez, U. Bastolla, 2013, PloS one.

Analysis of electron microscope images and electron diffraction patterns of thin crystals of phi 29 connectors in ice.

R Henderson, R. Henderson, J. Carrascosa, 1994, Journal of molecular biology.

Molecular Rearrangements Involved in the Capsid Shell Maturation of Bacteriophage T7*♦

J. Velázquez-Muriel, A. Cuervo, J. Carrascosa, 2010, The Journal of Biological Chemistry.

Assisted protein folding at low temperature: evolutionary adaptation of the Antarctic fish chaperonin CCT and its client proteins

J. Valpuesta, H. Detrich, H. Yébenes, 2014, Biology Open.

The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction

C. Roodveldt, J. Valpuesta, M. Marcilla, 2017, Scientific Reports.

Lipid-protein interactions. The mitochondrial complex III-phosphatidylcholine-water system.

F. Goñi, J. Valpuesta, J. Arrondo, 1988, Biochimica et biophysica acta.

, José Retarded by Posttranslational Modification Microcin E 492 Amyloid Formation Is

J. Valpuesta, G. Mercado, M. Marín, 2013 .

IHF protein inhibits cleavage but not assembly of plasmid R388 relaxosomes

M. Valle, J. Valpuesta, F. de la Cruz, 1999, Molecular microbiology.

Characterization of ATP and DNA Binding Activities of TrwB, the Coupling Protein Essential in Plasmid R388 Conjugation*

M. Valle, F. Goñi, J. Valpuesta, 1999, The Journal of Biological Chemistry.

Manipulation of single polymerase-DNA complexes

J. Carrascosa, J. Valpuesta, M. Salas, 2012, Cell cycle.

Phosphoinositide 3-Kinase Beta Protects Nuclear Envelope Integrity by Controlling RCC1 Localization and Ran Activity

J. Valpuesta, A. Carrera, Javier Redondo-Muñoz, 2014, Molecular and Cellular Biology.

Increased sensitivity of antigen-experienced T cells through the enrichment of oligomeric T cell receptor complexes.

W. Schamel, B. Alarcón, J. Valpuesta, 2011, Immunity.

Arc self‐association and formation of virus‐like capsids are mediated by an N‐terminal helical coil motif

C. Bramham, R. Loris, Aurora Martínez, 2020, The FEBS journal.

Divergent substrate-binding mechanisms reveal an evolutionary specialization of eukaryotic prefoldin compared to its archaeal counterpart.

P. Chacón, P. Gómez-Puertas, J. Valpuesta, 2007, Structure.

Molecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin.

J. Mwenifumbo, J. Valpuesta, M. Leroux, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Structure and Function of the Cochaperone Prefoldin.

J. Valpuesta, J. Martín-Benito, R. Arranz, 2018, Advances in experimental medicine and biology.

Molecular architecture of the Bardet–Biedl syndrome protein 2-7-9 subcomplex

S. Franklin, J. Valpuesta, Aman Makaju, 2019, The Journal of Biological Chemistry.

The yeast THO complex forms a 5-subunit assembly that directly interacts with active chromatin

J. Valpuesta, A. Dziembowski, J. Cuéllar, 2012, Bioarchitecture.

Expression, Functional Characterization, and Preliminary Crystallization of the Cochaperone Prefoldin from the Thermophilic Fungus Chaetomium thermophilum

K. Noguchi, K. Noi, T. Ogura, 2018, International journal of molecular sciences.

Clathrin Coat Disassembly Illuminates the Mechanisms of Hsp70 Force Generation

J. Valpuesta, A. Jin, R. Sousa, 2016, Nature Structural &Molecular Biology.

Assisted assembly of bacteriophage T7 core components for genome translocation across the bacterial envelope

A. Cuervo, J. Carrascosa, J. Valpuesta, 2021, Proceedings of the National Academy of Sciences.

Truncation-Driven Lateral Association of α-Synuclein Hinders Amyloid Clearance by the Hsp70-Based Disaggregase

A. Muga, J. Valpuesta, I. de la Arada, 2021, International journal of molecular sciences.

The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism

E. Sabidó, J. Valpuesta, J. Martín-Benito, 2019, Scientific Reports.

Ferritin is associated with the aberrant tau filaments present in progressive supranuclear palsy.

J. Valpuesta, M. Arrasate, A. Rábano, 1998, The American journal of pathology.

Purification and Properties of TrwB , a Hexameric , ATP-binding Integral Membrane Protein Essential for R 388 Plasmid Conjugation

F. Goñi, J. Valpuesta, I. Alkorta, 2002 .

Molecular determinants of Arc oligomerization and formation of virus-like capsids

C. Bramham, R. Loris, Aurora Martínez, 2019, bioRxiv.

The Structure of Human Tyrosine Hydroxylase Reveals the Mechanism for Feedback Inhibition by Dopamine

P. Chacón, J. López-Blanco, Aurora Martínez, 2020 .

Role of glycosaminoglycans in determining the helicity of paired helical filaments.

J. Ávila, J. Valpuesta, M. Arrasate, 1997, The American journal of pathology.

Interactions of the HIV-1 fusion peptide with large unilamellar vesicles and monolayers. A cryo-TEM and spectroscopic study.

F. Goñi, J. L. Nieva, R. Mendelsohn, 2000, Biochimica et biophysica acta.

FUNCTION FROM A FOLDING TO A STORING GroEL under Heat-Shock: SWITCHING STRUCTURE: PROTEIN CHEMISTRY AND

A. Muga, J. Carrascosa, J. Valpuesta, 2014 .

A Triton X-100-hydroxyapatite procedure for a rapid purification of bovine heart cytochrome-c oxidase. Characterization of the cytochrome-c oxidase/Triton X-100/phospholipid mixed micelles by laser light scattering.

J. Valpuesta, P. G. Barbon, 1988, Biochimica et biophysica acta.

Mechano-chemical kinetics of DNA replication: identification of the translocation step of a replicative DNA polymerase

J. Carrascosa, J. Valpuesta, M. Salas, 2015, Nucleic acids research.

Resorcinarenes with 2-benzimidazolone bridges: Self-aggregation, self-assembled dimeric capsules, and guest encapsulation

J. Valpuesta, P. Prados, J. de Mendoza, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Interbilayer lipid mixing induced by the human immunodeficiency virus type-1 fusion peptide on large unilamellar vesicles: the nature of the nonlamellar intermediates.

F. Goñi, J. L. Nieva, J. Valpuesta, 1999, Chemistry and physics of lipids.

Structural analysis of the bacteriophage T3 head-to-tail connector.

J. J. Fernández, J. Carrascosa, J. Valpuesta, 2000, Journal of structural biology.

Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin

M. Malumbres, C. Robinson, G. Montoya, 2011, Nature Structural &Molecular Biology.

A structural model for the GroEL chaperonin.

J. Carrascosa, G. Andrés, J. Valpuesta, 1993, FEMS microbiology letters.

Structural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA deposition

A. Velázquez‐Campoy, A. Muga, J. Segura, 2019, Scientific Reports.

Laser light-scattering characterization of mitochondrial complex III-Triton X-100-phospholipid mixed micelles.

F. Goñi, J. Valpuesta, J. M. Macarulla, 1985, Biochimica et biophysica acta.

Nucleus-translocated mitochondrial cytochrome c liberates nucleophosmin-sequestered ARF tumor suppressor by changing nucleolar liquid–liquid phase separation

I. Ayala, A. Velázquez‐Campoy, X. Salvatella, 2022, Nature Structural & Molecular Biology.

Physiological state of submitochondrial particles and their susceptibility to Triton X-100

F. Goñi, J. Valpuesta, J. Gurtubay, 1984, Experientia.

Effect of the nonionic detergent Triton X-100 on mitochondrial succinate-oxidizing enzymes.

F. Goñi, J. Valpuesta, J. Gurtubay, 1984, Archives of biochemistry and biophysics.

Three‐dimensional reconstruction of a recombinant influenza virus ribonucleoprotein particle

J. Ortega, J. Carrascosa, J. Valpuesta, 2001, EMBO reports.

Membrane-surfactant interactions. The role of surfactant in mitochondrial complex III-phospholipid-Triton X-100 mixed micelles.

F. Goñi, J. Valpuesta, J. Arrondo, 1986, The Journal of biological chemistry.

An intrinsic-tryptophan-fluorescence study of phage phi 29 connector/nucleic acid interactions.

J. Carrascosa, J. Valpuesta, M. Urbaneja, 1994, European journal of biochemistry.

Electron cryo-microscopic analysis of crystalline cytochrome oxidase.

R. Henderson, J. Valpuesta, T. Frey, 1990, Journal of molecular biology.

Maturation of phage T7 involves structural modification of both shell and inner core components

J. Carrascosa, X. Agirrezabala, J. Valpuesta, 2005, The EMBO journal.

Globular Aggregates Stemming from the Self-Assembly of an Amphiphilic N-Annulated Perylene Bisimide in Aqueous Media

J. Valpuesta, L. Sánchez, Manuel A Martínez, 2021, Nanomaterials.

The three-dimensional structure of an eukaryotic glutamine synthetase: functional implications of its oligomeric structure.

Alfonso Valencia, Marco Betti, Oscar Llorca, 2006, Journal of structural biology.

Structure of the connector of bacteriophage T7 at 8A resolution: structural homologies of a basic component of a DNA translocating machinery.

Alfonso Valencia, José L Carrascosa, Mikel Valle, 2005, Journal of molecular biology.

Role of the amino terminal domain in GroES oligomerization.

J. Carrascosa, J. Valpuesta, O. Llorca, 1997, Biochimica et biophysica acta.

Prediction of the structure of GroES and its interaction with GroEL

T J Hubbard, A Valencia, A. Valencia, 1995, Proteins.

Alpha,gamma-peptide nanotube templating of one-dimensional parallel fullerene arrangements.

R. Eritja, J. Carrascosa, J. Valpuesta, 2009, Journal of the American Chemical Society.

Yeast mitochondrial RNAP conformational changes are regulated by interactions with the mitochondrial transcription factor

J. Valpuesta, J. Martín-Benito, R. Sousa, 2014, Nucleic acids research.

Active DNA unwinding dynamics during processive DNA replication

J. Carrascosa, J. Valpuesta, M. Salas, 2012, Proceedings of the National Academy of Sciences.

Structural characterization of the NAP; the major adhesion complex of the human pathogen Mycoplasma genitalium

A. Frangakis, E. Querol, J. Piñol, 2017, Molecular microbiology.

Stress-induced recrystallization of a protein crystal by electron irradiation

R. Schuster, E. Beckmann, F. Zemlin, 1999, Nature.

Structural Insights into the Chaperone Activity of the 40-kDa Heat Shock Protein DnaJ

A. Muga, J. Valpuesta, F. Moro, 2013, The Journal of Biological Chemistry.

Engineering protein assemblies with allosteric control via monomer fold-switching

V. Muñoz, G. Rivas, J. M. Sanchez-Ruiz, 2019, Nature Communications.

An infrared spectroscopic study of specifically deuterated fatty-acyl methyl groups in phosphatidylcholine liposomes.

F. Goñi, J. Valpuesta, J. Castresana, 1991, Biochimica et Biophysica Acta.

Chaperonin Mechanisms: Multiple and (Mis)Understood?

A. Horovitz, J. Valpuesta, J. Cuéllar, 2022, Annual review of biophysics.

Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop

G. Rivas, J. Buchner, H. Itoh, 2014, Nature Communications.

Structure of GroEL in Complex with an Early Folding Intermediate of Alanine Glyoxylate Aminotransferase*

E. Salido, J. Valpuesta, J. Martín-Benito, 2010, The Journal of Biological Chemistry.

Beyond the known functions of the CCR4‐NOT complex in gene expression regulatory mechanisms

J. Valpuesta, A. Dziembowski, J. Cuéllar, 2016, BioEssays : news and reviews in molecular, cellular and developmental biology.

Infrared spectroscopic studies of detergent-solubilized uncoupling protein from brown-adipose-tissue mitochondria.

F. Goñi, A. Muga, J. Valpuesta, 1990, European journal of biochemistry.

Elevated levels of Secreted-Frizzled-Related-Protein 1 contribute to Alzheimer’s disease pathogenesis

P. Bovolenta, I. Ferrer, A. Lleó, 2019, Nature Neuroscience.

Hsp70 chaperone: a master player in protein homeostasis

M. Fernández-Fernández, J. Valpuesta, 2018, F1000Research.

The chaperonin CCT controls T cell receptor–driven 3D configuration of centrioles

I. Vernos, F. Sánchez‐Madrid, J. Vázquez, 2020, Science Advances.

Folding for the Immune Synapse: CCT Chaperonin and the Cytoskeleton

F. Sánchez‐Madrid, J. Valpuesta, N. Martín-Cófreces, 2021, Frontiers in Cell and Developmental Biology.

Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly

S. Franklin, J. Valpuesta, Aman Makaju, 2019, Nature Communications.

The chaperonin CCT promotes the formation of fibrillar aggregates of γ-tubulin.

J. Valpuesta, O. Monasterio, G. Araya, 2018, Biochimica et biophysica acta. Proteins and proteomics.

Programmed Cell Death Protein 5 Interacts with the Cytosolic Chaperonin Containing Tailless Complex Polypeptide 1 (CCT) to Regulate β-Tubulin Folding* ♦

Ryan M. Taylor, N. Ahn, J. Prince, 2013, The Journal of Biological Chemistry.

Interaction of p53 with the CCT Complex Promotes Protein Folding and Wild-Type p53 Activity

K. Vousden, P. Muller, J. Valpuesta, 2013, Molecular cell.

Chaperonins: two rings for folding.

G. Montoya, I. Muñoz, J. Valpuesta, 2011, Trends in biochemical sciences.

The substrate recognition mechanisms in chaperonins

K. Willison, P. Gómez-Puertas, J. Carrascosa, 2004, Journal of molecular recognition : JMR.

Modulation of the Hsp90 chaperone cycle by a stringent client protein.

J. Buchner, T. Madl, M. Sattler, 2014, Molecular cell.

SADB phosphorylation of γ-tubulin regulates centrosome duplication

J. Valpuesta, A. Carrera, M. Rodríguez, 2009, Nature Cell Biology.

Assembly of Archaeal Cell Division Protein FtsZ and a GTPase-inactive Mutant into Double-stranded Filaments*

J. Valpuesta, J. Martín-Benito, S. Huecas, 2003, Journal of Biological Chemistry.

Energetics and geometry of FtsZ polymers: nucleated self-assembly of single protofilaments.

J. Valpuesta, J. Martín-Benito, O. Llorca, 2008, Biophysical journal.

Purification and Properties of TrwB, a Hexameric, ATP-binding Integral Membrane Protein Essential for R388 Plasmid Conjugation*

F. Goñi, J. Valpuesta, F. de la Cruz, 2002, The Journal of Biological Chemistry.

Domain topology of human Rasal

A. Wittinghofer, J. Valpuesta, J. Cuéllar, 2017, Biological chemistry.

Polymerization of τ into Filaments in the Presence of Heparin: The Minimal Sequence Required for τ ‐ τ Interaction

J. Ávila, J. Valpuesta, M. Medina, 1996 .

Polymerization of tau into filaments in the presence of heparin: the minimal sequence required for tau-tau interaction.

J. Ávila, J. Valpuesta, M. Medina, 1996, Journal of neurochemistry.

Coexistence of multivalent and monovalent TCRs explains high sensitivity and wide range of response

B. Alarcón, J. Valpuesta, C. Risco, 2005, The Journal of experimental medicine.

The Structure of a Biologically Active Influenza Virus Ribonucleoprotein Complex

J. Carrascosa, J. Valpuesta, J. Martín-Benito, 2009, PLoS pathogens.

Recognition of Membrane-Bound Fusion-Peptide/MPER Complexes by the HIV-1 Neutralizing 2F5 Antibody: Implications for Anti-2F5 Immunogenicity

J. Valpuesta, R. Kunert, Nerea Huarte, 2012, PloS one.

Mitochondrial cytochrome c liberates the nucleophosmin-sequestered ARF tumor suppressor in the nucleolus

I. Ayala, A. Velázquez‐Campoy, X. Salvatella, 2020, bioRxiv.

Molecular architecture of the Bardet–Biedl syndrome protein 2-7-9 subcomplex

S. Franklin, J. Valpuesta, Aman Makaju, 2019, The Journal of Biological Chemistry.

The structure of the complex between &agr;‐tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism

R. Janowski, J. Valpuesta, J. Martín-Benito, 2015, Journal of Cell Science.

Modulation of the Chaperone DnaK Allosterism by the Nucleotide Exchange Factor GrpE*

Roberto Melero, Arturo Muga, Oscar Llorca, 2015, The Journal of Biological Chemistry.

The Hexameric Structure of a Conjugative VirB4 Protein ATPase Provides New Insights for a Functional and Phylogenetic Relationship with DNA Translocases*

A. Peña, J. Carrascosa, J. Valpuesta, 2012, The Journal of Biological Chemistry.

The Structure of Native Influenza Virion Ribonucleoproteins

J. J. Conesa, José Javier Conesa, J. Carrascosa, 2012, Science.

Changes in Microtubule Protofilament Number Induced by Taxol Binding to an Easily Accessible Site

P. Chacón, G. Diakun, J. Valpuesta, 1998, The Journal of Biological Chemistry.

Arc is a flexible modular protein capable of reversible self-oligomerization

C. Bramham, J. Haavik, Aurora Martínez, 2015, The Biochemical journal.

Structural Characterization of the Bacteriophage T7 Tail Machinery*♦

Mark J van Raaij, Mónica Chagoyen, José R Castón, 2013, The Journal of Biological Chemistry.

Eukaryotic type II chaperonin CCT interacts with actin through specific subunits

Julie Grantham, Keith R. Willison, J. J. Fernández, 1999, Nature.

3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin

Michael Radermacher, Keith R. Willison, Oscar Llorca, 1999, Nature Structural Biology.

Dynamics, flexibility, and allostery in molecular chaperonins

Aurora Martínez, J. Valpuesta, Lars Skjærven, 2015, FEBS letters.

Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT

Paulino Gómez-Puertas, José L Carrascosa, P. Gómez-Puertas, 2002, The EMBO journal.

Detailed architecture of a DNA translocating machine: the high-resolution structure of the bacteriophage phi29 connector particle.

José L Carrascosa, J. Pous, J. Carrascosa, 2002, Journal of molecular biology.

The interaction of DNA with bacteriophage phi 29 connector: a study by AFM and TEM.

M. Valle, J. Tamayo, J. Carrascosa, 1996, Journal of structural biology.

Structure of viral connectors and their function in bacteriophage assembly and DNA packaging

J. Carrascosa, J. Valpuesta, J L Carrascosa, 1994, Quarterly Reviews of Biophysics.

Three-dimensional structure of T3 connector purified from overexpressing bacteria.

J. Carazo, J. Carrascosa, J. Valpuesta, 1992, Journal of molecular biology.

The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones

J. Ausió, A. Muga, J. Valpuesta, 2013, Nucleic acids research.

Purification and functional characterization of p16, the ATPase of the bacteriophage Φ29 packaging machinery

J. Carrascosa, J. Valpuesta, B. Ibarra, 2001 .

Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT

K. Willison, P. Gómez-Puertas, J. Carrascosa, 2002, FEBS letters.

PhLP3 Modulates CCT-mediated Actin and Tubulin Folding via Ternary Complexes with Substrates*

J. Valpuesta, M. Leroux, R. Melki, 2006, Journal of Biological Chemistry.

Effects of the Inter-ring Communication in GroEL Structural and Functional Asymmetry*

A. Muga, J. Carrascosa, J. Valpuesta, 1997, The Journal of Biological Chemistry.

Conformational changes in the GroEL oligomer during the functional cycle.

J. Carrascosa, J. Valpuesta, O. Llorca, 1997, Journal of structural biology.

Biochemical Characterization of Symmetric GroEL-GroES Complexes

J. Carrascosa, J. Valpuesta, O. Llorca, 1996, The Journal of Biological Chemistry.

Chaperonins: Nanocarriers with Biotechnological Applications

M. Fernández-Fernández, J. Valpuesta, J. Cuéllar, 2021, Nanomaterials.

Molecular chaperones: functional mechanisms and nanotechnological applications

M. Fernández-Fernández, J. Valpuesta, B. Sot, 2016, Nanotechnology.

Structural analysis of the interactions between hsp70 chaperones and the yeast DNA replication protein Orc4p.

J. Valpuesta, J. Martín-Benito, A. Prieto, 2010, Journal of molecular biology.

GroEL Stability and Function

A. Muga, J. Valpuesta, S. Bañuelos, 2003, Journal of Biological Chemistry.

Topology of the components of the DNA packaging machinery in the phage phi29 prohead.

M. Valle, J. Carrascosa, J. Valpuesta, 2000, Journal of molecular biology.

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face*

J. Ausió, A. Muga, J. Valpuesta, 2010, The Journal of Biological Chemistry.

Ultrastructural and Functional Analyses of Recombinant Influenza Virus Ribonucleoproteins Suggest Dimerization of Nucleoprotein during Virus Amplification

J. Ortega, J. Carrascosa, J. Valpuesta, 2000, Journal of Virology.

Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation

C. Dobson, D. Klenerman, C. Roodveldt, 2015, Proceedings of the National Academy of Sciences.

The structural architecture of an α-synuclein toxic oligomer

D. Otzen, A. Muga, S. Ventura, 2023, bioRxiv.

Purification, crystallization and preliminary X‐ray diffraction studies of the bacteriophage φ29 connector particle

Antonio Párraga, J. Pous, A. Párraga, 1998 .

Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

J. Carrascosa, J. Valpuesta, J. Martín-Benito, 2004, Proceedings of the National Academy of Sciences of the United States of America.

A single-molecule mechanical assay to study DNA replication coupled to DNA unwinding

J. Carrascosa, J. Valpuesta, M. Salas, 2008 .

High resolution atomic force microscopy of double-stranded RNA.

E. Herrero-Galán, J. Valpuesta, J. Gómez‐Herrero, 2016, Nanoscale.

Mechanical properties of high-G.C content DNA with a-type base-stacking.

J. Carrascosa, J. Valpuesta, F. Moreno-Herrero, 2011, Biophysical journal.

Selection of antibody probes to correlate protein sequence domains with their structural distribution

M. Valle, C. Martínez-A, J. Carrascosa, 2008, Protein science : a publication of the Protein Society.

JP Albar domains with their structural distribution Selection of antibody probes to correlate protein sequence

M. Valle, J. Carrascosa, J. Valpuesta, 1999 .

All three chaperonin genes in the archaeon Haloferax volcanii are individually dispensable

C. Robinson, J. Benesch, J. Carrascosa, 2006, Molecular microbiology.

Structural comparison of prokaryotic and eukaryotic chaperonins.

J. Carrascosa, J. Valpuesta, O. Llorca, 2001, Micron.

Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi‐native conformations

J Martín-Benito, K. Willison, J. Carrascosa, 2000, The EMBO journal.

ATP Binding Induces Large Conformational Changes in the Apical and Equatorial Domains of the Eukaryotic Chaperonin Containing TCP-1 Complex*

K. Willison, J. Carrascosa, J. Valpuesta, 1998, The Journal of Biological Chemistry.

Reversible interaction of beta-actin along the channel of the TCP-1 cytoplasmic chaperonin.

J. Carrascosa, J. Valpuesta, S. Marco, 1994, Biophysical journal.

The molecular chaperone CCT sequesters gelsolin and protects it from cleavage by caspase-3.

J. Valpuesta, B. Willardson, J. Cuéllar, 2021, Journal of molecular biology.

Molecular determinants of the ATP hydrolysis asymmetry of the CCT chaperonin complex

F. Pazos, M. Chagoyen, J. Carrascosa, 2014, Proteins.

The structure of CCT–Hsc70NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin

Arturo Muga, Jorge Cuéllar, Eduardo López-Viñas, 2008, Nature Structural &Molecular Biology.

The inter‐ring arrangement of the cytosolic chaperonin CCT

Julie Grantham, José L Carrascosa, K. Willison, 2007, EMBO reports.

Folding, stability and polymerization properties of FtsZ chimeras with inserted tubulin loops involved in the interaction with the cytosolic chaperonin CCT and in microtubule formation.

J. Carrascosa, J. Valpuesta, I. Barthelemy, 2005, Journal of molecular biology.

HYDROMIC: prediction of hydrodynamic properties of rigid macromolecular structures obtained from electron microscopy images

J. García de la Torre, J. García de la Torre, J. Valpuesta, 2001, European Biophysics Journal.

Analysis of the interaction between the eukaryotic chaperonin CCT and its substrates actin and tubulin.

J Martín-Benito, K. Willison, P. Gómez-Puertas, 2001, Journal of structural biology.

Point mutations in a hinge linking the small and large domains of beta-actin result in trapped folding intermediates bound to cytosolic chaperonin CCT.

K. Willison, J. Carrascosa, E. A. McCormack, 2001, Journal of structural biology.

The ‘sequential allosteric ring’ mechanism in the eukaryotic chaperonin‐assisted folding of actin and tubulin

K. Willison, J. Carrascosa, J. Valpuesta, 2001, The EMBO journal.

Partial occlusion of both cavities of the eukaryotic chaperonin with antibody has no effect upon the rates of beta-actin or alpha-tubulin folding.

K. Willison, J. Valpuesta, O. Llorca, 2000, The Journal of biological chemistry.

Conformational Changes Generated in GroEL during ATP Hydrolysis as Seen by Time-resolved Infrared Spectroscopy*

W. Mäntele, A. Muga, J. Carrascosa, 1999, The Journal of Biological Chemistry.

ATP hydrolysis induces an intermediate conformational state in GroEL.

A. Muga, M. Menéndez, J. Carrascosa, 1999, European journal of biochemistry.

The formation of symmetrical GroEL‐GroES complexes in the presence of ATP

J. Carrascosa, J. Valpuesta, O. Llorca, 1994, FEBS letters.

Ionic interactions at both inter‐ring contact sites of GroEL are involved in transmission of the allosteric signal: A time‐resolved infrared difference study

W. Mäntele, A. Muga, J. Valpuesta, 2005, Protein science : a publication of the Protein Society.

Salt Bridges at the Inter-ring Interface Regulate the Thermostat of GroEL*

A. Muga, J. Valpuesta, B. Sot, 2002, The Journal of Biological Chemistry.

Biochemical Characterization of Symmetric GroEL-GroES Complexes EVIDENCE FOR A ROLE IN PROTEIN FOLDING*

J. Carrascosa, J. Valpuesta, O. Llorca, 1995 .

Controlledgrowthand electrical properties of heterojunctions of carbonnanotubes andsiliconnanowires

E. Beckmann, G. Ertl, J. Carrascosa, 1999 .

Prefoldin 5 Is Required for Normal Sensory and Neuronal Development in a Murine Model*

J. Naggert, B. King, Richard S. Smith, 2010, The Journal of Biological Chemistry.

Gold nanoparticles generated in ethosome bilayers, as revealed by cryo-electron-tomography.

M. del Puerto Morales, A. Hernando, J. Valpuesta, 2009, The journal of physical chemistry. B.

Identification of Key Amino Acid Residues Modulating Intracellular and In vitro Microcin E492 Amyloid Formation

J. Valpuesta, O. Monasterio, R. Lagos, 2016, Frontiers in Microbiology.

Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation

J. López-Blanco, Aurora Martínez, J. Valpuesta, 2022, Nature communications.

Architecture and nucleic acids recognition mechanism of the THO complex, an mRNP assembly factor

Jorge Cuéllar, Andrés Aguilera, Andrzej Dziembowski, 2012, The EMBO journal.

Condensation prevails over B-A transition in the structure of DNA at low humidity.

J. Carrascosa, J. Valpuesta, F. Moreno-Herrero, 2011, Biophysical journal.

Hsp70 – a master regulator in protein degradation

M. Fernández-Fernández, J. Valpuesta, Lucía Quintana-Gallardo, 2017, FEBS letters.

Mechanical stability of ethanol-induced A-DNA

J. Carrascosa, J. Valpuesta, J. R. Arias-Gonzalez, 2008 .

Bacterial Tubulin Distinct Loop Sequences and Primitive Assembly Properties Support Its Origin from a Eukaryotic Tubulin Ancestor*

A. Bhattacharyya, J. Valpuesta, J. Andreu, 2011, The Journal of Biological Chemistry.

Characterization of the structure and self-recognition of the human centrosomal protein NA14: implications for stability and function.

D. Laurents, J. Valpuesta, M. Jiménez, 2011, Protein engineering, design & selection : PEDS.

3D structure of the influenza virus polymerase complex: Localization of subunit domains

José L Carrascosa, J. Carrascosa, J. Valpuesta, 2003, Proceedings of the National Academy of Sciences of the United States of America.

The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism

E. Sabidó, J. Valpuesta, J. Martín-Benito, 2019, Scientific Reports.

Faculty Opinions recommendation of Proteasomes. A molecular census of 26S proteasomes in intact neurons.

J. Valpuesta, José M. Valpuesta, 2015 .

Structures of the Gβ-CCT and PhLP1–Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly

Andrew D. Mathis, S. Franklin, J. Prince, 2015, Proceedings of the National Academy of Sciences.

Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly

S. Franklin, J. Valpuesta, Aman Makaju, 2019, Nature Communications.

Symmetric GroEL‐GroES complexes can contain substrate simultaneously in both GroEL rings

J. Carrascosa, J. Valpuesta, O. Llorca, 1997, FEBS letters.

T cell asymmetry and metabolic crosstalk can fine-tune immunological synapses.

F. Sánchez‐Madrid, J. Valpuesta, N. Martín-Cófreces, 2021, Trends in immunology.

Chaperonin CCT controls extracellular vesicle production and cell metabolism through kinesin dynamics

F. Sánchez‐Madrid, J. Vázquez, E. Calvo, 2023, Journal of extracellular vesicles.

Characterization by atomic force microscopy and cryoelectron microscopy of tau polymers assembled in Alzheimer's disease.

J. Ávila, J. Valpuesta, F. Moreno-Herrero, 2001, Journal of Alzheimer's disease : JAD.

The Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 4E10 Monoclonal Antibody Is Better Adapted to Membrane-Bound Epitope Recognition and Blocking than 2F5

J. Valpuesta, R. Kunert, Nerea Huarte, 2008, Journal of Virology.

NEUTRALIZING ANTI-HIV-1 4 E 10 MONOCLONAL ANTIBODY IS BETTER ADAPTED TO MEMBRANE-BOUND EPITOPE RECOGNITION AND BLOCKING THAN 2 F 5

J. Valpuesta, R. Kunert, Nerea Huarte, 2008 .

Chaperonins: folding in the hole.

J. Carrascosa, J. Valpuesta, 2001, Journal of structural biology.

Segregated ordered lipid phases and protein-promoted membrane cohesivity are required for pulmonary surfactant films to stabilize and protect the respiratory surface.

J. Valpuesta, A. Cruz, J. Pérez-Gil, 2013, Faraday discussions.

Crystallographic analysis reveals the 12-fold symmetry of the bacteriophage phi29 connector particle.

J. Pous, A. Párraga, J. Carrascosa, 1998, Journal of molecular biology.

The three-dimensional structure of a DNA translocating machine at 10 A resolution.

J M Carazo, J. J. Fernández, J. Carazo, 1999, Structure.

Single centrosome manipulation reveals its electric charge and associated dynamic structure.

J. Carrascosa, J. Valpuesta, B. Lange, 2009, Biophysical journal.

Microcin E492 Amyloid Formation Is Retarded by Posttranslational Modification

J. Valpuesta, G. Mercado, M. Marín, 2013, Journal of bacteriology.

Structural characterization of the TCR complex by electron microscopy.

B. Alarcón, J. Valpuesta, D. Abia, 2010, International immunology.

A new side opening on prolyl oligopeptidase revealed by electron microscopy

T. Tarragó, M. Gairí, E. Giralt, 2009, FEBS letters.

Combining Electron Microscopy (EM) and Cross-Linking Mass Spectrometry (XL-MS) for Structural Characterization of Protein Complexes.

J. Buchner, D. Rutz, J. Valpuesta, 2021, Methods in molecular biology.

Role of the amino-terminal domain of bacteriophage phi 29 connector in DNA binding and packaging.

L. E. Donate, F. Rojo, J. Carrascosa, 1992, The Journal of biological chemistry.

Purification and functional characterization of p16, the ATPase of the bacteriophage Phi29 packaging machinery.

J. Carrascosa, J. Valpuesta, B. Ibarra, 2001, Nucleic acids research.

Domain architecture of the bacteriophage phi29 connector protein.

M. Valle, C. Martínez-A, J. Carrascosa, 1999, Journal of molecular biology.

Chaperonins: two rings for folding.

G. Montoya, I. Muñoz, J. Valpuesta, 2011, Trends in biochemical sciences.

Structure and Function of the Cytosolic Chaperonin CCT

K. Willison, J. Carrascosa, J. Valpuesta, 2008 .

Structural characterization of microcin E492 amyloid formation: Identification of the precursors.

J. Valpuesta, J. Martín-Benito, G. Mercado, 2012, Journal of structural biology.

Crystal structure of the mammalian cytosolic chaperonin CCT in complex with tubulin

C. Robinson, G. Montoya, E. Bragado‐Nilsson, 2010 .

Hsp70 chaperone: a master player in protein homeostasis

M. Fernández-Fernández, J. Valpuesta, A. Shonhai, 2018, F1000Research.

Increased sensitivity of antigen-experienced T cells through the enrichment of oligomeric T cell receptor complexes.

W. Schamel, B. Alarcón, J. Valpuesta, 2011, Immunity.

The chaperonin CCT promotes the formation of fibrillar aggregates of γ-tubulin.

J. Valpuesta, O. Monasterio, G. Araya, 2018, Biochimica et biophysica acta. Proteins and proteomics.

Temperature dependence of cytochrome c-induced phospholipid oxidation in liposomes

F. Goñi, J. Valpuesta, M. Ondarroa, 1986 .

Phosphorylation Dependence and Stoichiometry of the Complex Formed by Tyrosine Hydroxylase and 14-3-3γ*

A. Heck, J. Haavik, Aurora Martínez, 2014, Molecular & Cellular Proteomics.

Analysis of the interaction between the eukaryotic chaperonin CCT and its substrates actin and tubulin.

K. Willison, P. Gómez-Puertas, J. Carrascosa, 2001, Journal of structural biology.

The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70

Jean‐Didier Maréchal, A. Muga, J. Valpuesta, 2023, Nature communications.

Architecture and nucleic acids recognition mechanism of the THO complex, an mRNP assembly factor

J. Carrascosa, J. Valpuesta, A. Aguilera, 2012, The EMBO journal.