| P2093 | author name string | Alla S Kostyukova | |
| | Dmitri Tolkatchev | |
| | Garry E Smith | |
| P2860 | cites work | Effects of cardiomyopathy-linked mutations K15N and R21H in tropomyosin on thin-filament regulation and pointed-end dynamics. | Q64963237 |
| | Domain structure of tropomodulin: distinct properties of the N-terminal and C-terminal halves | Q73072354 |
| | The shapes and sizes of two domains of tropomodulin, the P-end-capping protein of actin-tropomyosin | Q73965331 |
| | A trivalent system from vancomycin.D-ala-D-Ala with higher affinity than avidin.biotin | Q74490796 |
| | cAPK-phosphorylation controls the interaction of the regulatory domain of cardiac myosin binding protein C with myosin-S2 in an on-off fashion | Q77998310 |
| | Effects of the N-terminal domains of myosin binding protein-C in an in vitro motility assay: Evidence for long-lived cross-bridges | Q79167123 |
| | Leiomodin/tropomyosin interactions are isoform specific | Q80485853 |
| | Ablation of cardiac myosin-binding protein-C accelerates stretch activation in murine skinned myocardium | Q83018811 |
| | Systematic analysis of tropomodulin/tropomyosin interactions uncovers fine-tuned binding specificity of intrinsically disordered proteins | Q84127722 |
| | Polyvalent Interactions in Biological Systems: Implications for Design and Use of Multivalent Ligands and Inhibitors | Q88519588 |
| | Cardiac-specific knockout of Lmod2 results in a severe reduction in myofilament force production and rapid cardiac failure | Q90918144 |
| | Mutations in beta-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C | Q22008775 |
| | Sequencing, expression analysis, and mapping of three unique human tropomodulin genes and their mouse orthologs | Q22011210 |
| | Cardiac myosin binding protein C: its role in physiology and disease | Q24294438 |
| | Mutations in the cardiac myosin binding protein-C gene on chromosome 11 cause familial hypertrophic cardiomyopathy | Q24304076 |
| | Complete sequence of human fast-type and slow-type muscle myosin-binding-protein C (MyBP-C). Differential expression, conserved domain structure and chromosome assignment | Q24313302 |
| | Dissecting the N-terminal myosin binding site of human cardiac myosin-binding protein C. Structure and myosin binding of domain C2 | Q24338368 |
| | Tropomyosin requires an intact N-terminal coiled coil to interact with tropomodulin | Q24537515 |
| | Tropomodulin caps the pointed ends of actin filaments | Q24672951 |
| | Tropomodulin capping of actin filaments in striated muscle development and physiology | Q26852179 |
| | Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping | Q27639906 |
| | Myosin Binding Protein C Positioned to Play a Key Role in Regulation of Muscle Contraction: Structure and Interactions of Domain C1 | Q27652530 |
| | Structure of a tropomyosin N-terminal fragment at 0.98 Å resolution | Q27673482 |
| | Structural Insight into Unique Cardiac Myosin-binding Protein-C Motif: A PARTIALLY FOLDED DOMAIN | Q27676683 |
| | Mechanism of actin filament pointed-end capping by tropomodulin | Q27684814 |
| | Structure validation by Calpha geometry: phi,psi and Cbeta deviation | Q27860657 |
| | Leiomodin is an actin filament nucleator in muscle cells | Q28117235 |
| | Different localizations and cellular behaviors of leiomodin and tropomodulin in mature cardiomyocyte sarcomeres | Q28119062 |
| | How Leiomodin and Tropomodulin use a common fold for different actin assembly functions | Q28119066 |
| | The Affinity-Enhancing Roles of Flexible Linkers in Two-Domain DNA-Binding Proteins† | Q58881325 |
| | Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy | Q28198707 |
| | Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C | Q28203957 |
| | The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner | Q28237568 |
| | Role of cardiac myosin binding protein C in sustaining left ventricular systolic stiffening | Q28254276 |
| | Cardiac myosin binding protein-C gene splice acceptor site mutation is associated with familial hypertrophic cardiomyopathy | Q28284626 |
| | Organization and sequence of human cardiac myosin binding protein C gene (MYBPC3) and identification of mutations predicted to produce truncated proteins in familial hypertrophic cardiomyopathy | Q28304526 |
| | Knockout of Lmod2 results in shorter thin filaments followed by dilated cardiomyopathy and juvenile lethality | Q28513164 |
| | Structural requirements of tropomodulin for tropomyosin binding and actin filament capping | Q28571101 |
| | Tropomodulin isoforms regulate thin filament pointed-end capping and skeletal muscle physiology | Q28589016 |
| | Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. | Q28909751 |
| | Leiomodin-3 dysfunction results in thin filament disorganization and nemaline myopathy | Q30090215 |
| | C0 and C1 N-terminal Ig domains of myosin binding protein C exert different effects on thin filament activation. | Q30357191 |
| | A Highly Conserved Yet Flexible Linker Is Part of a Polymorphic Protein-Binding Domain in Myosin-Binding Protein C. | Q30393954 |
| | The N-terminal domains of myosin binding protein C can bind polymorphically to F-actin | Q30424900 |
| | Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle. | Q30502467 |
| | The pleated sheet, a new layer configuration of polypeptide chains | Q33711390 |
| | Functional differences between the N-terminal domains of mouse and human myosin binding protein-C. | Q33773355 |
| | Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle. | Q33874993 |
| | Tropomodulin-binding site mapped to residues 7-14 at the N-terminal heptad repeats of tropomyosin isoform 5. | Q33907210 |
| | Unique single molecule binding of cardiac myosin binding protein-C to actin and phosphorylation-dependent inhibition of actomyosin motility requires 17 amino acids of the motif domain | Q34042167 |
| | Mammalian tropomodulins nucleate actin polymerization via their actin monomer binding and filament pointed end-capping activities. | Q34236824 |
| | JPred4: a protein secondary structure prediction server | Q34472202 |
| | Identification of residues within tropomodulin-1 responsible for its localization at the pointed ends of the actin filaments in cardiac myocytes | Q34503247 |
| | Myosin binding protein-C activates thin filaments and inhibits thick filaments in heart muscle cells | Q34830547 |
| | Speeding molecular recognition by using the folding funnel: the fly-casting mechanism | Q35189399 |
| | Mechanical unfolding of cardiac myosin binding protein-C by atomic force microscopy | Q35342243 |
| | Myosin binding protein-C: a regulator of actomyosin interaction in striated muscle | Q35389621 |
| | Myosin binding protein-C slow is a novel substrate for protein kinase A (PKA) and C (PKC) in skeletal muscle | Q35532113 |
| | Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells | Q36179211 |
| | Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle. | Q36232323 |
| | Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: tropomodulin requires tropomyosin for assembly. | Q36235536 |
| | Molecular basis of tropomyosin binding to tropomodulin, an actin-capping protein | Q36259368 |
| | The Phosphorylation Profile of Myosin Binding Protein-C Slow is Dynamically Regulated in Slow-Twitch Muscles in Health and Disease. | Q36273623 |
| | Myosin Binding Protein-C Slow Phosphorylation is Altered in Duchenne Dystrophy and Arthrogryposis Myopathy in Fast-Twitch Skeletal Muscles | Q36273662 |
| | Phosphorylation modulates the mechanical stability of the cardiac myosin-binding protein C motif | Q36554361 |
| | Cardiac Myosin Binding Protein-C Phosphorylation Modulates Myofilament Length-Dependent Activation | Q36579173 |
| | Molecular mechanics of cardiac myosin-binding protein C in native thick filaments | Q36579217 |
| | Tropomodulins and tropomyosins: working as a team | Q36640510 |
| | Site-directed spectroscopy of cardiac myosin-binding protein C reveals effects of phosphorylation on protein structural dynamics. | Q36742853 |
| | Phosphorylation and calcium antagonistically tune myosin-binding protein C's structure and function | Q36742858 |
| | Tropomodulin binds two tropomyosins: a novel model for actin filament capping | Q37000615 |
| | The N-terminal tropomyosin- and actin-binding sites are important for leiomodin 2's function. | Q37175795 |
| | Tropomyosin-binding properties modulate competition between tropomodulin isoforms | Q37365595 |
| | Myosin-binding protein C displaces tropomyosin to activate cardiac thin filaments and governs their speed by an independent mechanism | Q37587694 |
| | Phosphorylation and function of cardiac myosin binding protein-C in health and disease. | Q37644780 |
| | Species-specific differences in the Pro-Ala rich region of cardiac myosin binding protein-C. | Q37706135 |
| | Cardiac myosin-binding protein C: hypertrophic cardiomyopathy mutations and structure-function relationships | Q38163334 |
| | Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles | Q38791519 |
| | Programmatic access to bioinformatics tools from EMBL-EBI update: 2017 | Q38826408 |
| | Overview of the Muscle Cytoskeleton | Q39391006 |
| | Folding properties of functional domains of tropomodulin | Q40186280 |
| | Acceleration of crossbridge kinetics by protein kinase A phosphorylation of cardiac myosin binding protein C modulates cardiac function. | Q40457084 |
| | Calcium regulation of muscle contraction | Q41480233 |
| | The motif of human cardiac myosin-binding protein C is required for its Ca2+-dependent interaction with calmodulin | Q41767925 |
| | Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle | Q41874180 |
| | Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin | Q42375826 |
| | Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes | Q43941100 |
| | Isoform-specific interaction of tropomodulin with skeletal muscle and erythrocyte tropomyosins. | Q44405927 |
| | Effect of the structure of the N terminus of tropomyosin on tropomodulin function | Q44683440 |
| | The myosin mesa and the basis of hypercontractility caused by hypertrophic cardiomyopathy mutations | Q46174255 |
| | Tropomodulin in rat cardiac muscle. Localization of protein is independent of messenger RNA distribution during myofibrillar development | Q46179548 |
| | Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C. | Q46723642 |
| | Transforming bivalent ligands into retractable enzyme inhibitors through polypeptide-protein interactions | Q46734018 |
| | Tropomodulin contains two actin filament pointed end-capping domains | Q46897924 |
| | Characterizing interaction forces between actin and proteins of the tropomodulin family reveals the presence of the N-terminal actin-binding site in leiomodin. | Q47265042 |
| | Structural genomics of Caenorhabditis elegans: crystal structure of the tropomodulin C-terminal domain | Q47307280 |
| | Structural destabilization of tropomyosin induced by the cardiomyopathy-linked mutation R21H. | Q47378513 |
| | Crystal Structure of Leiomodin 2 in Complex with Actin: A Structural and Functional Reexamination | Q47914887 |
| | Skeletal myosin binding protein-C isoforms regulate thin filament activity in a Ca2+-dependent manner | Q49336760 |
| | Leiomodins: larger members of the tropomodulin (Tmod) gene family. | Q55034758 |
| | Leiomodin and tropomodulin in smooth muscle | Q56602165 |
| | NMR for the design of functional mimetics of protein-protein interactions: one key is in the building of bridges | Q56772546 |
| | N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament | Q57132073 |
| | Structural and functional effects of myosin-binding protein-C phosphorylation in heart muscle are not mimicked by serine-to-aspartate substitutions | Q57157253 |
| | Human Cardiac Myosin Binding Protein C: Structural Flexibility within an Extended Modular Architecture | Q57979770 |
| | Cardiac Disorders and Pathophysiology of Sarcomeric Proteins | Q58075710 |
| | Skeletal myosin binding protein-C: An increasingly important regulator of striated muscle physiology | Q58604849 |
| | Single-Chain versus Dimeric Protein Folding: Thermodynamic and Kinetic Consequences of Covalent Linkage | Q58881319 |
| P304 | page(s) | 311-340 | |
| P577 | publication date | 2019-04-13 | |
| P1433 | published in | Progress in Molecular Biology and Translational Science | Q15753415 |
| P1476 | title | Role of intrinsic disorder in muscle sarcomeres | |
| P478 | volume | 166 | |