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1 e organized from the perinuclear ring as the manchette.
2 ent mice, SPAG16L no longer localizes to the manchette.
3  indicating that PACRG recruits MEIG1 to the manchette.
4 ission electron microscopy revealed that the manchette, a microtubular organelle essential for sperm
5 cell bodies, but the protein migrates to the manchette, a unique structure at the base of elongating
6 ined by electrophoretic fractionation of rat manchette and epidermis footpad proteins.
7 uch as the Sertoli cell microtubules and the manchette and flagellum microtubules of the spermatids,
8 b is required for sperm head shaping via the manchette and proper flagellum formation.
9 ion of Sept10 in sperm, indicating defective manchette and sperm annulus formation.
10 rate that MEIG1/PACRG forms a complex in the manchette and that this complex is necessary to transpor
11 on microscopy revealed abnormal acrosome and manchette and the absence of implantation fossa at the c
12  cytoplasmic microtubules, mitotic spindles, manchette, and axonemes of sperm flagella.
13 ron microscopy demonstrate that fractionated manchettes are relatively intact.
14 2-kDa protein in the perinuclear ring of the manchette as well as in keratinocytes of the suprabasal
15              The protein is recruited to the manchette at a late stage of spermatogenesis.
16 c antibodies to alpha-tubulins show that the manchette contains acetylated, tyrosinated, glutamylated
17 s and to the perinuclear ring from which the manchette emerges.
18 a major component of the perinuclear ring of manchettes fractionated from rat spermatids.
19 en developed for the fractionation of intact manchettes from rat spermatids.
20 n addition, MEIG1 no longer localizes to the manchette in the remaining elongating spermatids of Pacr
21                                          The manchette is a transient structure that develops during
22                                          The manchette is a unique structure only present in male ger
23 somes, centrosome nuclear binding, transient manchette microtubule assembly for nuclear shaping, asso
24 cyte cytoplasm of wild-type mice, and in the manchette of elongating spermatids, but in the Meig1 or
25 n is a component the perinuclear ring of the manchette of rat spermatids.
26 st, MEIG1 and PACRG are still present in the manchette of Spag16L-deficient mice, indicating that SPA
27  mutant were morphologically abnormal in the manchette of spermatids and in Sertoli cells.
28                                    The sperm manchette plays a critical scaffolding function during n
29 ering enzymes KATNAL2 and KATNB1 to regulate manchette remodeling and shape the sperm head.
30 aps of silver-stained proteins of the intact manchette show four predominant proteins: alpha- and bet
31 ical role for the MEIG1/PARCG partnership in manchette structure and function and the control of sper
32 all microtubule-based organelles such as the manchette, the head-tail coupling apparatus (HTCA), and
33 , which is equivalent to the mammalian sperm manchette, to the centriolar adjunct and acrosomal cap d
34 calizes with alpha-tubulin, a marker for the manchette, whereas this localization was not changed in
35 rated by a microtubular structure termed the manchette, which attaches to the perinuclear ring of the
36 developed procedure for the fractionation of manchettes will facilitate a direct characterization of