[HTML][HTML] Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics
Protein complexes are highly dynamic entities that display substantial diversity in their
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics.
EA Chapman, DS Roberts… - Nature …, 2023 - search.ebscohost.com
Protein complexes are highly dynamic entities that display substantial diversity in their
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics
E Chapman, D Roberts, T Tiambeng… - Nature …, 2023 - europepmc.org
Protein complexes are highly dynamic entities that display substantial diversity in their
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics
EA Chapman, DS Roberts… - Nature …, 2023 - ui.adsabs.harvard.edu
Protein complexes are highly dynamic entities that display substantial diversity in their
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics
EA Chapman, DS Roberts, TN Tiambeng… - Nature …, 2023 - ideas.repec.org
Protein complexes are highly dynamic entities that display substantial diversity in their
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics
EA Chapman, DS Roberts, TN Tiambeng… - Nature …, 2023 - econpapers.repec.org
Protein complexes are highly dynamic entities that display substantial diversity in their
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics
EA Chapman, DS Roberts… - Nature …, 2023 - pubmed.ncbi.nlm.nih.gov
Protein complexes are highly dynamic entities that display substantial diversity in their
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
[HTML][HTML] Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics
EA Chapman, DS Roberts, TN Tiambeng… - Nature …, 2023 - ncbi.nlm.nih.gov
Protein complexes are highly dynamic entities that display substantial diversity in their
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics.
EA Chapman, DS Roberts… - Nature …, 2023 - search.ebscohost.com
Protein complexes are highly dynamic entities that display substantial diversity in their
assembly, post-translational modifications, and non-covalent interactions, allowing them to …
assembly, post-translational modifications, and non-covalent interactions, allowing them to …