Phosphorylation of a twitchin-related protein controls catch and calcium sensitivity of force production in invertebrate smooth muscle.
about
Large isoforms of UNC-89 (obscurin) are required for muscle cell architecture and optimal calcium release in Caenorhabditis elegansThe myosin cross-bridge cycle and its control by twitchin phosphorylation in catch muscleThe latch-bridge hypothesis of smooth muscle contractionRegulation of catch muscle by twitchin phosphorylation: effects on force, ATPase, and shortening.The N-terminal region of twitchin binds thick and thin contractile filaments: redundant mechanisms of catch force maintenance.Catch force links and the low to high force transition of myosinA force-activated kinase in a catch smooth muscle.Catch muscle myorod modulates ATPase activity of Myosin in a phosphorylation-dependent way.Twitchin kinase interacts with MAPKAP kinase 2 in Caenorhabditis elegans striated muscle.Myosin cross-bridge kinetics and the mechanism of catchInvertebrate muscles: muscle specific genes and proteins.An in vitro assay reveals essential protein components for the "catch" state of invertebrate smooth muscleTwitchin as a regulator of catch contraction in molluscan smooth muscle.Unphosphorylated twitchin forms a complex with actin and myosin that may contribute to tension maintenance in catch.Muscle contraction phenotypic analysis enabled by optogenetics reveals functional relationships of sarcomere components in Caenorhabditis elegansSingle-molecule force spectroscopy reveals a stepwise unfolding of Caenorhabditis elegans giant protein kinase domains.Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Small-angle X-ray diffraction studies of a molluscan smooth muscle in the catch stateMechanism of catch force: tethering of thick and thin filaments by twitchin.Myosin loop 2 is involved in the formation of a trimeric complex of twitchin, actin, and myosin.Temperature compensation of neuromuscular modulation in aplysia.Myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro.Protein phosphatase 2B dephosphorylates twitchin, initiating the catch state of invertebrate smooth muscle.Identification of multiple isoforms of the cAMP-dependent protein kinase catalytic subunit in the bivalve mollusc Mytilus galloprovincialis.Regulation of Contraction by the Thick Filaments in Skeletal Muscle.Why are muscles strong, and why do they require little energy in eccentric action?
P2860
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P2860
Phosphorylation of a twitchin-related protein controls catch and calcium sensitivity of force production in invertebrate smooth muscle.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Phosphorylation of a twitchin- ...... in invertebrate smooth muscle.
@ast
Phosphorylation of a twitchin- ...... in invertebrate smooth muscle.
@en
type
label
Phosphorylation of a twitchin- ...... in invertebrate smooth muscle.
@ast
Phosphorylation of a twitchin- ...... in invertebrate smooth muscle.
@en
prefLabel
Phosphorylation of a twitchin- ...... in invertebrate smooth muscle.
@ast
Phosphorylation of a twitchin- ...... in invertebrate smooth muscle.
@en
P2093
P2860
P356
P1476
Phosphorylation of a twitchin- ...... in invertebrate smooth muscle.
@en
P2093
D Funabara
D J Hartshorne
M J Siegman
S Kinoshita
T M Butler
P2860
P304
P356
10.1073/PNAS.95.9.5383
P407
P577
1998-04-01T00:00:00Z