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A HaloTag-TEV genetic cassette for mechanical phenotyping of proteins from tissues
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/anie.200906388openalex-snapshot
A “Force Buffer” Protecting Immunoglobulin Titin
inferredcites →https://doi.org/10.1002/anie.201700411openalex-snapshot
Elasticity of the Transition State Leading to an Unexpected Mechanical Stabilization of Titin Immunoglobulin Domains
inferredcites →https://doi.org/10.1002/anie.201703630openalex-snapshot
Mechanical Deformation Accelerates Protein Ageing
inferredcites →https://doi.org/10.1006/jmbi.1996.0441openalex-snapshot
Towards a Molecular Understanding of the Elasticity of Titin
inferredcites →https://doi.org/10.1006/jmbi.2000.4279openalex-snapshot
Titin and the sarcomere symmetry paradox11Edited by J. Karn
inferredcites →https://doi.org/10.1007/s10974-016-9454-4openalex-snapshot
Is muscle powered by springs or motors?
inferredcites →https://doi.org/10.1007/s12195-014-0364-5openalex-snapshot
Talin Dependent Mechanosensitivity of Cell Focal Adhesions
inferredcites →https://doi.org/10.1016/j.bpj.2009.07.041openalex-snapshot
Tuning Passive Mechanics through Differential Splicing of Titin during Skeletal Muscle Development
inferredcites →https://doi.org/10.1016/j.bpj.2010.02.053openalex-snapshot
Collapse Dynamics of Single Proteins Extended by Force
inferredcites →https://doi.org/10.1016/j.bpj.2015.06.002openalex-snapshot
Titin Domains Progressively Unfolded by Force Are Homogenously Distributed along the Molecule
inferredcites →https://doi.org/10.1016/j.cell.2014.01.056openalex-snapshot
S-Glutathionylation of Cryptic Cysteines Enhances Titin Elasticity by Blocking Protein Folding
inferredcites →https://doi.org/10.1016/j.celrep.2016.01.025openalex-snapshot
Work Done by Titin Protein Folding Assists Muscle Contraction
inferredcites →https://doi.org/10.1016/j.celrep.2019.04.046openalex-snapshot
The Mechanical Power of Titin Folding
inferredcites →https://doi.org/10.1016/j.pep.2007.04.013openalex-snapshot
A combined approach to improving large-scale production of tobacco etch virus protease
inferredcites →https://doi.org/10.1016/j.redox.2018.101074openalex-snapshot
Redox regulation of protein nanomechanics in health and disease: Lessons from titin
inferredcites →https://doi.org/10.1016/j.str.2011.12.008openalex-snapshot
Dissecting the Fibrillin Microfibril: Structural Insights into Organization and Function
inferredcites →https://doi.org/10.1016/j.str.2013.02.020openalex-snapshot
Structural Insight into the Giant Ca2+-Binding Adhesin SiiE: Implications for the Adhesion of Salmonella enterica to Polarized Epithelial Cells
inferredcites →https://doi.org/10.1016/j.tcb.2016.07.005openalex-snapshot
The Piconewton Force Awakens: Quantifying Mechanics in Cells
inferredcites →https://doi.org/10.1016/s0006-3495(97)78123-2openalex-snapshot
Actin-titin interaction in cardiac myofibrils: probing a physiological role
inferredcites →https://doi.org/10.1021/acs.bioconjchem.5b00191openalex-snapshot
HaloTag Technology: A Versatile Platform for Biomedical Applications
inferredcites →https://doi.org/10.1021/acs.jpclett.7b01509openalex-snapshot
Proteins Breaking Bad: A Free Energy Perspective
inferredcites →https://doi.org/10.1021/acsnano.6b01658openalex-snapshot
All Subdomains of the Talin Rod Are Mechanically Vulnerable and May Contribute To Cellular Mechanosensing
inferredcites →https://doi.org/10.1021/cb800025kopenalex-snapshot
HaloTag: A Novel Protein Labeling Technology for Cell Imaging and Protein Analysis
inferredcites →https://doi.org/10.1021/jacs.6b05429openalex-snapshot
A HaloTag Anchored Ruler for Week-Long Studies of Protein Dynamics
inferredcites →https://doi.org/10.1021/la101658aopenalex-snapshot
Application of HaloTag Protein to Covalent Immobilization of Recombinant Proteins for Single Molecule Force Spectroscopy
inferredcites →https://doi.org/10.1038/14907openalex-snapshot
Single protein misfolding events captured by atomic force microscopy.
inferredcites →https://doi.org/10.1038/323160a0openalex-snapshot
A physiological role for titin and nebulin in skeletal muscle
inferredcites →https://doi.org/10.1038/347685a0openalex-snapshot
Sequence and domain structure of talin
inferredcites →https://doi.org/10.1038/387308a0openalex-snapshot
Elasticity and unfolding of single molecules of the giant muscle protein titin
inferredcites →https://doi.org/10.1038/47083openalex-snapshot
Mechanical unfolding intermediates in titin modules
inferredcites →https://doi.org/10.1038/nature00938openalex-snapshot
Reverse engineering of the giant muscle protein titin
inferredcites →https://doi.org/10.1038/nature01517openalex-snapshot
Hidden complexity in the mechanical properties of titin
inferredcites →https://doi.org/10.1038/nature10099openalex-snapshot
Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins
inferredcites →https://doi.org/10.1038/nchembio.1939openalex-snapshot
Mapping the energy landscape for second-stage folding of a single membrane protein
inferredcites →https://doi.org/10.1038/ng815openalex-snapshot
Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy
inferredcites →https://doi.org/10.1038/nprot.2013.056openalex-snapshot
Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy
inferredcites →https://doi.org/10.1038/s41467-017-00771-6openalex-snapshot
Trigger factor chaperone acts as a mechanical foldase
inferredcites →https://doi.org/10.1038/s41467-017-02528-7openalex-snapshot
Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity
inferredcites →https://doi.org/10.1056/nejmoa1110186openalex-snapshot
Truncations of Titin Causing Dilated Cardiomyopathy
inferredcites →https://doi.org/10.1056/nejmoa1505517openalex-snapshot
Shared Genetic Predisposition in Peripartum and Dilated Cardiomyopathies
inferredcites →https://doi.org/10.1073/pnas.0400033101openalex-snapshot
The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
inferredcites →https://doi.org/10.1073/pnas.0805034105openalex-snapshot
Mechanoenzymatics of titin kinase
inferredcites →https://doi.org/10.1073/pnas.1211274109openalex-snapshot
Dynamic force sensing of filamin revealed in single-molecule experiments
inferredcites →https://doi.org/10.1073/pnas.1322611111openalex-snapshot
Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments
inferredcites →https://doi.org/10.1073/pnas.1411493111openalex-snapshot
Deleting titin’s I-band/A-band junction reveals critical roles for titin in biomechanical sensing and cardiac function
inferredcites →https://doi.org/10.1073/pnas.1821284116openalex-snapshot
Ephemeral states in protein folding under force captured with a magnetic tweezers design
inferredcites →https://doi.org/10.1073/pnas.96.7.3694openalex-snapshot
Mechanical and chemical unfolding of a single protein: A comparison
inferredcites →https://doi.org/10.1073/pnas.98.2.468openalex-snapshot
Stepwise unfolding of titin under force-clamp atomic force microscopy
inferredcites →https://doi.org/10.1074/jbc.m307473200openalex-snapshot
Association of the Chaperone αB-crystallin with Titin in Heart Muscle
inferredcites →https://doi.org/10.1083/jcb.106.5.1563openalex-snapshot
The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line.
inferredcites →https://doi.org/10.1083/jcb.201010099openalex-snapshot
Titin visualization in real time reveals an unexpected level of mobility within and between sarcomeres
inferredcites →https://doi.org/10.1085/jgp.200409091openalex-snapshot
The Early History of the Biochemistry of Muscle Contraction
inferredcites →https://doi.org/10.1085/jgp.200509364openalex-snapshot
Isoform Diversity of Giant Proteins in Relation to Passive and Active Contractile Properties of Rabbit Skeletal Muscles
inferredcites →https://doi.org/10.1086/342380openalex-snapshot
Tibial Muscular Dystrophy Is a Titinopathy Caused by Mutations in TTN, the Gene Encoding the Giant Skeletal-Muscle Protein Titin
inferredcites →https://doi.org/10.1091/mbc.e13-12-0707openalex-snapshot
Force is a signal that cells cannot ignore
inferredcites →https://doi.org/10.1111/febs.14854openalex-snapshot
Posttranslational modifications of titin from cardiac muscle: how, where, and what for?
inferredcites →https://doi.org/10.1126/sciadv.aaq0243openalex-snapshot
The force-dependent mechanism of DnaK-mediated mechanical folding
inferredcites →https://doi.org/10.1126/science.1092497openalex-snapshot
Force-Clamp Spectroscopy Monitors the Folding Trajectory of a Single Protein
inferredcites →https://doi.org/10.1126/science.1116702openalex-snapshot
Direct Observation of the Three-State Folding of a Single Protein Molecule
inferredcites →https://doi.org/10.1126/science.1162912openalex-snapshot
Stretching Single Talin Rod Molecules Activates Vinculin Binding
inferredcites →https://doi.org/10.1126/science.1439819openalex-snapshot
Direct Mechanical Measurements of the Elasticity of Single DNA Molecules by Using Magnetic Beads
inferredcites →https://doi.org/10.1126/science.276.5315.1109openalex-snapshot
Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM
inferredcites →https://doi.org/10.1126/science.276.5315.1112openalex-snapshot
Folding-Unfolding Transitions in Single Titin Molecules Characterized with Laser Tweezers
inferredcites →https://doi.org/10.1126/science.8079175openalex-snapshot
Entropic Elasticity of λ-Phage DNA
inferredcites →https://doi.org/10.1126/science.aaf0659openalex-snapshot
Detyrosinated microtubules buckle and bear load in contracting cardiomyocytes
inferredcites →https://doi.org/10.1126/science.aat5011openalex-snapshot
CRISPR-Cas guides the future of genetic engineering
inferredcites →https://doi.org/10.1146/annurev-physiol-021317-121234openalex-snapshot
Titin Gene and Protein Functions in Passive and Active Muscle
inferredcites →https://doi.org/10.1146/annurev-physiol-021317-121254openalex-snapshot
The Work of Titin Protein Folding as a Major Driver in Muscle Contraction
inferredcites →https://doi.org/10.1161/circresaha.108.184408openalex-snapshot
Protein Kinase G Modulates Human Myocardial Passive Stiffness by Phosphorylation of the Titin Springs
inferredcites →https://doi.org/10.1161/circresaha.109.198465openalex-snapshot
PKC Phosphorylation of Titin’s PEVK Element
inferredcites →https://doi.org/10.1161/circulationaha.110.005405openalex-snapshot
Genetic Variation in Titin in Arrhythmogenic Right Ventricular Cardiomyopathy–Overlap Syndromes
inferredcites →https://doi.org/10.1161/hh2301.100981openalex-snapshot
The Complete Gene Sequence of Titin, Expression of an Unusual ≈700-kDa Titin Isoform, and Its Interaction With Obscurin Identify a Novel Z-Line to I-Band Linking System
inferredcites →https://doi.org/10.1186/s40478-017-0474-0openalex-snapshot
Translocation of molecular chaperones to the titin springs is common in skeletal myopathy patients and affects sarcomere function
inferredcites →https://doi.org/10.1212/wnl.43.8.1581openalex-snapshot
Titin antibodies in myasthenia gravis
inferredcites →https://doi.org/10.1242/jcs.104.1.119openalex-snapshot
A survey of interactions made by the giant protein titin
inferredcites →https://doi.org/10.1242/jcs.108.9.3029openalex-snapshot
Characterization of a 5.4 kb cDNA fragment from the Z-line region of rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases
inferredcites →https://doi.org/10.1242/jcs.111.11.1567openalex-snapshot
Characterizing titin’s I-band Ig domain region as an entropic spring
inferredcites →https://doi.org/10.1242/jcs.138461openalex-snapshot
Low-force transitions in single titin molecules reflect a memory of contractile history
inferredcites →https://doi.org/10.1371/journal.ppat.1006418openalex-snapshot
Structural and functional dissection reveals distinct roles of Ca2+-binding sites in the giant adhesin SiiE of Salmonella enterica
inferredcites →https://doi.org/10.1529/biophysj.106.091561openalex-snapshot
Contour Length and Refolding Rate of a Small Protein Controlled by Engineered Disulfide Bonds
inferredcites →https://doi.org/10.1529/biophysj.106.097741openalex-snapshot
The Mechanical Fingerprint of a Parallel Polyprotein Dimer
inferredcites →https://doi.org/10.3389/fphys.2014.00035openalex-snapshot
Titin isoform size is not correlated with thin filament length in rat skeletal muscle
inferredcites →https://doi.org/10.3791/54052openalex-snapshot
The Treadmill Fatigue Test: A Simple, High-throughput Assay of Fatigue-like Behavior for the Mouse
inferredcites →https://doi.org/10.7554/elife.09406openalex-snapshot
An internal promoter underlies the difference in disease severity between N- and C-terminal truncation mutations of Titin in zebrafish
inferredcites →https://doi.org/10.7554/elife.40532openalex-snapshot
Downsizing the molecular spring of the giant protein titin reveals that skeletal muscle titin determines passive stiffness and drives longitudinal hypertrophy
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1007/s12551-021-00822-9openalex-snapshot
Protein nanomechanics in biological context
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