Retinoschisin (RS1) interacts with negatively charged lipid bilayers in the presence of Ca2+: an atomic force microscopy study.
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The dynamic architecture of photoreceptor ribbon synapses: cytoskeletal, extracellular matrix, and intramembrane proteinsStructural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.Cog-Wheel Octameric Structure of RS1, the Discoidin Domain Containing Retinal Protein Associated with X-Linked RetinoschisisX-linked juvenile retinoschisis: clinical diagnosis, genetic analysis, and molecular mechanisms.Biology of retinoschisinAtomic force microscopy of model lipid membranes.High resolution nanomechanical characterization of multi-domain model membranes by fast Force Volume.Retinoschisin Facilitates the Function of L-Type Voltage-Gated Calcium Channels.Measurements of elastic modulus for human anterior lens capsule with atomic force microscopy: the effect of loading force
P2860
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P2860
Retinoschisin (RS1) interacts with negatively charged lipid bilayers in the presence of Ca2+: an atomic force microscopy study.
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2010 nî lūn-bûn
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2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին հրատարակված գիտական հոդված
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Retinoschisin (RS1) interacts ...... atomic force microscopy study.
@ast
Retinoschisin (RS1) interacts ...... atomic force microscopy study.
@en
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Retinoschisin (RS1) interacts ...... atomic force microscopy study.
@ast
Retinoschisin (RS1) interacts ...... atomic force microscopy study.
@en
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Retinoschisin (RS1) interacts ...... atomic force microscopy study.
@ast
Retinoschisin (RS1) interacts ...... atomic force microscopy study.
@en
P2093
P2860
P356
P1433
P1476
Retinoschisin (RS1) interacts ...... atomic force microscopy study.
@en
P2093
Camasamudram Vijayasarathy
Emilios K Dimitriadis
Howard Jaffe
Paul A Sieving
Svetlana Kotova
P2860
P304
P356
10.1021/BI1007029
P407
P577
2010-08-01T00:00:00Z