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1 ater than 50% reduction in the production of type II procollagen and a similar decrease in the corres
2 pe IIB NH2-propeptide and all other forms of type II procollagens and mature collagen did not react w
3 P and an interaction between mutant COMP and type II procollagen are initiating events in the assembl
4 ide from cleavage of CI and CII [C1,2C], and type II procollagen carboxy-propeptide [CPII] in serum,
5 irds of families linked to the gene encoding type II procollagen (COL2A1).
6 recombinant system was used to prepare human type II procollagen containing the substitution of Cys f
7  type IIA collagen (PIIANP), C-propeptide of type II procollagen (CPII), and type II collagen neoepit
8  matrix organization was identified in which type II procollagen formed a central core surrounded by
9                  Alternative splicing of the type II procollagen gene (COL2A1) is developmentally reg
10 lizing a mini-gene consisting of part of the type II procollagen gene (COL2A1), we show that TIA-1 in
11 transfected NIH 3T3 cells expressing a human type II procollagen gene under the control of the human
12 orresponding to various regions of the human type II procollagen gene were used to analyze the DNA fr
13                                              Type II procollagen is expressed as two splice forms.
14        The amino acid sequence of the canine type II procollagen is predicted to contain 1487 residue
15                                            A type II procollagen minigene that lacks exons 16-27 was
16 RCS-LTC cell line fails to express an active type II procollagen N-proteinase and, therefore, offers
17  II collagen (CII) messenger RNA, C-terminal type II procollagen propeptide (CPII), the collagenase c
18  type IIB collagen messenger RNA, C-terminal type II procollagen propeptide (CPII), the collagenase c
19 onstrating that the C-terminal propeptide of type II procollagen supports alpha2beta1-mediated bindin
20  and a similar decrease in the corresponding type II procollagen transcripts.
21                                        Human type II procollagen was prepared in a recombinant system
22 and disease can cleave the NH(2) terminus of type II procollagens, we tested eight types of enzymes.

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