ABSTRACT Glanzmann thrombasthenia (GT) is an inherited hemorrhagic disorder characterised by impaired platelet functions, manifested clinically as spontaneous bleeding. It is usually inherited in an autosomal recessive manner. Platelet dysfunction in patients with GT is caused by quantitative and/or qualitative deficiencies in αIIbβ3, which result from
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Cryo-ET and MD simulations reveal that dynein-2 is tuned for binding to the A-tubule of the ciliary doublet. [PDF]
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Defective I1 dynein in <i>Chlamydomonas</i> axonemes is epistatic to the RII-binding domain function of radial spoke protein 3 (RSP3) in the regulation of ciliary motility. [PDF]
Sebastian MJ, Solmonson A, Gaillard AR.
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NuMA and Ninein: Dynein Cargo-Adaptors Without a Classical Cargo. [PDF]
Guo K, Merdes A.
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Active fluctuations of cytoplasmic actomyosin networks facilitate dynein-driven transport. [PDF]
Torisawa T, Saito K, Furuta K, Kimura A.
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Structural diversity and unity amongst axonemal dynein assembly factors. [PDF]
Ren M, Jaleel SA, King SM, Mali GR.
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A Syd and RUFY dynein adaptor complex mediates axonal circulation of dense core vesicles. [PDF]
Lund VK +8 more
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Dominant spinal muscular atrophy linked mutations in the cargo binding domain of BICD2 result in altered interactomes and dynein hyperactivity. [PDF]
Neiswender H +8 more
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A LisH-domain protein interaction map reveals a Lis1-ARIH2-dynein regulatory axis. [PDF]
Gupta D, Maddika S.
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The Rab7-Epg5 and Rab39-ema modules cooperatively position autophagosomes for efficient lysosomal fusions. [PDF]
Boda A +9 more
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