戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

コーパス検索結果 (1語後でソート)

通し番号をクリックするとPubMedの該当ページを表示します
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                                              Amelogenin (AMELX) and matrix metalloproteinase-20 (MMP2
24 ild-type (WT) with those having mutations in amelogenin (Amelx) and matrix metalloproteinase-20 (Mmp2
25                                              Amelogenin (AMELX) is the predominant extracellular enam
26                                  Enamel from amelogenin (Amelx) null mice is hypoplastic and disorgan
27 c lines that expressed ameloblastin from the amelogenin (AmelX) promoter and identified transgenic li
28 f major tooth enamel matrix proteins (EMPs), amelogenin (AMELX), enamelin (ENAM), ameloblastin (AMBN)
29 ication of sex chromosome-linked isoforms of amelogenin, an enamel-forming protein, by nanoflow liqui
30 ealth Gene Technologies (China), multiplexes amelogenin and 22 autosomal STRs, 17 of which are non-CO
31                            Recombinant human amelogenin and a purified 5-kDa protein fraction derived
32                                              Amelogenin and ameloblastin are 2 extracellular matrix p
33 calization images of N-terminal fragments of amelogenin and ameloblastin around the prism boundary re
34                    We recently reported that amelogenin and ameloblastin colocalized during the secre
35                                              Amelogenin and ameloblastin expression is reduced and/or
36 ical analysis revealed accumulations of both amelogenin and ameloblastin in affected cells.
37 er demonstrated spatial interactions between amelogenin and ameloblastin N-terminal fragments.
38                                              Amelogenin and ameloblastin, the major enamel matrix pro
39 the role of fluoride in interactions between amelogenin and apatite crystals.
40 and kallikrein 4 (KLK4), are known to cleave amelogenin and are necessary for proper enamel formation
41 nteractions of a recombinant wild-type human amelogenin and its P41T mutant with recombinant human MM
42 ic system mainly composed of the full-length amelogenin and its proteolytic cleavage products.
43 1T mutation reduces the interactions between amelogenin and MMP20, leading to decreased degradation o
44 e effect of P41T on the interactions between amelogenin and MMP20, which may contribute to the format
45 Y-chromosome STR typing system consisting of amelogenin and three Y STR loci (DYS390, DYS393, DYS439)
46 We compared apatite binding affinity between amelogenins and their digest products during proteolysis
47 oth-specific genes that encode ameloblastin, amelogenin, and enamelin.
48  for dominant-negative activity for the P70T amelogenin, and for the robust nature of the process of
49                                              Amelogenin-apatite binding affinity was progressively re
50 f amelogenin by MMP-20 and then KLK4 reduces amelogenin-apatite interaction.
51 suggest that alterations in self-assembly of amelogenin are a consequence of destabilization of the i
52                                 Collagen and amelogenin are two major extracellular organic matrix pr
53                                              Amelogenins are a group of heterogenous proteins first i
54                                              Amelogenins are proteins formed by alternative splicing
55                                              Amelogenins are the most abundant protein species in for
56                                          The amelogenins are the most abundant secreted proteins in d
57  that upon oligomerization the C terminus of amelogenin (around residue Trp(161)) is exposed at the s
58 ere recorded for 15N- and 13C-labeled murine amelogenin as a function of increasing NaCl and CaCl2 co
59 rity was also increased by recombinant human amelogenin as indicated by a maximal score of 2.9 +/- 0.
60                                              Amelogenin assembled at pH 7.2 was also found to contain
61                         We further show that amelogenin assemblies stabilize mineral prenucleation cl
62 d the interactions between collagen fibrils, amelogenin assemblies, and forming mineral in vitro, usi
63 attice alters the crystal surface to enhance amelogenin binding, with no direct interactions between
64                                              Amelogenin bound most abundantly to gelatin-coated cultu
65 ng enamel maturation, stepwise processing of amelogenin by MMP-20 and then KLK4 reduces amelogenin-ap
66                       Stepwise processing of amelogenin by MMP-20 in the CS-AMEL hydrogel prevented u
67 mino acid variants slowed the degradation of amelogenin by MMP20 and inhibited the growth and phase t
68 d MMP20, leading to decreased degradation of amelogenin by MMP20, and resulting in AI.
69 lyzed the secondary structures of nanoribbon amelogenin by x-ray diffraction (XRD) and Fourier transf
70 f KO molar enamel, it was concluded that the amelogenin C-terminus is essential for proper enamel den
71 he interactions between collagen fibrils and amelogenin-calcium phosphate mineral complexes lead to o
72                                 Unprotonated amelogenins can bind protons, suggesting that amelogenin
73 h development, and that low-molecular-weight amelogenins can enhance pulp cell proliferation.
74 anding of how single amino acid variation in amelogenins can lead to malformed enamel.
75 proteolysis, we used 2 different isoforms of amelogenin combined with the appropriate enzymes to anal
76                                              Amelogenins constitute the major portion of secretory en
77                                              Amelogenin constitutes 90% of the protein matrix in deve
78 ding, suggests that the unique properties of amelogenins containing exon4 cause a specific enhancemen
79     The temporal and spatial localization of amelogenins containing exon4 peptide, and their function
80           The findings have implications for amelogenin-controlled calcium phosphate mineralization i
81 melogenins can bind protons, suggesting that amelogenins could regulate the pH in enamel in situ.
82  that a hydrogel system composed of chitosan-amelogenin (CS-AMEL) and calcium phosphate is effective
83 gth native amelogenin, while the predominant amelogenin degradation product in developing enamel (e.g
84 we determined the spatiotemporal location of amelogenins derived from transcripts containing exon4 (A
85 tion of palatal fibroblasts with recombinant amelogenin did not alter expression of IL-11 and PRG4.
86  suggesting that these residues may initiate amelogenin dimerization, the first step in nanosphere as
87 he enamel extracellular matrix (EEM) protein amelogenin disrupts the secretory pathway in the enamel-
88                                     However, amelogenin does not have significant effects on PDL cell
89 e suggesting that mutations within conserved amelogenin domains could account for enamel variations p
90                        The N- and C-terminal amelogenin domains in non-phosphorylated LRAP are, there
91 ggest that the 37-kDa isoform interacts with amelogenin during early tooth development.
92 o the CS-AMEL hydrogel to cleave full-length amelogenin during the growth of enamel-like crystals on
93       We propose that Mmp-20 alone processes amelogenin during the secretory stage.
94           To obtain structural insights into amelogenin during these early stages of enamel developme
95 lable on the structure or the orientation of amelogenin, either in solution or bound to hydroxyapatit
96 from other enamel matrix proteins, including amelogenin, enamelin, and amelotin.
97  Using this protocol, we find that, although amelogenin exists primarily as ~26 nm in diameter nanosp
98    Of all the alternatively spliced forms of amelogenins, exon4 is most commonly spliced out.
99                                Conversion to amelogenin expressing dental epithelial cells involved a
100 ation and conversion of mesenchymal cells to amelogenin expressing epithelial cells via miR-200a.
101 mel formation, with decreased E-cadherin and amelogenin expression and increased noggin expression.
102 re/loxP recombination system to characterize amelogenin expression in C/EBPalpha conditional knock-ou
103                                 About 90% of amelogenin expression is from AMELX, which is nested wit
104 iously been shown to modestly participate in amelogenin expression, in vitro but found no significant
105 a mRNA levels; however, rather than ablating amelogenin expression, we observe wild-type amelogenin m
106 reduced in length and width and have reduced amelogenin expression.
107 actosidase activity mimicking the endogenous amelogenin expression.
108 s showed that the binding of the P41T mutant amelogenin for MMP20 was significantly lower than that o
109 ositively charged APS-treated mica surfaces, amelogenin forms a relatively uniform population of deca
110                                              Amelogenin forms into nanospheres in solution, while its
111 n peptide (LRAP) is an alternatively spliced amelogenin found in the developing enamel organ.
112 in vitro study provides further insight into amelogenin function, using variations of the Leucine-Ric
113 el-free biosensor for sensitive detection of Amelogenin gene (AMEL) using reduced graphene oxide modi
114 nt transactivator of the mouse X-chromosomal amelogenin gene acting at the C/EBPalpha cis-element loc
115  and NF-Y synergistically activate the mouse amelogenin gene and can contribute to its physiological
116   C/EBPalpha is implicated to regulate mouse amelogenin gene expression during tooth enamel formation
117 meloblast precursor cells and a reduction in amelogenin gene expression.
118 efect amelogenesis imperfecta resulting from amelogenin gene mutations.
119                Analyses of the mouse and rat amelogenin gene structures confirmed that exon 8 arose i
120 ing, such as gender identification where the amelogenin gene was used as a model target system, and d
121 oteins formed by alternative splicing of the amelogenin gene, and are essential for tooth enamel form
122 xons 4-5 were present in the bovine or human amelogenin genes, suggesting that this translocation occ
123         In humans there are two, non-allelic amelogenin genes: AMELX (Xp22.3) and AMELY (Yp11.2).
124  At the center of the wound, neither EMD nor amelogenin had a significant wound-fill effect.
125              The findings obtained show that amelogenin has intrinsic structural flexibility to accom
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 predominant protein found during ename
146                In particular, protein AMELY (amelogenin isoform Y) is present in the enamel dental ti
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 hat both recombinant and enamel-tissue-based amelogenin nanoribbons are capable of guiding fibrous ap
180                              We propose that amelogenin nanoribbons template the growth of apatite mi
181 s and followed by the C-terminus, leading to amelogenin nanosphere assembly.
182 ther insight into the molecular mechanism of amelogenin nanosphere formation, we manipulated the inte
183 comprised of beta-sheets by up to 75%, while amelogenin nanospheres had predominantly random-coil str
184 lete lack of this domain is unable to rescue amelogenin null enamel.
185                                         When amelogenin-null (KO) and TgCTRNC transgenic mice were ma
186 ting that the C terminus is not critical for amelogenin oligomerization.
187 a successful attempt to identify the size of amelogenin oligomers and to directly monitor assembly an
188  concentration to create isolated metastable amelogenin oligomers.
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  growth factor-BB (PDGF-BB), EMD+PDGF-BB, or amelogenin+PDGF-BB.
194 at amelogenin isoforms M180 and leucine-rich amelogenin peptide (LRAP) are expressed in the periodont
195                                 Leucine-rich amelogenin peptide (LRAP) is an alternatively spliced am
196 mel regeneration and the use of leucine-rich amelogenin peptide (LRAP), a nonphosphorylated 56-amino
197 nction, using variations of the Leucine-Rich Amelogenin Peptide (LRAP), an alternative splice product
198 ion that in mice overexpressing leucine-rich amelogenin peptide (TgLRAP), in which ameloblasts differ
199 namel matrix derivative (EMD), tyrosine-rich amelogenin peptide (TRAP), and a synthetic proline-rich
200  biologically active amelogenin-leucine-rich amelogenin peptide and ameloblastin 17-kDa peptides.
201 blastin (Ambn-N) and the TRAP (tyrosine-rich amelogenin peptide) fragments.
202                        The potential role of amelogenin phosphorylation in enamel formation is elucid
203 ium phosphate (ACP) - a capacity enhanced by amelogenin phosphorylation.
204 ns of either enamel matrix derivative (EMD), amelogenin, platelet-derived growth factor-BB (PDGF-BB),
205 th and used them to digest the tyrosine-rich amelogenin polypeptide (TRAP), the leucine-rich amelogen
206                                    Defective amelogenin post-secretory self-assembly and processing w
207 t of the time during alternative splicing of amelogenin pre-mRNA, a novel mature miRNA is generated f
208  we find that C/EBPdelta activates the mouse amelogenin promoter and synergistically cooperates with
209             Dlx2 and FoxJ1 also activate the amelogenin promoter, and amelogenin is required for enam
210 ter as well as Dlx2 and FoxJ1 binding to the amelogenin promoter.
211 ly inhibits PITX2 activation of the Dlx2 and amelogenin promoters.
212 logenin polypeptide (TRAP), the leucine-rich amelogenin protein (LRAP), and 5 fluorescence peptides.
213 ample, a change in one amino acid within the amelogenin protein can lead to drastic changes in enamel
214 odontoblasts actively synthesize and secrete amelogenin protein during human tooth development, and t
215 ation associated with absence of full-length amelogenin protein in the developing enamel matrix, loss
216 ditions that induce nanoribbon structures of amelogenin protein in vitro raises questions about their
217 , we exploited the dimorphic features of the amelogenin protein to determine the sex of the so-called
218               It was concluded that a single amelogenin protein was able to significantly rescue the
219                                              Amelogenin protein was found in the forming dentin matri
220                                 The abundant amelogenin proteins are responsible for generating prope
221                                              Amelogenin proteins are secreted by ameloblasts within t
222 ication of molecular traits that classify 12 amelogenin proteins as members of the intrinsically diso
223                                 Furthermore, amelogenin proteins delivered by EMD liquid were able to
224  cleavage products are the most abundant non-amelogenin proteins in the enamel matrix of developing t
225  Analyses by TEM revealed that adsorption of amelogenin proteins were significantly farther from the
226  study was conducted to assess the effect of amelogenin proteolysis on calcium phosphate formation.
227 o investigate whether apatite affects normal amelogenin proteolysis, we used 2 different isoforms of
228 Studies focused on the native 20-kDa porcine amelogenin proteolytic cleavage product P148 that is pro
229 rity was also increased by recombinant human amelogenin raises the possibility that this 28.9-kDa pro
230 ormatics studies and confirm that one of the amelogenins, recombinant porcine rP172, exists in an ext
231 namics involving essentially the same set of amelogenin residues was observed.
232 nant mouse amelogenin (rM179) and C-terminal amelogenin, respectively.
233 orescence experiments with single tryptophan amelogenins revealed that upon oligomerization the C ter
234 rticles of the recombinant full-length human amelogenin (rH174) and two proteolytic products (rH163 a
235 Nanoribbons of recombinant human full-length amelogenin (rH174) are about 17 nm wide and self-align i
236                            Recombinant human amelogenin (rh174) was bound to carbonated hydroxyapatit
237 illa cells was enhanced by recombinant human amelogenin rH72 (LRAP+ exon 4), while pulp cells respond
238 bodies against full-length recombinant mouse amelogenin (rM179) and C-terminal amelogenin, respective
239 ophysical properties of a recombinant murine amelogenin (rM180) and two point mutations identified fr
240                                              Amelogenin RNA transcripts undergo extensive alternative
241 pH-triggered assembly of recombinant porcine amelogenin rP172 and its interactions with mature hydrox
242                        We used a recombinant amelogenin (rP172), a homolog of its major cleavage prod
243                          Recombinant porcine amelogenins (rP172 and rP148) and three different mutant
244 f non-phosphorylated recombinant full-length amelogenin, rP172, a longer induction period was observe
245                                              Amelogenin's capacity to regulate enamel formation is re
246 ternative splice product comprised solely of amelogenin's N- and C-terminal domains.
247 rystal growth was achieved by interaction of amelogenin scaffolds with acidic macromolecules that fac
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 at altering one amino acid within the murine amelogenin sequence (natural variants T21 and P41T, and
254                                 Mutations in amelogenin sequence result in defective enamel, and the
255                               Mmp-20 cleaves amelogenin sequences after Pro(162), Ser(148), His(62),
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                         Conserved domains in amelogenin suggest their importance to biomineralization
261 new insights into the early events governing amelogenin supramolecular self-assembly have been identi
262           To date, a convincing link between amelogenin supramolecular structures and mature enamel h
263 escence showed that rH58 treatment increased amelogenin synthesis, but down-regulated Notch1 expressi
264 cted with an amelogenin minigene to increase amelogenin synthesis, the transfected cells synthesized
265  knockout mice, an in vivo model for reduced amelogenin synthesis, we found reduced miR-exon4, with n
266 genic strains that express the most abundant amelogenin (TgM180) have relatively normal enamel, but s
267 , but strains of mice that express a mutated amelogenin (TgP70T), which leads to amelogenesis imperfe
268 MD liquid + DFDBA adsorbed higher amounts of amelogenin than all other treatment modalities.
269                                   Regions of amelogenin that appear to be primarily random coil in th
270 ids and we identify a specific region within amelogenin that self-assembles into beta-sheets.
271 anger 2 (Ae2a,b), chloride channel Cftr, and amelogenins that can bind protons.
272                 We hypothesized that without amelogenins the enamel would acidify unless ameloblasts
273                                              Amelogenin, the major extracellular enamel matrix protei
274                                              Amelogenin, the major extracellular matrix protein of de
275                                              Amelogenin, the major protein of forming dental enamel,
276                           It is assumed that amelogenin, the most abundant protein in EMD, is the pro
277 ily focuses on the structure and function of amelogenin, the predominant enamel matrix protein.
278 e microscopy (AFM) study of self-assembly by amelogenin--the principal protein of the extracellular m
279                      The binding affinity of amelogenin to apatite was found to be in the descending
280                     Can both enzymes process amelogenin to generate the major cleavage products that
281 cific (13)C-, (15)N-labeled sample of murine amelogenin to provide insight into the structure of the
282 demonstrates a large variability of adsorbed amelogenin to the surface of bone grafting materials whe
283                            The adsorption of amelogenin to the surface of grafting material varied su
284  56-amino acid alternative splice product of amelogenin, to regulate the shape and orientation of gro
285 rotein-protein interactions mediated via the amelogenin tri-tyrosyl motif are a key mechanistic facto
286 ography confirmed accumulation of 3H-labeled amelogenin trityrosyl motif peptide in the region of Tom
287                            Since full-length amelogenin undergoes proteolysis by matrix metalloprotei
288 cryoelectron microscopy, we demonstrate that amelogenin undergoes stepwise hierarchical self-assembly
289 urther compared binding affinity among the 3 amelogenins using a Langmuir model for protein adsorptio
290 binant analog of a MMP20-cleavage product of amelogenin was capable of guiding apatite mineralization
291                                We found that amelogenin was gradually degraded by MMP-20 in the prese
292 onditions of 2% acetic acid at pH 3.0, where amelogenin was monomeric.
293                    The MMP-20 proteolysis of amelogenin was studied, and the morphology, composition,
294 art by the proteolysis of full-length native amelogenin, while the predominant amelogenin degradation
295                                              Amelogenin with a proline 41 to threonine mutation (P41T
296 sed gene targeting in mice to replace native amelogenin with one of two engineered amelogenins.
297  of this protein facilitates interactions of amelogenin with other macromolecules or with minerals fo
298 ondary structure and dynamics of full-length amelogenin within a nanosphere-gel and on the surface of
299  locus of the mouse ameloblast-specific gene amelogenin X (Amelx-iCre) with a large (250-kb) bacteria
300                                 Assay of the Amelogenin Y gene (AMELY) on Yp is widely used in DNA-ba

 
Page Top