ライフサイエンスコーパス: amelogenin

1 rinsically disordered EMPs, ameloblastin and amelogenin.

2 n of the enamel extracellular matrix protein amelogenin.

3 hydrophilic C terminus found in full-length amelogenin.

4 s significantly lower than that of wild-type amelogenin.

5 ally occurring splice variant of full-length amelogenin.

6 no direct interactions between fluoride and amelogenin.

7 e-linked immunosorbent assay (ELISA) kit for amelogenin.

8 onding to 4.7 A is present in nanoribbons of amelogenin.

9 ental epithelial cell differentiation marker amelogenin.

10 parameter in directing the self-assembly of amelogenins.

11 Da, 20-kDa, 13-kDa, 11-kDa, and 6-kDa (TRAP) amelogenins.

12 native amelogenin with one of two engineered amelogenins.

13 The expression profile of amelogenin, a known enamel-specific gene, was not altere

14 Furthermore, differences in amelogenin adsorption were observed among NBM, DFDBA, an

15 Without amelogenins, Ae2 could compensate for the pH drop associ

16 15 mV in the same pH range, indicating that amelogenin aggregation occurred when surface potentials

17 le for some of its clinical effects, or that amelogenin alone may not trigger the regenerative potent

18 We characterized 3 previously unidentified amelogenin alternatively spliced transcripts and demonst

19 To test this hypothesis, we generated amelogenin ( Amel) promoter-driven Ambn-transgenic mice,

20 ing normal tooth development Pitx2 activates Amelogenin (Amel) expression, whose product is required

21 ) mice: expression of the ameloblast markers amelogenin, ameloblastin, and enamelin was down-regulate

22 size and secrete the enamel matrix proteins (amelogenin, ameloblastin, and enamelin).

23 ild-type (WT) with those having mutations in amelogenin (Amelx) and matrix metalloproteinase-20 (Mmp2

24 Amelogenin (AMELX) and matrix metalloproteinase-20 (MMP2

25 Enamel from amelogenin (Amelx) null mice is hypoplastic and disorgan

26 c lines that expressed ameloblastin from the amelogenin (AmelX) promoter and identified transgenic li

27 f major tooth enamel matrix proteins (EMPs), amelogenin (AMELX), enamelin (ENAM), ameloblastin (AMBN)

28 ication of sex chromosome-linked isoforms of amelogenin, an enamel-forming protein, by nanoflow liqui

29 Recombinant human amelogenin and a purified 5-kDa protein fraction derived

30 Amelogenin and ameloblastin are 2 extracellular matrix p

31 calization images of N-terminal fragments of amelogenin and ameloblastin around the prism boundary re

32 We recently reported that amelogenin and ameloblastin colocalized during the secre

33 Amelogenin and ameloblastin expression is reduced and/or

34 ical analysis revealed accumulations of both amelogenin and ameloblastin in affected cells.

35 er demonstrated spatial interactions between amelogenin and ameloblastin N-terminal fragments.

36 Amelogenin and ameloblastin, the major enamel matrix pro

37 the role of fluoride in interactions between amelogenin and apatite crystals.

38 and kallikrein 4 (KLK4), are known to cleave amelogenin and are necessary for proper enamel formation

39 nteractions of a recombinant wild-type human amelogenin and its P41T mutant with recombinant human MM

40 ic system mainly composed of the full-length amelogenin and its proteolytic cleavage products.

41 1T mutation reduces the interactions between amelogenin and MMP20, leading to decreased degradation o

42 e effect of P41T on the interactions between amelogenin and MMP20, which may contribute to the format

43 Y-chromosome STR typing system consisting of amelogenin and three Y STR loci (DYS390, DYS393, DYS439)

44 We compared apatite binding affinity between amelogenins and their digest products during proteolysis

45 oth-specific genes that encode ameloblastin, amelogenin, and enamelin.

46 for dominant-negative activity for the P70T amelogenin, and for the robust nature of the process of

47 ping human tooth buds were immunostained for amelogenin, and mRNA was detected by in situ hybridizati

48 Amelogenin-apatite binding affinity was progressively re

49 f amelogenin by MMP-20 and then KLK4 reduces amelogenin-apatite interaction.

50 suggest that alterations in self-assembly of amelogenin are a consequence of destabilization of the i

51 Collagen and amelogenin are two major extracellular organic matrix pr

52 Amelogenins are a group of heterogenous proteins first i

53 Amelogenins are proteins formed by alternative splicing

54 Amelogenins are the most abundant protein species in for

55 The amelogenins are the most abundant secreted proteins in d

56 that upon oligomerization the C terminus of amelogenin (around residue Trp(161)) is exposed at the s

57 ere recorded for 15N- and 13C-labeled murine amelogenin as a function of increasing NaCl and CaCl2 co

58 rity was also increased by recombinant human amelogenin as indicated by a maximal score of 2.9 +/- 0.

59 Amelogenin assembled at pH 7.2 was also found to contain

60 We further show that amelogenin assemblies stabilize mineral prenucleation cl

61 d the interactions between collagen fibrils, amelogenin assemblies, and forming mineral in vitro, usi

62 attice alters the crystal surface to enhance amelogenin binding, with no direct interactions between

63 Amelogenin bound most abundantly to gelatin-coated cultu

64 ng enamel maturation, stepwise processing of amelogenin by MMP-20 and then KLK4 reduces amelogenin-ap

65 Stepwise processing of amelogenin by MMP-20 in the CS-AMEL hydrogel prevented u

66 d MMP20, leading to decreased degradation of amelogenin by MMP20, and resulting in AI.

67 lyzed the secondary structures of nanoribbon amelogenin by x-ray diffraction (XRD) and Fourier transf

68 f KO molar enamel, it was concluded that the amelogenin C-terminus is essential for proper enamel den

69 he interactions between collagen fibrils and amelogenin-calcium phosphate mineral complexes lead to o

70 Unprotonated amelogenins can bind protons, suggesting that amelogenin

71 h development, and that low-molecular-weight amelogenins can enhance pulp cell proliferation.

72 proteolysis, we used 2 different isoforms of amelogenin combined with the appropriate enzymes to anal

73 Amelogenins constitute the major portion of secretory en

74 Amelogenin constitutes 90% of the protein matrix in deve

75 ding, suggests that the unique properties of amelogenins containing exon4 cause a specific enhancemen

76 The temporal and spatial localization of amelogenins containing exon4 peptide, and their function

77 The findings have implications for amelogenin-controlled calcium phosphate mineralization i

78 melogenins can bind protons, suggesting that amelogenins could regulate the pH in enamel in situ.

79 that a hydrogel system composed of chitosan-amelogenin (CS-AMEL) and calcium phosphate is effective

80 gth native amelogenin, while the predominant amelogenin degradation product in developing enamel (e.g

81 we determined the spatiotemporal location of amelogenins derived from transcripts containing exon4 (A

82 tion of palatal fibroblasts with recombinant amelogenin did not alter expression of IL-11 and PRG4.

83 suggesting that these residues may initiate amelogenin dimerization, the first step in nanosphere as

84 he enamel extracellular matrix (EEM) protein amelogenin disrupts the secretory pathway in the enamel-

85 However, amelogenin does not have significant effects on PDL cell

86 e suggesting that mutations within conserved amelogenin domains could account for enamel variations p

87 The N- and C-terminal amelogenin domains in non-phosphorylated LRAP are, there

88 ggest that the 37-kDa isoform interacts with amelogenin during early tooth development.

89 o the CS-AMEL hydrogel to cleave full-length amelogenin during the growth of enamel-like crystals on

90 We propose that Mmp-20 alone processes amelogenin during the secretory stage.

91 To obtain structural insights into amelogenin during these early stages of enamel developme

92 lable on the structure or the orientation of amelogenin, either in solution or bound to hydroxyapatit

93 Using this protocol, we find that, although amelogenin exists primarily as ~26 nm in diameter nanosp

94 Of all the alternatively spliced forms of amelogenins, exon4 is most commonly spliced out.

95 Our aim was: to identify the mouse amelogenin exons 8/9 sequences; to investigate the poten

96 sence of the alternative spliced isoforms of amelogenin exons 8/9; and to immunolocalize proteins con

97 Conversion to amelogenin expressing dental epithelial cells involved a

98 ation and conversion of mesenchymal cells to amelogenin expressing epithelial cells via miR-200a.

99 mel formation, with decreased E-cadherin and amelogenin expression and increased noggin expression.

100 re/loxP recombination system to characterize amelogenin expression in C/EBPalpha conditional knock-ou

101 About 90% of amelogenin expression is from AMELX, which is nested wit

102 iously been shown to modestly participate in amelogenin expression, in vitro but found no significant

103 a mRNA levels; however, rather than ablating amelogenin expression, we observe wild-type amelogenin m

104 reduced in length and width and have reduced amelogenin expression.

105 s showed that the binding of the P41T mutant amelogenin for MMP20 was significantly lower than that o

106 ositively charged APS-treated mica surfaces, amelogenin forms a relatively uniform population of deca

107 Amelogenin forms into nanospheres in solution, while its

108 n peptide (LRAP) is an alternatively spliced amelogenin found in the developing enamel organ.

109 in vitro study provides further insight into amelogenin function, using variations of the Leucine-Ric

110 el-free biosensor for sensitive detection of Amelogenin gene (AMEL) using reduced graphene oxide modi

111 nt transactivator of the mouse X-chromosomal amelogenin gene acting at the C/EBPalpha cis-element loc

112 and NF-Y synergistically activate the mouse amelogenin gene and can contribute to its physiological

113 C/EBPalpha is implicated to regulate mouse amelogenin gene expression during tooth enamel formation

114 meloblast precursor cells and a reduction in amelogenin gene expression.

115 efect amelogenesis imperfecta resulting from amelogenin gene mutations.

116 Analyses of the mouse and rat amelogenin gene structures confirmed that exon 8 arose i

117 ing, such as gender identification where the amelogenin gene was used as a model target system, and d

118 oteins formed by alternative splicing of the amelogenin gene, and are essential for tooth enamel form

119 expression aspect of the regulation for the amelogenin gene.

120 xons 4-5 were present in the bovine or human amelogenin genes, suggesting that this translocation occ

121 In humans there are two, non-allelic amelogenin genes: AMELX (Xp22.3) and AMELY (Yp11.2).

122 At the center of the wound, neither EMD nor amelogenin had a significant wound-fill effect.

123 Individually, EMD and amelogenin had no significant effect on PDL cell prolife

124 The findings obtained show that amelogenin has intrinsic structural flexibility to accom

125 Since amelogenins have been ascribed cell-signaling activities

126 r results indicate that interactions between amelogenin hydrophilic C-terminal telopeptides are essen

127 Structural information of full-length amelogenin in either of these physiologically important

128 in is compatible with the known functions of amelogenin in enamel biomineralization, i.e., self-assem

129 binding that may be important in the role of amelogenin in enamel development.

130 In addition, FTIR analysis showed that amelogenin in the form of nanoribbons was comprised of b

131 later, the 37-kDa isoform co-localizes with amelogenin in Tomes' process and formative enamel, as re

132 yproline-type II (PPII) conformation in both amelogenins in addition to alpha-helix and unordered con

133 e functions of various alternatively spliced amelogenins in enamel formation are not well understood.

134 to elucidate the expression and function of amelogenins in the human dentin-pulp complex.

135 per enamel thickness and structure, and most amelogenins include a conserved hydrophilic C-terminus.

136 amel defects in both families were caused by amelogenin insufficiency, that deletion of AMELX results

137 r) technique to demonstrate ameloblastin and amelogenin interaction in the maturing mouse enamel.

138 cate that collagen fibrils guide assembly of amelogenin into elongated chain or filament-like structu

139 rarchical assembly of spherical particles of amelogenins into supramolecular structures of a higher o

140 The extended, labile conformation of rP172 amelogenin is compatible with the known functions of ame

141 Amelogenin is one of the key protein constituents respon

142 1 also activate the amelogenin promoter, and amelogenin is required for enamel formation and late sta

143 Amelogenin is soluble at low pH and self-assembles to fo

144 In forming enamel, amelogenin is the abundant protein that undergoes self-a

145 Amelogenin is the major protein component of the forming

146 Amelogenin is the predominant protein found during ename

147 scripts and demonstrated that exon-8-encoded amelogenin isoforms are processed by MMP-20.

148 We previously reported that amelogenin isoforms M180 and leucine-rich amelogenin pep

149 al and chloride content in incisor enamel of amelogenin-knockout (AmelX(-/-)) mice and determined the

150 ssociated with increased cementum defects in amelogenin-knockout (KO) mice.

151 major cleavage product (rP148), and a native amelogenin lacking both N- and C-termini (13k).

152 we generated transgenic mice that express an amelogenin lacking the C-terminal 13 amino acids (CTRNC)

153 porcine full length (rP172) and a truncated amelogenin lacking the hydrophilic C-terminal (rP148) we

154 asts express but fail to secrete full-length amelogenin leading to engorgement of the endoplasmic ret

155 est concentration of the biologically active amelogenin-leucine-rich amelogenin peptide and ameloblas

156 h, have in modulating the interaction of the amelogenin, LRAP, with hydroxyapatite (HAP).

157 nderstand the function of the 180-amino-acid amelogenin (M180), and to test the hypothesis that a sin

158 We conclude that among amelogenins, M180 alone is sufficient for normal enamel

159 generated AmelxKO/Mmp20KO (DKO) mice with an amelogenin (M180Tg) transgene.

160 Amelogenins make up a class of proteins associated with

161 The results suggest that unprotonated amelogenins may regulate the pH of forming enamel in sit

162 ggest that interactions between collagen and amelogenin might play an important role in the formation

163 e hypothesized that enamel proteases control amelogenin-mineral interaction, which, in turn can affec

164 ew insights into the potential importance of amelogenin-mineral interactions in enamel biomineralizat

165 st-like cells (LS8) were transfected with an amelogenin minigene to increase amelogenin synthesis, th

166 ess mineralized, possibly related to altered amelogenin-modulated crystal growth.

167 that the kinetics of nanochain formation of amelogenin molecules is well described by a combination

168 Extensive aggregation of amelogenin molecules with the particle size reaching abo

169 ed protocol for determining the size of both amelogenin monomers and oligomers.

170 ion, we manipulated the interactions between amelogenin monomers by altering pH, temperature, and pro

171 ns: higher-order assemblies of oligomers and amelogenin monomers, while on negatively charged bare mi

172 amelogenin expression, we observe wild-type amelogenin mRNA abundance levels.

173 BPalpha mRNA levels and coordinately altered amelogenin mRNA abundance.

174 RT-PCR analyses of amelogenin mRNA between control and Mmp20(-/-)mice revea

175 itu hybridization revealed a periodicity for amelogenin mRNA hybridization signals ranging from low t

176 was found in the forming dentin matrix, and amelogenin mRNA was localized in the dentin, presumably

177 pathogenesis associated with the p.Tyr64His amelogenin mutation involves ameloblast apoptosis induce

178 on of the secondary structure as a result of amelogenin mutations.

179 We propose that amelogenin nanoribbons template the growth of apatite mi

180 s and followed by the C-terminus, leading to amelogenin nanosphere assembly.

181 ther insight into the molecular mechanism of amelogenin nanosphere formation, we manipulated the inte

182 comprised of beta-sheets by up to 75%, while amelogenin nanospheres had predominantly random-coil str

183 lete lack of this domain is unable to rescue amelogenin null enamel.

184 When amelogenin-null (KO) and TgCTRNC transgenic mice were ma

185 ting that the C terminus is not critical for amelogenin oligomerization.

186 a successful attempt to identify the size of amelogenin oligomers and to directly monitor assembly an

187 concentration to create isolated metastable amelogenin oligomers.

188 The effects of recombinant amelogenins on pulp and papilla cell proliferation were

189 the activity was induced by BMP rather than amelogenin or other unknown proteins.

190 at native phosphorylated full-length porcine amelogenin (P173) and its predominant cleavage product (

191 Because transgenic full-length amelogenin partially rescues both density and volume of

192 With amelogenin PCR used for detecting the presence of a Y ch

193 e (P<0.001), and EMD alone, EMD+PDGF-BB, and amelogenin+PDGF-BB significantly increased PDL cell prol

194 growth factor-BB (PDGF-BB), EMD+PDGF-BB, or amelogenin+PDGF-BB.

195 at amelogenin isoforms M180 and leucine-rich amelogenin peptide (LRAP) are expressed in the periodont

196 Leucine-rich amelogenin peptide (LRAP) is an alternatively spliced am

197 mel regeneration and the use of leucine-rich amelogenin peptide (LRAP), a nonphosphorylated 56-amino

198 nction, using variations of the Leucine-Rich Amelogenin Peptide (LRAP), an alternative splice product

199 ion that in mice overexpressing leucine-rich amelogenin peptide (TgLRAP), in which ameloblasts differ

200 namel matrix derivative (EMD), tyrosine-rich amelogenin peptide (TRAP), and a synthetic proline-rich

201 biologically active amelogenin-leucine-rich amelogenin peptide and ameloblastin 17-kDa peptides.

202 blastin (Ambn-N) and the TRAP (tyrosine-rich amelogenin peptide) fragments.

203 The potential role of amelogenin phosphorylation in enamel formation is elucid

204 ium phosphate (ACP) - a capacity enhanced by amelogenin phosphorylation.

205 ns of either enamel matrix derivative (EMD), amelogenin, platelet-derived growth factor-BB (PDGF-BB),

206 th and used them to digest the tyrosine-rich amelogenin polypeptide (TRAP), the leucine-rich amelogen

207 Defective amelogenin post-secretory self-assembly and processing w

208 t of the time during alternative splicing of amelogenin pre-mRNA, a novel mature miRNA is generated f

209 we find that C/EBPdelta activates the mouse amelogenin promoter and synergistically cooperates with

210 is in vivo observation led us to examine the amelogenin promoter for the activity of transcription fa

211 Dlx2 and FoxJ1 also activate the amelogenin promoter, and amelogenin is required for enam

212 ter as well as Dlx2 and FoxJ1 binding to the amelogenin promoter.

213 ly inhibits PITX2 activation of the Dlx2 and amelogenin promoters.

214 logenin polypeptide (TRAP), the leucine-rich amelogenin protein (LRAP), and 5 fluorescence peptides.

215 odontoblasts actively synthesize and secrete amelogenin protein during human tooth development, and t

216 ation associated with absence of full-length amelogenin protein in the developing enamel matrix, loss

217 ditions that induce nanoribbon structures of amelogenin protein in vitro raises questions about their

218 Self-assembly of amelogenin protein into nanospheres has been recognized

219 It was concluded that a single amelogenin protein was able to significantly rescue the

220 Amelogenin protein was found in the forming dentin matri

221 The abundant amelogenin proteins are responsible for generating prope

222 Amelogenin proteins are secreted by ameloblasts within t

223 ication of molecular traits that classify 12 amelogenin proteins as members of the intrinsically diso

224 Furthermore, amelogenin proteins delivered by EMD liquid were able to

225 cleavage products are the most abundant non-amelogenin proteins in the enamel matrix of developing t

226 Analyses by TEM revealed that adsorption of amelogenin proteins were significantly farther from the

227 study was conducted to assess the effect of amelogenin proteolysis on calcium phosphate formation.

228 o investigate whether apatite affects normal amelogenin proteolysis, we used 2 different isoforms of

229 Studies focused on the native 20-kDa porcine amelogenin proteolytic cleavage product P148 that is pro

230 rity was also increased by recombinant human amelogenin raises the possibility that this 28.9-kDa pro

231 ormatics studies and confirm that one of the amelogenins, recombinant porcine rP172, exists in an ext

232 namics involving essentially the same set of amelogenin residues was observed.

233 nant mouse amelogenin (rM179) and C-terminal amelogenin, respectively.

234 orescence experiments with single tryptophan amelogenins revealed that upon oligomerization the C ter

235 rticles of the recombinant full-length human amelogenin (rH174) and two proteolytic products (rH163 a

236 Nanoribbons of recombinant human full-length amelogenin (rH174) are about 17 nm wide and self-align i

237 Recombinant human amelogenin (rh174) was bound to carbonated hydroxyapatit

238 illa cells was enhanced by recombinant human amelogenin rH72 (LRAP+ exon 4), while pulp cells respond

239 bodies against full-length recombinant mouse amelogenin (rM179) and C-terminal amelogenin, respective

240 ophysical properties of a recombinant murine amelogenin (rM180) and two point mutations identified fr

241 Amelogenin RNA transcripts undergo extensive alternative

242 pH-triggered assembly of recombinant porcine amelogenin rP172 and its interactions with mature hydrox

243 We used a recombinant amelogenin (rP172), a homolog of its major cleavage prod

244 Recombinant porcine amelogenins (rP172 and rP148) and three different mutant

245 f non-phosphorylated recombinant full-length amelogenin, rP172, a longer induction period was observe

246 Amelogenin's capacity to regulate enamel formation is re

247 ternative splice product comprised solely of amelogenin's N- and C-terminal domains.

248 Here we show compelling evidence that amelogenin self-assembles into an amyloid-like structure

249 Amelogenin self-assembles to form an extracellular prote

250 PPII conformation plays an important role in amelogenin self-assembly and that rP172 assembly is more

251 gain clearer insight into the mechanisms of amelogenin self-assembly, we first investigated the occu

252 interactions are the main driving force for amelogenin self-assembly.

253 Mutations in amelogenin sequence result in defective enamel, and the

254 Mmp-20 cleaves amelogenin sequences after Pro(162), Ser(148), His(62),

255 of proteolytic processing by MMP-20 affects amelogenin signaling and consequently alters amelogenin

256 t, all factors and their combinations except amelogenin significantly enhanced cell migration compare

257 teract with the developing matrix to provide amelogenin-specific protein to protein, protein to miner

258 ties and prism patterns, but that additional amelogenin splice products are required to restore ename

259 Of at least 16 different amelogenin splice products, the most abundant isoform fo

260 amelogenin signaling and consequently alters amelogenin splice site selection.

261 Conserved domains in amelogenin suggest their importance to biomineralization

262 new insights into the early events governing amelogenin supramolecular self-assembly have been identi

263 To date, a convincing link between amelogenin supramolecular structures and mature enamel h

264 escence showed that rH58 treatment increased amelogenin synthesis, but down-regulated Notch1 expressi

265 cted with an amelogenin minigene to increase amelogenin synthesis, the transfected cells synthesized

266 knockout mice, an in vivo model for reduced amelogenin synthesis, we found reduced miR-exon4, with n

267 genic strains that express the most abundant amelogenin (TgM180) have relatively normal enamel, but s

268 , but strains of mice that express a mutated amelogenin (TgP70T), which leads to amelogenesis imperfe

269 MD liquid + DFDBA adsorbed higher amounts of amelogenin than all other treatment modalities.

270 Regions of amelogenin that appear to be primarily random coil in th

271 ids and we identify a specific region within amelogenin that self-assembles into beta-sheets.

272 anger 2 (Ae2a,b), chloride channel Cftr, and amelogenins that can bind protons.

273 We hypothesized that without amelogenins the enamel would acidify unless ameloblasts

274 Amelogenin, the major extracellular enamel matrix protei

275 Amelogenin, the major extracellular matrix protein of de

276 Amelogenin, the major protein of forming dental enamel,

277 It is assumed that amelogenin, the most abundant protein in EMD, is the pro

278 ily focuses on the structure and function of amelogenin, the predominant enamel matrix protein.

279 e microscopy (AFM) study of self-assembly by amelogenin--the principal protein of the extracellular m

280 The binding affinity of amelogenin to apatite was found to be in the descending

281 Can both enzymes process amelogenin to generate the major cleavage products that

282 cific (13)C-, (15)N-labeled sample of murine amelogenin to provide insight into the structure of the

283 demonstrates a large variability of adsorbed amelogenin to the surface of bone grafting materials whe

284 The adsorption of amelogenin to the surface of grafting material varied su

285 56-amino acid alternative splice product of amelogenin, to regulate the shape and orientation of gro

286 rotein-protein interactions mediated via the amelogenin tri-tyrosyl motif are a key mechanistic facto

287 ography confirmed accumulation of 3H-labeled amelogenin trityrosyl motif peptide in the region of Tom

288 Since full-length amelogenin undergoes proteolysis by matrix metalloprotei

289 cryoelectron microscopy, we demonstrate that amelogenin undergoes stepwise hierarchical self-assembly

290 the evidence presented, that the full-length amelogenin uniquely regulates proper enamel formation th

291 urther compared binding affinity among the 3 amelogenins using a Langmuir model for protein adsorptio

292 We found that amelogenin was gradually degraded by MMP-20 in the prese

293 onditions of 2% acetic acid at pH 3.0, where amelogenin was monomeric.

294 The MMP-20 proteolysis of amelogenin was studied, and the morphology, composition,

295 art by the proteolysis of full-length native amelogenin, while the predominant amelogenin degradation

296 Amelogenin with a proline 41 to threonine mutation (P41T

297 sed gene targeting in mice to replace native amelogenin with one of two engineered amelogenins.

298 of this protein facilitates interactions of amelogenin with other macromolecules or with minerals fo

299 ondary structure and dynamics of full-length amelogenin within a nanosphere-gel and on the surface of

300 Assay of the Amelogenin Y gene (AMELY) on Yp is widely used in DNA-ba