José M. Valpuesta

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

Ortega, Joaquín, Martín-Benito, Jaime, Zürcher, Thomas, Valpuesta, José M., Carrascosa, José L., Ortín, Juan

Influenza virus ribonucleoproteins (RNPs) were reconstituted in vivo from cloned cDNAs expressing the three polymerase subunits, the nucleoprotein (NP), and short template RNAs. The structure of...

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

Martín-Benito, Jaime, Boskovic, Jasminka, Gómez-Puertas, Paulino, Carrascosa, José L., Simons, C.Torrey, Lewis, Sally A., ...

The biogenesis of the cytoskeletal proteins actin and tubulin involves interaction of nascent chains of each of the two proteins with the oligomeric protein prefoldin (PFD) and their subsequent...

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

Llorca, Oscar, Martín-Benito, Jaime, Grantham, Julie, Ritco-Vonsovici, Monica, Willison, Keith R., Carrascosa, José L., ...

Folding to completion of actin and tubulin in the eukaryotic cytosol requires their interaction with cytosolic chaperonin CCT [chaperonin containing tailless complex polypeptide 1 (TCP-1)]....

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

Llorca, Oscar, Martín-Benito, Jaime, Ritco-Vonsovici, Monica, Grantham, Julie, Hynes, Gillian M., Willison, Keith R., ...

Three-dimensional reconstruction from cryoelectron micrographs of the eukaryotic cytosolic chaperonin CCT complexed to tubulin shows that CCT interacts with tubulin (both the α and β isoforms)...

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

Area, Estela, Martín-Benito, Jaime, Gastaminza, Pablo, Torreira, Eva, Valpuesta, José M., Carrascosa, José L., ...

The 3D structure of the influenza virus polymerase complex was determined by electron microscopy and image processing of recombinant ribonucleoproteins (RNPs). The RNPs were generated by in vivo...

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

Lundin, Victor F., Stirling, Peter C., Gomez-Reino, Juan, Mwenifumbo, Jill C., Obst, Jennifer M., Valpuesta, José M., ...

Prefoldin (PFD) is a jellyfish-shaped molecular chaperone that has been proposed to play a general role in de novo protein folding in archaea and is known to assist the biogenesis of actins,...

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

Martín-Benito, Jaime, Bertrand, Sara, Hu, Ting, Ludtke, Paul J., McLaughlin, Joseph N., Willardson, Barry M., ...

The three-dimensional structure of the complex formed between the cytosolic chaperonin CCT (chaperonin containing TCP-1) and phosducin (Pdc)-like protein (PhLP), a regulator of CCT activity, has been...

Three-dimensional reconstruction of a recombinant influenza virus ribonucleoprotein particle

Martín-Benito, Jaime, Area, Estela, Ortega, Joaquín, Llorca, Oscar, Valpuesta, José M., Carrascosa, José L., ...

A three-dimensional structural model of an influenza virus ribonucleoprotein particle reconstituted in vivo from recombinant proteins and a model genomic vRNA has been generated by electron...

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

Ortega, Joaquín, Martín-Benito, Jaime, Zürcher, Thomas, Valpuesta, José M., Carrascosa, José L., Ortín, Juan

Influenza virus ribonucleoproteins (RNPs) were reconstituted in vivo from cloned cDNAs expressing the three polymerase subunits, the nucleoprotein (NP), and short template RNAs. The structure of...

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

Martín-Benito, Jaime, Boskovic, Jasminka, Gómez-Puertas, Paulino, Carrascosa, José L., Simons, C.Torrey, Lewis, Sally A., ...

The biogenesis of the cytoskeletal proteins actin and tubulin involves interaction of nascent chains of each of the two proteins with the oligomeric protein prefoldin (PFD) and their subsequent...

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

Llorca, Oscar, Martín-Benito, Jaime, Grantham, Julie, Ritco-Vonsovici, Monica, Willison, Keith R., Carrascosa, José L., ...

Folding to completion of actin and tubulin in the eukaryotic cytosol requires their interaction with cytosolic chaperonin CCT [chaperonin containing tailless complex polypeptide 1 (TCP-1)]....

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

Llorca, Oscar, Martín-Benito, Jaime, Ritco-Vonsovici, Monica, Grantham, Julie, Hynes, Gillian M., Willison, Keith R., ...

Three-dimensional reconstruction from cryoelectron micrographs of the eukaryotic cytosolic chaperonin CCT complexed to tubulin shows that CCT interacts with tubulin (both the α and β isoforms)...

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

Area, Estela, Martín-Benito, Jaime, Gastaminza, Pablo, Torreira, Eva, Valpuesta, José M., Carrascosa, José L., ...

The 3D structure of the influenza virus polymerase complex was determined by electron microscopy and image processing of recombinant ribonucleoproteins (RNPs). The RNPs were generated by in vivo...

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

Lundin, Victor F., Stirling, Peter C., Gomez-Reino, Juan, Mwenifumbo, Jill C., Obst, Jennifer M., Valpuesta, José M., ...

Prefoldin (PFD) is a jellyfish-shaped molecular chaperone that has been proposed to play a general role in de novo protein folding in archaea and is known to assist the biogenesis of actins,...

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

Martín-Benito, Jaime, Bertrand, Sara, Hu, Ting, Ludtke, Paul J., McLaughlin, Joseph N., Willardson, Barry M., ...

The three-dimensional structure of the complex formed between the cytosolic chaperonin CCT (chaperonin containing TCP-1) and phosducin (Pdc)-like protein (PhLP), a regulator of CCT activity, has been...

Three-dimensional reconstruction of a recombinant influenza virus ribonucleoprotein particle

Martín-Benito, Jaime, Area, Estela, Ortega, Joaquín, Llorca, Oscar, Valpuesta, José M., Carrascosa, José L., ...

A three-dimensional structural model of an influenza virus ribonucleoprotein particle reconstituted in vivo from recombinant proteins and a model genomic vRNA has been generated by electron...

The inter-ring arrangement of the cytosolic chaperonin CCT

Martín-Benito, Jaime, Grantham, Julie, Boskovic, Jasminka, Brackley, Karen I, Carrascosa, José L, Willison, Keith R, ...

The eukaryotic cytosolic chaperonin CCT (chaperonin containing TCP-1) is the most complex of all chaperonins—an oligomeric structure built from two identical rings, each composed of single copies...

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

Schamel, Wolfgang W.A., Arechaga, Ignacio, Risueño, Ruth M., Van Santen, Hisse M., Cabezas, Pilar, Risco, Cristina, ...

A long-standing paradox in the study of T cell antigen recognition is that of the high specificity–low affinity T cell receptor (TCR)–major histocompatibility complex peptide (MHCp) interaction....