ライフサイエンスコーパス: microfibril

1 alyses pointing toward an 18-chain cellulose microfibril.

2 rdered lattice constituting the core of each microfibril.

3 of type-I collagen within the context of the microfibril.

4 r xylan to the hydrophilic face of cellulose microfibrils.

5 rs, which are then secreted and assembled to microfibrils.

6 motetramers that are incorporated into mixed microfibrils.

7 ond to the hydrophilic surfaces of cellulose microfibrils.

8 zed the assembly of these into tetramers and microfibrils.

9 bule (CMT)-mediated orientation of cellulose microfibrils.

10 tein 1 and influence assembly of fibrillin 1 microfibrils.

11 of certain matrix polymers within cellulose microfibrils.

12 he pectin backbone, lodged between cellulose microfibrils.

13 s they most likely reflect nascent cellulose microfibrils.

14 es containing LTBP-3 with mutant fibrillin-1 microfibrils.

15 f the 10-12 nm diameter extracellular matrix microfibrils.

16 n the culture medium and no association with microfibrils.

17 of obstacles, like disintegration of chitin microfibrils.

18 extracellular matrix protein associated with microfibrils.

19 the hemicelluloses that tether to cellulose microfibrils.

20 TGFbeta large latent complex for binding to microfibrils.

21 AGP1) is a component of extracellular matrix microfibrils.

22 ng assays, rVN bound to isolated nondegraded microfibrils.

23 les and the orientation of nascent cellulose microfibrils.

24 g of (1-->4)-beta-glucan chains in cellulose microfibrils.

25 al interactions to enhance HA recruitment to microfibrils.

26 lin-1, the main constituent of extracellular microfibrils.

27 ically in mediating the recruitment of HA to microfibrils.

28 tories to orient newly synthesized cellulose microfibrils.

29 in limited regions of tight contact between microfibrils.

30 celluloses via binding to emerging cellulose microfibrils.

31 come into direct contact with the cellulose microfibrils.

32 1, which is a major structural component of microfibrils.

33 loosen noncovalent bonding between cellulose microfibrils.

34 tion of mutant fibrillin-1 incorporated into microfibrils.

35 lice variant was able to assemble into short microfibrils.

36 is a ubiquitous component of fibrillin-rich microfibrils.

37 thick fibrils and spots with densely packed microfibrils.

38 ll adhesion and as a structural component of microfibrils.

39 these proteins have been immunolocalized to microfibrils.

40 LTBP-1 and LTBP-4 are not incorporated into microfibrils.

41 -1, LTBP-1, and LTBP-4 are incorporated into microfibrils.

42 ress-induced deposition of aligned cellulose microfibrils.

43 he orientation of synthesis of the cellulose microfibrils.

44 le, by partially dissolving silk fibers into microfibrils.

45 egulate the fibrillin isoform composition of microfibrils.

46 atial scale of molecular connections between microfibrils.

47 olecule to align and to form well-structured microfibrils.

48 accumulates in the narrow spaces between the microfibrils.

49 be visualized in the context of the stiffer microfibrils.

50 ndle individual glucan chains into cellulose microfibrils.

51 ellulosic polysaccharide, binds to cellulose microfibrils.

52 iate the adsorption of mucilage to cellulose microfibrils.

53 lan onto the hydrophilic face of a cellulose microfibril (1-3) .

54 on three different models of Ibeta cellulose microfibrils, 18, 24, and 36 chains, to investigate thei

55 thickening and the orientation of cellulose microfibrils [2], our understanding of the composition o

56 ose polymer cellulose is assembled into long microfibrils a few nanometers in diameter.

57 from midribs were consistent with cellulose microfibril aggregation, and polarization microscopy rev

58 lastin, and proteins associated with elastic microfibrils, albeit miR-29b showed a stronger effect, p

59 re, including a slight increase in cellulose microfibril alignment along the growing stem.

60 ulose SFG spectrum is sensitive to cellulose microfibril alignment and packing within the cell wall.

61 cifically surrounded by abundant collagen VI microfibrils, an outcome accentuated by Down syndrome.

62 tween a hydrophobic surface of the cellulose microfibril and an aromatic motif on the expansin surfac

63 xes, which is a key determinate of cellulose microfibril and cell wall properties.

64 ment increased intracutaneous fibrillin-rich microfibril and collagen III deposition and decreased ma

65 d in vertebrates and have important roles in microfibril and elastic fiber structure, homeostasis, an

66 nterestingly, jia1 results in both cellulose microfibril and microtubule disorganization.

67 d by walls composed of crystalline cellulose microfibrils and a variety of matrix polymers.

68 Improved understanding of how fibrillin microfibrils and associated proteins regulated TGF-beta

69 fibrillin-2 epitopes are masked in postnatal microfibrils and can be revealed by enzymatic digestion

70 creating a dense matrix that binds cellulose microfibrils and crosslinks other wall components, there

71 ow that nonuniform distribution of cellulose microfibrils and demethylated pectin coincides with spat

72 Thus, alteration of MAGP-2, a component of microfibrils and elastic fibers, appears as an initiatin

73 e are deficient in extracellular collagen VI microfibrils and exhibit myopathic features, including d

74 establishing interactions between cellulose microfibrils and hemicelluloses.

75 beta-1,4-glucan chains that coalesce to form microfibrils and higher-ordered macrofibrils.

76 for KOR1 both in the synthesis of cellulose microfibrils and in the intracellular trafficking of CSC

77 , xyloglucan is thought to connect cellulose microfibrils and regulate their separation during wall e

78 polymers form an inner core within postnatal microfibrils and that microfibril structure evolves as g

79 length or quantity of a subset of cellulose microfibrils and that this, in turn, alters microfibril

80 ) C2a chain do not assemble efficiently into microfibrils and there is a severe collagen VI deficienc

81 rVN enhanced HA recruitment both to isolated microfibrils and to microfibrils in tissue sections in a

82 , our data identify MFAP4 as a new ligand of microfibrils and tropoelastin involved in proper elastic

83 Naked collagen microfibrils and weaker banded structure observed in the

84 association by coacervation, deposition onto microfibrils, and cross-linking to form elastic fibers.

85 omannan and xylan bind to the same cellulose microfibrils, and lignin is associated with both of thes

86 omain can be cleaved off after assembly into microfibrils, and the cleavage product has been implicat

87 es in individual polymer chains of cellulose microfibrils, and typically exhibit specificity for eith

88 l associations with wood density, stiffness, microfibril angle and ring width in a population of 1694

89 between the gene PgNAC8, wood stiffness and microfibril angle, as well as considerable within-season

90 possible role for Ca(2+) in stabilizing the microfibril architecture and moderating extension in viv

91 Fibrillin microfibrils are 10-12 nm diameter, extracellular matrix

92 hin the cell wall layers, and that cellulose microfibrils are highly anisotropic and have higher cond

93 ctron microscopy demonstrated that cellulose microfibrils are oriented in near longitudinal orientati

94 imary wall microfibril structure because its microfibrils are oriented with unusual uniformity, facil

95 Cellulose microfibrils are para-crystalline arrays of several doze

96 Fibrillin microfibrils are polymeric structures present in connect

97 Cellulose microfibrils are synthesized at the plasma membrane, whe

98 Plant cellulose microfibrils are synthesized by a process that propels t

99 Cellulose microfibrils are the major load-bearing component in pla

100 mplex that synthesizes an 18-chain cellulose microfibril as its fundamental product.

101 r, these findings identify the extracellular microfibrils as critical regulators of bone formation th

102 brillin strengthens the concept of fibrillin microfibrils as extracellular scaffolds integrating cell

103 ganize multiple linear glucose polymers into microfibrils as load-bearing wall components.

104 At present the mechanisms that regulate microfibril assembly are still to be elucidated.

105 there were differences in the secretion and microfibril assembly profiles of fibrillin-1 variants co

106 site at the C terminus to prevent premature microfibril assembly.

107 t the first hybrid domain is dispensable for microfibril assembly.

108 ecretion of collagen VI tetramers and during microfibril assembly.

109 These consist of KRT7/SCX+ cells expressing microfibril associated genes, PTX3+ cells co-expressing

110 rkers PTX3, CXCL1, CXCL6, CXCL8, and PDPN by microfibril associated tenocytes.

111 Microfibril-associated glycoprotein (MAGP) 1 and 2 are e

112 Microfibril-associated glycoprotein 1 (MAGP1) is a compo

113 Microfibril-associated glycoprotein-1 (MAGP-1) is a comp

114 sualized using antibodies to Fbn1, Fbn2, and microfibril-associated glycoprotein-1 (Magp1) in conjunc

115 ers caused by mutations in fibrillins and in microfibril-associated molecules.

116 Yet, microfibril-associated protein-1 (MAGP1)-rich ciliary zo

117 n microscopy, which revealed localization to microfibrils at the microscopic level.

118 ely our data demonstrated that extracellular microfibrils balance local catabolic and anabolic signal

119 alytic domain (CD) of Cel7B with a cellulose microfibril before and after complexing a glucan chain i

120 ndings suggest that ADAMTS10 participates in microfibril biogenesis rather than in fibrillin-1 turnov

121 ate, and the role of ADAMTS10 in influencing microfibril biogenesis was addressed.

122 otein which has been implicated in fibrillin microfibril biogenesis, cause ectopia lentis (EL) and EL

123 To investigate the role of ADAMTS10 in microfibril biogenesis, fetal bovine nuchal ligament cel

124 dded ADAMTS10 led to accelerated fibrillin-1 microfibril biogenesis.

125 syndrome (WMS), implicating it in fibrillin microfibril biology since some fibrillin-1 mutations als

126 so known as Magp2), which encodes an elastin-microfibril bridging factor, is upregulated in Fgfr3;4 m

127 an essential component for the formation of microfibril bundles in ciliary zonules.

128 brils merge into and out of short regions of microfibril bundles, thereby forming a reticulated netwo

129 e, and has similar rigidity to the cellulose microfibrils, but reverts to the threefold screw conform

130 thought to be largely dominated by cellulose microfibrils, but the mechanism leading to more complex

131 g the 20- to 40-nm spacing between cellulose microfibrils, but they do implicate a minor xyloglucan c

132 t success of in vitro synthesis of cellulose microfibrils by a single recombinant cellulose synthase

133 he AFM thus preferentially detects cellulose microfibrils by probing through the soft matrix in these

134 interaction between cellulose synthases and microfibrils, can maintain aligned cellulose synthase tr

135 major structural components of extracellular microfibrils, cause pleiotropic manifestations in Marfan

136 icellulose (HC) tethering with the cellulose microfibrils (CMFs) as one of the major load-bearing mec

137 ndicular to the net orientation of cellulose microfibrils (CMFs), which is in turn controlled by cort

138 hich in turn mediate deposition of cellulose microfibrils (CMFs).

139 coupling networks in Cel7B-glucan and Cel7B-microfibril complexes reveal a previously unresolved all

140 that mediates the synthesis of a fundamental microfibril composed of 18 glucan chains.

141 Our results show that wall loosening alters microfibril connectivity, enabling microfibril dynamics

142 The cellulose microfibril consists of bundles of linear beta-1,4-gluca

143 n of how many chains an elementary cellulose microfibril contains is critical to understanding the mo

144 The rigidity and orientation of these microfibrils control cell expansion; therefore, cellulos

145 Consistent with measurements of lower microfibril crystallinity, cellulose extracts from mutat

146 2 immunoreactivity can serve as a marker for microfibril degradation.

147 rid domain) in fibrillin-1 results in stable microfibrils, demonstrating that fibrillin-1 molecules a

148 ntact or defective surface structures on the microfibril, depending on the complexation state.

149 We previously showed that microfibril deposition requires fibronectin-induced foca

150 epithelial cell-cell junction formation, and microfibril deposition.

151 , the structural components of extracellular microfibrils, differentially regulate TGF-beta and bone

152 Microfibril direction within a lamella did not change gr

153 -ray diffraction, we show that the cellulose microfibrils displayed reduced width and an additional c

154 are often considered as spacers of cellulose microfibrils during growth.

155 ng alters microfibril connectivity, enabling microfibril dynamics not seen during mechanical stretch.

156 The cell wall consists of cellulose microfibrils embedded within a matrix of hemicellulose a

157 Microfibrils, enriched in Fbn2 and Magp1, were prominent

158 In conclusion, when microfibrils extend, there is a large molecular rearrang

159 Fibrillin microfibrils form the ocular zonule and are present in t

160 , linkage analysis, and imaging of cellulose microfibril formation using transmission electron micros

161 ESA) glycosyltransferases mediates cellulose microfibril formation.

162 ifference in glucan chain association during microfibril formation.

163 hat suggests a molecular basis for cellulose microfibril formation.

164 ng estimates of the diameter of the smallest microfibril formed from the beta-1,4 glucan chains synth

165 rculating fragments of fibrillin-1, or other microfibril fragments, are associated with TAA and disse

166 together with the fibrillins, contributes to microfibril function.

167 pe II arabinogalactans retained by cellulose microfibrils had a higher content of (methyl)glucuronic

168 plex and the number of cellulose chains in a microfibril have been debated for many years.

169 Fibrillin microfibrils have essential roles in elastic fiber forma

170 15), nanometre-scale movements of individual microfibrils have not been directly observed.

171 hat control the interactions among cellulose microfibrils, hemicelluloses, and lignin are still not w

172 timately binding to the surface of cellulose microfibrils in a semi-crystalline fashion.

173 It colocalizes to fibrillin-1 containing microfibrils in cultured fibroblasts and suppresses fibr

174 Disruption of microfibrils in fibrillin-1-deficient mice leads to frag

175 like matrix between stress-bearing cellulose microfibrils in growing plant cell walls.

176 localized ADAMTS10 to fibrillin-1-containing microfibrils in human tissues.

177 c lamellae and also display fragmentation of microfibrils in other tissues.

178 py is sensitive to the ordering of cellulose microfibrils in plant cell walls at the meso scale (nm t

179 ts the predominant hypothesis of twisting of microfibrils in plant primary cell walls.

180 of wall-degrading enzymes, removed cellulose microfibrils in superficial lamellae sequentially, layer

181 in vitro evidence excludes a direct role of microfibrils in supporting mineral deposition.

182 wall polymers that are retained by cellulose microfibrils in tension wood and normal wood of hybrid a

183 screw ribbon to bind intimately to cellulose microfibrils in the cell wall.

184 riented deposition of load-bearing cellulose microfibrils in the cell wall.

185 ADAMTSL4 colocalized with fibrillin-1 microfibrils in the ECM of these cells.

186 have significant interactions with cellulose microfibrils in the native primary wall.

187 iable, but still small, surface of cellulose microfibrils in the onion wall is tightly bound with ext

188 ed to function as a tether between cellulose microfibrils in the primary cell wall, limiting cell enl

189 at EMILIN-1 and -2 are targeted to fibrillin microfibrils in the skin.

190 Microfibrils in the thick lamellae are oriented almost p

191 lmost parallel to the fibre cell axis, while microfibrils in the thin lamellae are oriented almost pe

192 A role for fibrillin microfibrils in tissue elasticity has been implied by th

193 uitment both to isolated microfibrils and to microfibrils in tissue sections in a dose-dependent mann

194 ppresses fibrillin-2 (FBN2) incorporation in microfibrils, in part by transcriptional downregulation

195 Cross-lamellate networks of cellulose microfibrils influenced creep and tensile stiffness wher

196 rowth factor beta (TGFB) bioavailability and microfibril integrity.

197 he least characterized member of the elastin microfibril interface-located protein (EMILIN)/Multimeri

198 to interact with an intracellular domain of microfibril interface-located protein 1 (EMILIN 1), a me

199 Elastin microfibril interface-located proteins (EMILINs) 1 and 2

200 cellulose microfibril surfaces and to tether microfibrils into a load-bearing network, thereby playin

201 fibrillar networks with focal aggregation of microfibrils into PEX-like fibrils on stimulation with T

202 The assembly of collagen VI microfibrils is a multistep process in which proteolytic

203 reinforcement of the wall by stiff cellulose microfibrils is central to contemporary models of plant

204 Synthesis of 18-chain microfibrils is consistent with a model for cellulose-sy

205 osition of aggregated and helically oriented microfibrils is coupled to rapid and highly localized ce

206 The organization of cellulose microfibrils is critical for the strength and growth of

207 The interaction between xylan and cellulose microfibrils is important for secondary cell wall proper

208 The crystalline nature of cellulose microfibrils is one of the key factors influencing bioma

209 Assembly of fibrillin monomers into microfibrils is thought to occur at the cell surface, wi

210 as predigested with xyloglucanase, whereupon microfibril labelling was extensive.

211 llulose synthase complex rosette synthesizes microfibrils likely comprised of either 18 or 24 chains.

212 lecular assembly of VG1Fs in the HA-versican-microfibril macrocomplex has not yet been elucidated.

213 ly deposited wall surface showed that single microfibrils merge into and out of short regions of micr

214 ells by siRNA disrupted the formation of the microfibril meshwork by the cells.

215 TBP-2 in culture medium not only rescued the microfibril meshwork formation in LTBP2-suppressed cilia

216 its near-native state, with implications for microfibrils motions in different lamellae during uniaxi

217 These insights into microfibril movements and connectivities need to be inco

218 Microfibril movements during forced mechanical extension

219 ntation, we observed a diverse repertoire of microfibril movements that reveal the spatial scale of m

220 lanases capable of degrading the crystalline microfibrils of 1,3-xylan that reinforce the cell walls

221 ly divergent proteins that are components of microfibrils of the extracellular matrix.

222 nase-digested cell walls revealed an altered microfibril organization but did not yield clear evidenc

223 been shown to play a key role in controlling microfibril organization by guiding cellulose synthase c

224 ndary cell walls, but their biosynthesis and microfibril organization have not been examined.

225 ucanase in cellulose synthesis and cellulose microfibril organization in plants.

226 network, which leads to disordered cellulose microfibril organization in the cell wall.

227 o plant growth, cellulose content, cellulose microfibril organization, CSC dynamics and subcellular l

228 layers characterized by transverse cellulose microfibril orientation in both normal and compression w

229 and polarization microscopy revealed helical microfibril orientation only in wild type leaves.

230 wood cell walls, including lignification and microfibril orientation, may be mediated by changes in t

231 lationships with lignification and cellulose microfibril orientation.

232 0 nm thick, containing 3.5-nm wide cellulose microfibrils oriented in a common direction within a lam

233 rounded by a rigid wall made up of cellulose microfibrils, pectins, hemicelluloses, and lignin.

234 cused on how fibrillin-1 is organized within microfibril polymers.

235 tide blocks the assembly of fibrillin-1 into microfibrils produced by dermal fibroblasts; and (iii) t

236 Although passive microfibril reorientation during wall extension has been

237 N1 (encoding fibrillin-1, which forms tissue microfibrils), respectively, yet they are clinically ind

238 ation of elastic fibres requires a fibrillin microfibril scaffold for the deposition of elastin.

239 First, we develop a nematic silk microfibril solution, highly viscous and stable, by part

240 ations with hemicelluloses are important for microfibril spacing and for maintaining cell wall tensil

241 ith ADAMTS10 mutations deposited fibrillin-1 microfibrils sparsely compared with unaffected control c

242 II arabinogalactan are trapped by cellulose microfibrils specifically in tension wood and, thus, are

243 throughout development, and is essential for microfibril structural integrity.

244 e not required to be in perfect register for microfibril structure and function and that the first hy

245 A central question concerns the mechanism of microfibril structure and how this is linked to the cata

246 l model system for the study of primary wall microfibril structure because its microfibrils are orien

247 ns unclear whether modification of cellulose microfibril structure can be achieved genetically, which

248 core within postnatal microfibrils and that microfibril structure evolves as growth and development

249 CESA1(A903V) and CESA3(T942I) have modified microfibril structure in terms of crystallinity and sugg

250 microfibrils and that this, in turn, alters microfibril structure in the primary cell wall resulting

251 However, knowledge of microfibril structure is limited, largely due to their i

252 , these results suggest that perturbation of microfibril structure may underlie one of the major feat

253 er, while organization of the CSC determines microfibril structure, how individual CESA proteins are

254 1 cause disorders through primary effects on microfibril structure, two different mutations were gene

255 termine the role of fibrillin-2 in postnatal microfibril structure.

256 omplexity and tissue-specific differences in microfibril structure.

257 These results suggest that MAGP1-rich microfibrils support immune cell migration post-injury.

258 ypothesized to bind extensively to cellulose microfibril surfaces and to tether microfibrils into a l

259 Cellulose microfibrils, synthesized by plasma membrane-localized c

260 and -5, are components of the elastic fiber/microfibril system and are implicated in the formation a

261 commonly depicted as a scaffold of cellulose microfibrils tethered by xyloglucans.

262 extracellular glycoprotein fibrillin-1 forms microfibrils that act as the template for elastic fibers

263 omposite material containing stiff cellulose microfibrils that are embedded within a pectin matrix an

264 hains polymerized by CesA are assembled into microfibrils that are frequently bundled into macrofibri

265 ry elements and fibers are rich in cellulose microfibrils that are helically oriented and laterally a

266 glucan chains assembled into paracrystalline microfibrils that are synthesized by plasma membrane-loc

267 These chains form the microfibrils that confer the remarkable structural prope

268 reflection of helicoidally stacked cellulose microfibrils that form multilayers in the cell walls of

269 ted of a dense meshwork of radially oriented microfibrils that we termed the fibrillar girdle.

270 large matrix polymers retained by cellulose microfibrils that were specifically found in tension woo

271 ent of vertebrate extracellular matrix (ECM) microfibrils that, together with the fibrillins, contrib

272 on the orientation of crystalline cellulose microfibrils, their bonding to the polysaccharide matrix

273 s synthesize elastin and other components of microfibrils; these may serve structural roles, providin

274 ween the rosette structure and the cellulose microfibrils they synthesize.

275 pose that cleaved VG1Fs can be recaptured by microfibrils through VG1F homotypical interactions to en

276 ily of genes responsible for the assembly of microfibrils throughout development, and is essential fo

277 The importance of fibrillin microfibrils to connective tissue function has been demo

278 h was used to circumvent the insolubility of microfibrils to determine the role of fibrillin-2 in pos

279 of steps involved in the digestion of Abeta microfibrils to nanospheres or nanofilaments by protease

280 ll enlargement by restricting the ability of microfibrils to separate laterally.

281 ficiently "glued" the structural elements of microfibrils together, producing a unique inorganic-orga

282 the closed state, indicating that cellulose microfibrils undergo dynamic reorganization during stoma

283 age thickness and RMS roughness of cellulose microfibrils upon exposure to cellulolytic enzymes, prov

284 ich cell wall matrix embedded with cellulose microfibrils, we show that strong, circumferentially ori

285 pectroscopy, we show that celery collenchyma microfibrils were 2.9 to 3.0 nm in mean diameter, with a

286 Interestingly, cellulose microfibrils were disordered only in the epidermal cells

287 There was evidence that adjacent microfibrils were noncovalently aggregated together over

288 Several microfibrils were observed either inside or on the outer

289 ll surface obscured the underlying cellulose microfibrils when imaged by FESEM, but not by AFM.

290 llin-1 from being secreted or assembled into microfibrils, whereas MFS-associated substitutions in th

291 re viable models for an elementary cellulose microfibril, which also correlates with recent scatterin

292 ve pectin entrapment in or between cellulose microfibrils, which cannot be mimicked by in vitro bindi

293 SL4 influences the biogenesis of fibrillin-1 microfibrils, which compose the zonule.

294 this protease or its connection to fibrillin microfibrils, whose major component, fibrillin-1, is gen

295 bserved less densely packed fibrillin-1-rich microfibrils with irregular edges in the skin of individ

296 mulated peak shapes, calculated for 36-chain microfibrils with perfect order or uncorrelated disorder

297 due to the distinct orientation of cellulose microfibrils within the cell wall layers, and that cellu

298 of cellulose chains and their assembly into microfibrils within the cell walls of land plants and th

299 ke up its cellular structure, through to the microfibrils within the cell walls, down to the molecula

300 n four KC corneas showed the degeneration of microfibrils within the CFs and disturbance in the attac