| human | Q5 |
| P856 | official website | https://risweb.st-andrews.ac.uk:443/portal/en/persons/carlos-penedo(e1903c4a-e36d-4555-9c7e-e604c9873ba0).html |
| P496 | ORCID iD | 0000-0002-5807-5385 |
| P1053 | ResearcherID | B-5568-2009 |
| P1153 | Scopus author ID | 6602376462 |
| P108 | employer | University of St Andrews | Q216273 |
| P734 | family name | Penedo | Q37329706 |
| Penedo | Q37329706 | ||
| Penedo | Q37329706 | ||
| P735 | given name | Carlos | Q364753 |
| Carlos | Q364753 | ||
| P106 | occupation | researcher | Q1650915 |
| P21 | sex or gender | male | Q6581097 |
| Q39146425 | An integrated perspective on RNA aptamer ligand-recognition models: clearing muddy waters. |
| Q38354852 | Application of fluorescent measurements for characterization of riboswitch-ligand interactions. |
| Q38295252 | Binding dynamics of a monomeric SSB protein to DNA: a single-molecule multi-process approach. |
| Q35144890 | Constitutive regulatory activity of an evolutionarily excluded riboswitch variant. |
| Q87957419 | Fluorescence tools to investigate riboswitch structural dynamics |
| Q26740493 | Fluorescence-Based Strategies to Investigate the Structure and Dynamics of Aptamer-Ligand Complexes |
| Q43207204 | Folding of the natural hammerhead ribozyme is enhanced by interaction of auxiliary elements. |
| Q98177170 | Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer |
| Q35787200 | Functional Studies of DNA-Protein Interactions Using FRET Techniques |
| Q47981568 | Functional studies of DNA-protein interactions using FRET techniques. |
| Q36245957 | High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein |
| Q36775572 | Mechanism of DNA loading by the DNA repair helicase XPD. |
| Q53143766 | Morphology-Specific Inhibition of β-Amyloid Aggregates by 17β-Hydroxysteroid Dehydrogenase Type 10. |
| Q33719345 | PCNA and XPF cooperate to distort DNA substrates |
| Q36986746 | PCNA stimulates catalysis by structure-specific nucleases using two distinct mechanisms: substrate targeting and catalytic step. |
| Q45288242 | Photophysical study of a family of [Ru(phen)2(Me n dpq)]2+ complexes in different solvents and DNA: a specific water effect promoted by methyl substitution. |
| Q50318506 | Real-time observation of conformational switching in single conjugated polymer chains. |
| Q51774769 | Real-time probing of β-amyloid self-assembly and inhibition using fluorescence self-quenching between neighbouring dyes. |
| Q35787193 | Single-Molecule Approaches for the Characterization of Riboswitch Folding Mechanisms. |
| Q41941402 | Single-molecule characterization of Fen1 and Fen1/PCNA complexes acting on flap substrates |
| Q39876540 | Single-molecule chemical denaturation of riboswitches. |
| Q86496511 | Single-molecule fluorescence of nucleic acids |
| Q51066039 | Solution-based single molecule imaging of surface-immobilized conjugated polymers. |
| Q62545156 | Solvent dependent photophysics of fac-[Re(CO)3(11,12-X2dppz)(py)]+ (X = H, F or Me) |
| Q48383279 | Towards ratiometric sensing of amyloid fibrils in vitro. |
| Q79878780 | Two competitive routes in the lactim-lactam phototautomerization of a hydroxypyridine derivative cation in water: dissociative mechanism versus water-assisted proton transfer |
| Q96171834 | Ubiquitin transfer by a RING E3 ligase occurs from a closed E2~ubiquitin conformation |
| Q35459320 | Using sm-FRET and denaturants to reveal folding landscapes. |
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