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Unknown
(49)
Genomics
(4)
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Acromyrmex echinatior
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Lactiplantibacillus paraplantarum
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NEWT:185687
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Functional Phosphoproteomics lab, Murdoch Children's Research Institute, Melbourne Australia
(1)
School of Nursing and School of Medicine, Department of Neurology, Johns Hopkins University, Baltimore, MD, United States
(1)
University of Copenhagen, Department of Biomedical Sciences, Jepps Lab, Copenhagen, Denmark
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Ca
2+
attenuates nucleation activity of leiomodin.
Not available
S-EPMC9207750
|
biostudies-literature
Cite
Leiomodin creates a leaky cap at the pointed end of actin-thin filaments.
Not available
S-EPMC7500696
|
biostudies-literature
Cite
The N-terminal tropomyosin- and actin-binding sites are important for leiomodin 2's function.
Not available
S-EPMC4985258
|
biostudies-literature
Cite
The role of leiomodin in actin dynamics: a new road or a secret gate.
Not available
S-EPMC8761783
|
biostudies-literature
Cite
Putative Autoantigen Leiomodin-1 Is Expressed in the Human Brain and in the Membrane Fraction of Newly Formed Neurons.
Not available
S-EPMC7763904
|
biostudies-literature
Cite
Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle.
Not available
S-EPMC2931607
|
biostudies-literature
Cite
A leiomodin 2 neonatal dilated cardiomyopathy causing mutation results inaltered actin-regulatory gene signatures andcardiomyocyte dysfunction
A leiomodin 2 neonatal dilated cardiomyopathy causing mutation results inaltered actin-regulatory gene signatures andcardiomyocyte dysfunction
PRJNA1133781
|
ENA
Cite
Location matters – how the cytoskeletal protein Leiomodin 1 controls myogenic differentiation by modulating Sirtuin 1 localization
Location matters – how the cytoskeletal protein Leiomodin 1 controls myogenic differentiation by modulating Sirtuin 1 localization
PRJNA1070589
|
ENA
Cite
Localization of the binding interface between leiomodin-2 and α-tropomyosin.
Not available
S-EPMC5079754
|
biostudies-literature
Cite
Leiomodin-3 dysfunction results in thin filament disorganization and nemaline myopathy.
Not available
S-EPMC4347224
|
biostudies-literature
Cite
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