Talin-1
UniProt Q9Y490 · gene TLN1 · Homo sapiens · 2541 residues
Coverage grid
Mapped evidence per state and technique. Shaded rows rest on a single technique. Badge = best data level in the cell: raw (traces, images, FIDs: can be re-analysed), proc (maps, curves, tables, trajectories) or rep (values in the paper only).
| State | Basis | xray | cryoem | nmr_structure | nmr_shifts | saxs_sans | force_spectroscopy | af_prediction | Total |
|---|---|---|---|---|---|---|---|---|---|
| autoinhibited, compact talin-autoinhibited | observed (one method) | · | proc 1 | · | · | · | · | · | 1 |
| rod unfolded under force (vinculin-binding sites exposed) talin-rod-unfolded | inferred | proc 2 | · | · | · | · | rep 30 | · | 32 |
Unmapped evidence: 41 of 74 items. Mappings come from curator assignments and curated rules; see About for how rules work.
Sources
| Source | Evidence | Mapped |
|---|---|---|
| AlphaFold DB | 1 | 0 |
| BMRB | 16 | 0 |
| RCSB PDB | 4 | 3 |
| SASBDB | 3 | 0 |
| SMASH-BIO | 50 | 30 |
Curated rules applied
talin-force-unfolding: 30 itemstalin-vbs-vinculin: 2 items
Structure
Choose a state. Each model is badged observed or inferred; assumptions are one click away.
States and transitions
| State | Basis | Parent | Description |
|---|---|---|---|
| autoinhibited, compact talin-autoinhibited | observed | — | Full-length talin-1 folded into a compact autoinhibited arrangement, as in 6R9T (cryo-EM, 6.2 Å). |
| rod unfolded under force (vinculin-binding sites exposed) talin-rod-unfolded | inferred | — | Rod helical bundles unfolded by mechanical load, exposing vinculin-binding helices.Assumptions (3)
|
No transitions recorded in this version (no rate or free-energy evidence has been curated yet).
Evidence
One row per deposit or experiment. Filter by technique, environment or text. Unmapped evidence is listed too.
| Evidence | Technique | Observable | Conditions | Mapped to state |
|---|---|---|---|---|
| EV-PDB-4DJ9-2 RCSB PDB | xray | resolution: 2.25 Å | in vitro · -173.15 °C · pH 7.5 Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin binding site 50 (VBS50, residues 2078-2099) · Talin-1 (chains B) | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-vbs-vinculin · low Isolated talin vinculin-binding-site peptide bound to vinculin: the exposed helix, the end point of rod unfolding. |
| EV-PDB-6R9T-1 RCSB PDB | cryoem | resolution: 6.2 Å | in vitro Cryo-EM structure of autoinhibited human talin-1 · Talin-1 (chains A) | autoinhibited, compact · curator:draft (unreviewed) · high Title: cryo-EM structure of autoinhibited human talin-1. |
| EV-PDB-2MWN-2 RCSB PDB | nmr_structure | structure | in vitro · 24.85 °C · pH 6.8 Talin-F3 / RIAM N-terminal Peptide complex · Talin-1 (chains B) | unmapped |
| EV-PDB-1SYQ-2 RCSB PDB | xray | resolution: 2.42 Å | in vitro · -173.15 °C Human vinculin head domain VH1, residues 1-258, in complex with human talin's vinculin binding site 1, residues 607-636 · Talin 1 (chains B) | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-vbs-vinculin · low Isolated talin vinculin-binding-site peptide bound to vinculin: the exposed helix, the end point of rod unfolding. |
| EV-BMRB-15411 BMRB | nmr_shifts | chemical_shift | in vitro · 45 °C · pH 6 NMR structure of the talin C-terminal actin binding site · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-15457 BMRB | nmr_shifts | chemical_shift | in vitro · 34.85 °C · pH 6.5 NMR Structure of the Talin Rod domain, 1655-1822 · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-15615 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.5 NMR Structure of the F0F1 double domain (residues 1-202) of the Talin FERM domain · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-15616 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.5 NMR Structure of the F1 domain (residues 86-202) of the Talin FERM domain · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-15792 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.8 talin-F2F3 · BMRB data: 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-16930 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.5 Chemical shift assignments of the Talin F2 domain (residues 196-309) · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-16932 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.5 Chemical shift assignments of the Talin F2F3 domain (residues 196-405) · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17070 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.5 SOLUTION STRUCTURE OF THE R6 DOMAIN OF TALIN · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17332 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.5 Solution Structure of the talin Vbs2b domain · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17350 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.5 SOLUTION STRUCTURE OF THE R2 DOMAIN OF TALIN · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17363 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.5 NMR Structure of the B domain of talin · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-17555 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.5 Chemical shift assignments of the VBS1 domain of talin · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-18313 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.5 Solution Structure of the A domain of talin · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-BMRB-25343 BMRB | nmr_shifts | chemical_shift | in vitro · -0.15 °C · pH 6.8 Talin-F3 / RIAM N-terminal Peptide complex · BMRB data: 1H chemical shifts, 15N chemical shifts | unmapped |
| EV-BMRB-6285 BMRB | nmr_shifts | chemical_shift | in vitro · 29.85 °C · pH 6.5 15N, 13C, 1H NMR assignment of a 14kDa construct of the focal adhesion protein Talin · BMRB data: 15N chemical shifts, 1H chemical shifts, 13C chemical shifts | unmapped |
| EV-BMRB-7061 BMRB | nmr_shifts | chemical_shift | in vitro · 24.85 °C · pH 6.3 NMR structure of talin-PTB in complex with PIPKI · BMRB data: 13C chemical shifts, 15N chemical shifts, 1H chemical shifts | unmapped |
| EV-SASBDB-SASDFS7 SASBDB | saxs_sans | radius_of_gyration: 3.28 nm ± 0.08 | in vitro · 10 °C · pH 7.2 The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering. · Talin-1 (Δ139-168), human | unmapped |
| EV-SASBDB-SASDFT7 SASBDB | saxs_sans | radius_of_gyration: 3.35 nm ± 0.02 | in vitro · 10 °C · pH 7.2 The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering. · Talin-1, human | unmapped |
| EV-SASBDB-SASDFU7 SASBDB | saxs_sans | radius_of_gyration: 3.02 nm ± 0.08 | in vitro · 10 °C · pH 7.2 The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering. · Talin-1 (Δ134-170/GAG insert), human | unmapped |
| EV-AFDB-AF-Q9Y490-F1 AlphaFold DB | af_prediction | plddt: 75.88 pLDDT | in silico AlphaFold DB prediction AF-Q9Y490-F1 · AlphaFold Monomer v2.0 pipeline, residues 1-2541 | unmapped |
| EV-SMASH-SMFS-000183 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical tension expands the microtubule lattice stepwise and modulates kinesin-1 binding in an isoform-dependent manner · Talin-1; optical tweezers; experiment class: force_generation_motor | unmapped |
| EV-SMASH-SMFS-000317 SMASH-BIO | force_spectroscopy | study_record | in vitro Talin controls the spatial distribution of vinculin tension in focal adhesions · Talin-1; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-000318 SMASH-BIO | force_spectroscopy | study_record | in vitro Talin controls the spatial distribution of vinculin tension in focal adhesions · Talin-1; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-000491 SMASH-BIO | force_spectroscopy | study_record | in cell Locked Nucleic Acid-Modified Force Probe Reveals High-Force Regulation of Yes-Associated Protein through Talin-Vinculin in Breast Cancer. · Talin-1; tension sensors; experiment class: force_generation_motor, receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-000605 SMASH-BIO | force_spectroscopy | study_record | in vitro Single-Molecule Force Spectroscopy Reveals the Mechanical Role of p47 in Protein Stabilization. · Talin-1; magnetic tweezers; experiment class: unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-000797 SMASH-BIO | force_spectroscopy | study_record | in vitro Identical sequences, different behaviors: Protein diversity captured at the single-molecule level. · Talin-1; magnetic tweezers; experiment class: unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-000859 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Molecular dynamics simulations reveal how vinculin refolds partially unfolded talin rod helices to stabilize them against mechanical force. · Talin-1; magnetic tweezers; experiment class: force_generation_motor, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-000978 SMASH-BIO | force_spectroscopy | study_record | in vitro The Novel Chaperone Activity of p47 Modulates Force-Mediated Retrotranslocation from the Endoplasmic Reticulum to the Cytosol · Talin-1; magnetic tweezers; experiment class: force_generation_motor, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-001050 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7 Allosteric activation of vinculin by talin. · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-001140 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.3 Enhanced statistical sampling reveals microscopic complexity in the talin mechanosensor folding energy landscape. · Talin-1; magnetic tweezers; experiment class: unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-001209 SMASH-BIO | force_spectroscopy | study_record | in vitro Kindlin stabilizes the talin·integrin bond under mechanical load by generating an ideal bond. · Talin-1; optical tweezers; experiment class: force_generation_motor, receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-001237 SMASH-BIO | force_spectroscopy | study_record | in vitro Microfluidics-Based Force Spectroscopy Enables High-Throughput Force Experiments with Sub-Nanometer Resolution and Sub-Piconewton Sensitivity. · Talin-1; afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-001290 SMASH-BIO | force_spectroscopy | study_record | in vitro Rapid Regulation of Cardiomyocytes Adhesion on Substrates with Varied Modulus via Mechanical Cues. · Talin-1; afm smfs; experiment class: nucleic_acid_protein_interaction, receptor_ligand_adhesion, rheology_cell, rheology_material | unmapped |
| EV-SMASH-SMFS-001407 SMASH-BIO | force_spectroscopy | study_record | in vitro Analysis of the polar residues located at the head domain of focal adhesion protein vinculin under the presence of the Shigella effector IpaA and its possible implications during in vivo mechanotransduction · Talin-1; force spectroscopy unspecified; experiment class: force_generation_motor, receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-001479 SMASH-BIO | force_spectroscopy | study_record | in vitro Direct Observation of the Mechanical Role of Bacterial Chaperones in Protein Folding. · Talin-1; magnetic tweezers; experiment class: force_generation_motor, rheology_cell, translation_transcription_replication, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-001482-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 11 pN | in vitro · pH 7.4 Direct observation of chaperone-modulated talin mechanics with single-molecule resolution. · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-001523 SMASH-BIO | force_spectroscopy | study_record | in vitro Force-enhanced biophysical connectivity of platelet β3 integrin signaling through Talin is predicted by steered molecular dynamics simulations. · Talin-1; afm smfs; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-001547 SMASH-BIO | force_spectroscopy | study_record | in vitro How talin allosterically activates vinculin · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-001548 SMASH-BIO | force_spectroscopy | study_record | in vitro How talin allosterically activates vinculin · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-001589 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.2 Mechanical regulation of talin through binding and history-dependent unfolding. · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-001597 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechano-Redox Control of Integrins in Thromboinflammation. · Talin-1; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-001679 SMASH-BIO | force_spectroscopy | study_record | in vitro Pulling, failing, and adaptive mechanotransduction of macrophage filopodia. · Talin-1; optical tweezers; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-001744 SMASH-BIO | force_spectroscopy | study_record | in vitro Talin-drug interaction reveals a key molecular determinant for biphasic mechanical effect: studied under single-molecule resolution · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-001750 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.1 The C-terminal actin-binding domain of talin forms an asymmetric catch bond with F-actin. · Talin-1; optical tweezers; experiment class: force_generation_motor, receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-001774 SMASH-BIO | force_spectroscopy | study_record | in vitro Trimethylamine N-oxide (TMAO) enhances substrate mechanical stability probed by single molecule magnetic tweezers · Talin-1; magnetic tweezers; experiment class: unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-001958 SMASH-BIO | force_spectroscopy | study_record | in vitro Identical Sequences, Different Behaviors: Protein Diversity Captured at the Single-Molecule Level · Talin-1; magnetic tweezers; experiment class: unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-002102-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 6 pN | in vitro Real Time Observation of Chaperone-modulated Talin Mechanics Under Single Molecule Resolution · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-002103-r0 SMASH-BIO | force_spectroscopy | unfolding_force: 6 pN | in vitro Real time observation of chaperone-modulated talin mechanics with single molecule resolution · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-002173 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Talin mechanosensitivity is modulated by a direct interaction with cyclin-dependent kinase-1. · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-002181 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 6 The force loading rate drives cell mechanosensing through both reinforcement and cytoskeletal softening. · Talin-1; optical tweezers; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-002182 SMASH-BIO | force_spectroscopy | study_record | in vitro The force loading rate drives cell mechanosensing through both reinforcement and fluidization · Talin-1; optical tweezers; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-002301 SMASH-BIO | force_spectroscopy | study_record | in vitro Different Vinculin Binding Sites Use the Same Mechanism to Regulate Directional Force Transduction. · Talin-1; afm smfs; experiment class: force_generation_motor, receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-002304 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Direct observation of a coil-to-helix contraction triggered by vinculin binding to talin. · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-002565 SMASH-BIO | force_spectroscopy | study_record | in vitro The C-terminal actin binding domain of talin forms an asymmetric catch bond with F-actin · Talin-1; optical tweezers; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-002686 SMASH-BIO | force_spectroscopy | study_record | in vitro Direct Observation of a Coil-to-Helix Contraction Triggered by Vinculin Binding to Talin · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-002689-r0 SMASH-BIO | force_spectroscopy | bond_lifetime: 1000 s | in vitro Direct single-molecule quantification reveals unexpectedly high mechanical stability of vinculin-talin/α-catenin linkages. · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-002714 SMASH-BIO | force_spectroscopy | study_record | in vitro Ephemeral states in protein folding under force captured with a magnetic tweezers design. · Talin-1; magnetic tweezers; experiment class: force_generation_motor, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-003094 SMASH-BIO | force_spectroscopy | study_record | in vitro Ephemeral states in protein folding under force captured with a novel magnetic tweezers design · Talin-1; magnetic tweezers; experiment class: force_generation_motor, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-003182 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 8.5 Mechanical unfolding reveals stable 3-helix intermediates in talin and α-catenin. · Talin-1; afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-003185 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Mechanotransduction in talin through the interaction of the R8 domain with DLC1. · Talin-1; afm smfs; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-003600 SMASH-BIO | force_spectroscopy | study_record | in vitro Molecular stretching modulates mechanosensing pathways. · Talin-1; force spectroscopy unspecified; experiment class: receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-003606 SMASH-BIO | force_spectroscopy | study_record | in cell Multiplexing molecular tension sensors reveals piconewton force gradient across talin-1. · Talin-1; tension sensors; experiment class: force_generation_motor, receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-003816 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 8.5 All Subdomains of the Talin Rod Are Mechanically Vulnerable and May Contribute To Cellular Mechanosensing. · Talin-1; afm smfs; experiment class: receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-003925 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 Improving Osteoblast Response In Vitro by a Nanostructured Thin Film with Titanium Carbide and Titanium Oxides Clustered around Graphitic Carbon. · Talin-1; afm smfs; experiment class: receptor_ligand_adhesion | unmapped |
| EV-SMASH-SMFS-004083 SMASH-BIO | force_spectroscopy | study_record | in vitro · pH 7.4 The mechanical response of talin. · Talin-1; afm smfs; experiment class: receptor_ligand_adhesion, rheology_cell, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-004311 SMASH-BIO | force_spectroscopy | study_record | in vitro Non-channel mechanosensors working at focal adhesion-stress fiber complex. · Talin-1; force spectroscopy unspecified; experiment class: membrane_mechanics, receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-004602 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation. · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-005252 SMASH-BIO | force_spectroscopy | study_record | in vitro Mechano-sensing by actin filaments and focal adhesion proteins. · Talin-1; optical tweezers; experiment class: receptor_ligand_adhesion, unfolding_protein | rod unfolded under force (vinculin-binding sites exposed) · rule:talin-force-unfolding · low SMASH-BIO force record for talin classed as protein unfolding; rod unfolding under load. Most values are extracted automatically. |
| EV-SMASH-SMFS-006213 SMASH-BIO | force_spectroscopy | study_record | in vitro Stretching single talin rod molecules activates vinculin binding. · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
| EV-SMASH-SMFS-007049-r0 SMASH-BIO | force_spectroscopy | elastic_modulus: 200 Pa | in vitro Protrusion force transmission of amoeboid cells crawling on soft biological tissue. · Talin-1; magnetic tweezers; experiment class: receptor_ligand_adhesion, rheology_cell | unmapped |
Conflicts
No conflicts found among comparable evidence.
71 evidence items could not be compared: they lack a comparable observable type, a value, or an uncertainty. Absence of a conflict here is not agreement.
Downloads
- Protein bundle (JSON)
- talin-autoinhibited-cif (mmCIF, observed)
- talin-autoinhibited-pdb (PDB, observed)
- Curation file (YAML)