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1 at least one ligand in extracellular matrix (type I procollagen).
2 omplex involved in prolyl 3-hydroxylation in type I procollagen.
3 RNA, but markedly increased the half-life of type I procollagen.
4 nd showed a 3-fold increase in intracellular type I procollagen.
5  RNA expression, secretion, or processing of type I procollagen.
6  by TGF-beta, thereby reducing expression of type I procollagen.
7 both propeptide chains that constitute human type I procollagen.
8 ne the association profile between Hsp47 and type I procollagen.
9 lagenase, respectively) and synthesized less type I procollagen (36 and 88% reduction, respectively,
10                                              Type I procollagen accumulates in the Golgi of fibroblas
11 revealed less fibrosis and less staining for type I procollagen after imatinib mesylate treatment, bu
12 for the prominence of a homotrimeric form of type I procollagen (alpha1 trimer) during vertebrate dev
13 gen telopeptide, aminoterminal propeptide of type I procollagen, aminoterminal propeptide of type III
14 ls was further examined by colocalization of type I procollagen and bromodeoxyuridine labeling to act
15 vated CYR61 expression substantially reduces type I procollagen and concurrently increases matrix met
16                       These cells synthesize type I procollagen and degrade it intracellularly; howev
17 hetic activity manifested by the presence of type I procollagen and elastin at 3 months after injury.
18 n that binds the COOH-terminal propeptide of type I procollagen and potentiates its cleavage by proco
19 ng growth factor-beta pathway, which reduced type I procollagen and raised MMP-1 expression.
20                                Tropoelastin, type I procollagen and TGF-beta gene expression, and ang
21 ively during posttranslational maturation of type I procollagen and that FKBP65 and HSP47 but fail to
22 enuates UV irradiation-induced inhibition of type-I procollagen and upregulation of MMP-1.
23 pplement to obtain high expression levels of type I procollagen as heat-stable heterotrimers in Sacch
24 rmal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
25 onitors the integrity of the triple helix of type I procollagen at the ER/cis-Golgi boundary and, whe
26 is study, we first searched for mutations in type I procollagen by analyses of protein and mRNA in fi
27 monstrated by a lower in vitro production of type I procollagen by dermal fibroblasts isolated from s
28 n that potentiates enzymatic cleavage of the type I procollagen C-propeptide by bone morphogenetic pr
29 nces the enzymatic activity that cleaves the type I procollagen C-propeptide, was previously mapped t
30 rphogenetic protein-1 (BMP-1), also known as type I procollagen C-proteinase ().
31 no-acid protein that has 43% identity to the Type I procollagen C-proteinase enhancer protein (PCOLCE
32 cleotide sequences homologous to that of the type I procollagen C-proteinase enhancer protein (PCPE)
33                                A novel human Type I procollagen C-proteinase enhancer protein-like ge
34 but rather in the most C-terminal domains of type I procollagen chains.
35  genes SERPINH1 and FKBP10, which encode the type I procollagen chaperones HSP47 and FKBP65, respecti
36 lants of MSFs from transgenic mice harboring type I procollagen-chloramphenicol acetyltransferase con
37 radiation from the sun reduces production of type I procollagen (COLI), the major structural protein
38 lse-chase experiments, the newly synthesized type I procollagen, composed of pro alpha 1(I) and pro a
39          The carboxyl-terminal propeptide of type I procollagen (CPP-I) plays a key role in regulatio
40 NA is shown to differ from that of BMP-1 and type I procollagen during mouse development, consistent
41 layer; medium fractions showed no detectable type I procollagen during the entire 120-minute chase.
42 a coordinate decrease in CTGF, TGF-beta, and type I procollagen expression and content.
43 -beta/Smad/CTGF axis likely mediates reduced type I procollagen expression in aged human skin in vivo
44  irradiation and precedes down-regulation of type I procollagen expression in human skin in vivo.
45 ata indicate that in human skin fibroblasts, type I procollagen expression is dependent on endogenous
46  contrast, overexpression of CTGF stimulated type I procollagen expression, and increased promoter ac
47 coincident temporal and spatial overlap with type I procollagen expression, implicating this cytokine
48 hibitory Smad7 abolished CTGF stimulation of type I procollagen expression.
49    Repeated UV-A1 exposures did not suppress type I procollagen expression.
50                                Regulation of type I procollagen gene (COL1A2) transcription by TGF-be
51  from the same individuals were assessed for type I procollagen gene expression by in situ hybridizat
52                                  We examined type I procollagen gene expression in human atherosclero
53 expression protects against UV inhibition of type I procollagen gene expression in human skin fibrobl
54  marked suppression of lung tropoelastin and type I procollagen gene expression in the presence of AC
55  did not alter matrix metalloproteinase 1 or type I procollagen gene expression.
56  cases result from dominant mutations in the type I procollagen genes, but mutations in a growing num
57                     The folding mechanism of type I procollagen has been well characterized, and prot
58 tide, is essential for efficient assembly of type I procollagen heterotrimers.
59      This study shows that MAGP-2 stabilizes type I procollagen, identifying an important function of
60 cient for correct assembly and processing of type I procollagen in a eucaryotic system that does not
61 his was followed by a sustained synthesis of type I procollagen in neointima beginning at 7 days and
62 sed for 120 minutes demonstrated no trace of type I procollagen in the cell layer; medium fractions s
63 s and release both C- and N-propeptides from type I procollagen in vitro and in vivo and contribute t
64 g activity against Chordin, probiglycan, and type I procollagen in vitro.
65                                              Type I procollagen is a heterotrimer composed of two pro
66                        Reduced production of type I procollagen is a prominent feature of chronologic
67       Compared with atherosclerotic plaques, type I procollagen is increased and MMP-1 is decreased i
68  individual and a population of the secreted type I procollagen is protease sensitive.
69 howed that exogenously added Sfrp2 inhibited type I procollagen maturation in primary cardiac fibrobl
70       MAGP-2 overexpression had no effect on type I procollagen messenger RNA, but markedly increased
71                              Assembly of the type I procollagen molecule begins with interactions amo
72 ral part, and near the C terminus) along the type I procollagen molecule for both A-domains.
73 erely affected infant make some overmodified type I procollagen molecules.
74 d by immunohistochemistry) and expression of type I procollagen mRNA (detected by in situ hybridizati
75 tic lesions (< 1.5 years) contained abundant type I procollagen mRNA but little immunoreactive MMP-1
76                    In situ hybridization for type I procollagen mRNA displayed increased gene express
77                                              Type I procollagen mRNA expression was demonstrated in m
78 CTGF substantially reduced the expression of type I procollagen mRNA, protein, and promoter activity.
79 eactive MMP-1 and TIMP-1 as well as abundant type I procollagen mRNA.
80 mutations in the COL1A1 and COL1A2 genes for type I procollagen, mutations have been difficult to det
81 function of the NH(2)-terminal propeptide of type I procollagen (N-propeptide) is poorly understood.
82 let-derived growth factor A (p = 0.033), and Type I procollagen (p = 0.096) were lower; and IFN-gamma
83 sslinks [CTX], and N-terminal propeptides of type I procollagen [P1NP]) markers were measured.
84 BAL), fluid we investigated the synthesis of type I procollagen (PICP) and type I/II collagen degrada
85     Levels of serum C-terminal propeptide of type I procollagen (PICP) were significantly higher in m
86                     N-terminal propeptide of type I procollagen (PINP) and C-telopeptide of type I co
87 on triple helix formation, human recombinant type I procollagen, pN-collagen (procollagen without the
88 pro alpha1(III)] and the pro alpha2 chain of type I procollagen [pro alpha2(I)] as examples of procol
89              CRT(-/-) MEFs also have reduced type I procollagen processing and deposition into the ex
90 t high concentration inhibited human and rat type I procollagen processing by Bmp1 in vitro.
91  as a stable heterotrimeric helix similar to type I procollagen produced in tissue culture.
92                          cAMP also increased type I procollagen production and gene expression of mat
93 of human dermal fibroblasts and no effect on type I procollagen production by these cells.
94 pathway and the impact of this impairment on type I procollagen production in human skin fibroblasts,
95        In the present study, we investigated type I procollagen production in photodamaged and sun-pr
96         We next investigated whether reduced type I procollagen production was because of inherently
97 ; interstitial collagenase) were reduced and type I procollagen production was increased.
98 ion of TbetaRII, with attendant reduction of type I procollagen production, is a critical molecular m
99 e similar in their capacities for growth and type I procollagen production; and 2) the accumulation o
100 nhibitor of metalloproteinases 2, C-terminal type I procollagen propeptide (PICP), and the immature c
101  expression by in situ hybridization and for type I procollagen protein by immunostaining.
102 gen-alpha 1(I) transcripts and intracellular type I procollagen protein increased in the adventitia w
103  and produced virtually identical amounts of type I procollagen protein.
104 OL1A1 and COL1A2, which encode the chains of type I procollagen, result in dominant forms of OI, and
105  the activity of FKBP65 has several effects: type I procollagen secretion is slightly delayed, the st
106 likely reflect a diminished amount of normal type I procollagen, small populations of overmodified he
107 and is associated with a marked reduction in type I procollagen synthesis and impairment in adhesion.
108                The interaction of Hsp47 with type I procollagen synthesis in CECs was also studied.
109 -beta/Smad pathway is the major regulator of type I procollagen synthesis in human skin.
110     These findings indicate that the lack of type I procollagen synthesis in sun-damaged skin is not
111                             UV inhibition of type I procollagen synthesis is mediated in part by c-Ju
112 ctions of transforming growth factor beta on type I procollagen synthesis.
113 ithin photodamaged skin act to down-regulate type I procollagen synthesis.
114 nhibit, by an as yet unidentified mechanism, type I procollagen synthesis.
115 he collagenous extracellular matrix regulate type I procollagen synthesis.
116    PICP was measured by ELISA as a marker of type I procollagen synthesis.
117                            Langerin bound to type I procollagen that was immunoprecipitated from fibr
118 th HFpEF and higher C-terminal propeptide of type I procollagen values also had higher mean pulmonary
119 lloproteinase-2 and C-terminal propeptide of type I procollagen values than hypertensive controls.
120               Immunohistochemistry indicated type I procollagen was being expressed by an alpha-smoot
121        Subcellular localization of Hsp47 and type I procollagen was determined by immunofluorescent s
122                       Within the parenchyma, type I procollagen was expressed uniquely within granulo
123                                              Type I procollagen was found to be associated with Hsp47
124                                              Type I procollagen was produced as a stable heterotrimer
125 se inhibitor 1, and C-terminal propeptide of type I procollagen were determined in 28 patients with H
126                                 They express type I procollagen, with some of them translocating to t
127 ility and post-translational modification of type I procollagen, without which bone mass and quality

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