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Structural modeling for the open state of an NMDA receptor.
Structural modeling for the open state of an NMDA receptor.
Role of cardiac troponin I carboxy terminal mobile domain and linker sequence in regulating cardiac contraction.
Role of cardiac troponin I carboxy terminal mobile domain and linker sequence in regulating cardiac contraction.
DNA Interactions Probed by Hydrogen-Deuterium Exchange (HDX) Fourier Transform Ion Cyclotron Resonance Mass Spectrometry Confirm External Binding Sites on the Minichromosomal Maintenance (MCM) Helicase.
DNA Interactions Probed by Hydrogen-Deuterium Exchange (HDX) Fourier Transform Ion Cyclotron Resonance Mass Spectrometry Confirm External Binding Sites on the Minichromosomal Maintenance (MCM) Helicase.
Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains.
Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains.
Divergent roles of a peripheral transmembrane segment in AMPA and NMDA receptors.
Divergent roles of a peripheral transmembrane segment in AMPA and NMDA receptors.
structure of the actin-smooth muscle myosin motor domain complex in the rigor state.
structure of the actin-smooth muscle myosin motor domain complex in the rigor state.
Structural Influences
Structural Influences
Enhanced troponin I binding explains the functional changes produced by the hypertrophic cardiomyopathy mutation A8V of cardiac troponin C.
Enhanced troponin I binding explains the functional changes produced by the hypertrophic cardiomyopathy mutation A8V of cardiac troponin C.
DEAD-box Protein Rok1 Orchestrates 40S and 60S Ribosome Assembly by Promoting the Release of Rrp5 from Pre-40S Ribosomes to Allow for 60S Maturation.
DEAD-box Protein Rok1 Orchestrates 40S and 60S Ribosome Assembly by Promoting the Release of Rrp5 from Pre-40S Ribosomes to Allow for 60S Maturation.
functional significance of the last 5 residues of the C-terminus of cardiac troponin I.
functional significance of the last 5 residues of the C-terminus of cardiac troponin I.