Organization of the exons coding for pro α1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes

Ming Wan Su; Virginia Benson-Chanda; Henrik Vissing; Francesco Ramirez

doi:10.1016/0888-7543(89)90353-4

Organization of the exons coding for pro α1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes

Ming Wan Su, Virginia Benson-Chanda, Henrik Vissing, Francesco Ramirez

Research output: Contribution to journal › Article › peer-review

26 Scopus citations

Abstract

The organization of the exons coding for the N-terminal portion of human type II procollagen has been determined. Aside from inferring the previously unknown primary structure of type II N-propeptide, this study has revealed that this coding domain of the gene exhibits an organization uniquely distinct from those of type I and type III collagens. This finding substantiates the notion that the N-propeptide coding domains of the fibrillar collagen genes evolved under less stringent selection than those encoding the C-propeptide and triple helical regions.

Original language	English
Pages (from-to)	438-441
Number of pages	4
Journal	Genomics
Volume	4
Issue number	3
DOIs	https://doi.org/10.1016/0888-7543(89)90353-4
State	Published - Apr 1989
Externally published	Yes

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@article{646b886aee4f41f3b53190337b26e27a,

title = "Organization of the exons coding for pro α1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes",

abstract = "The organization of the exons coding for the N-terminal portion of human type II procollagen has been determined. Aside from inferring the previously unknown primary structure of type II N-propeptide, this study has revealed that this coding domain of the gene exhibits an organization uniquely distinct from those of type I and type III collagens. This finding substantiates the notion that the N-propeptide coding domains of the fibrillar collagen genes evolved under less stringent selection than those encoding the C-propeptide and triple helical regions.",

author = "Su, \{Ming Wan\} and Virginia Benson-Chanda and Henrik Vissing and Francesco Ramirez",

note = "Funding Information: This work was supported by grants from the National Institutes of Health (AR38646 and HD22657). The authors thank Ms. Sharon Boast for many helpful suggestions and Ms. Roseann Lingeza for preparing and typing of the manuscript.",

year = "1989",

month = apr,

doi = "10.1016/0888-7543(89)90353-4",

language = "English",

volume = "4",

pages = "438--441",

journal = "Genomics",

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publisher = "Academic Press Inc.",

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T1 - Organization of the exons coding for pro α1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes

AU - Su, Ming Wan

AU - Benson-Chanda, Virginia

AU - Vissing, Henrik

AU - Ramirez, Francesco

N1 - Funding Information: This work was supported by grants from the National Institutes of Health (AR38646 and HD22657). The authors thank Ms. Sharon Boast for many helpful suggestions and Ms. Roseann Lingeza for preparing and typing of the manuscript.

PY - 1989/4

Y1 - 1989/4

N2 - The organization of the exons coding for the N-terminal portion of human type II procollagen has been determined. Aside from inferring the previously unknown primary structure of type II N-propeptide, this study has revealed that this coding domain of the gene exhibits an organization uniquely distinct from those of type I and type III collagens. This finding substantiates the notion that the N-propeptide coding domains of the fibrillar collagen genes evolved under less stringent selection than those encoding the C-propeptide and triple helical regions.

AB - The organization of the exons coding for the N-terminal portion of human type II procollagen has been determined. Aside from inferring the previously unknown primary structure of type II N-propeptide, this study has revealed that this coding domain of the gene exhibits an organization uniquely distinct from those of type I and type III collagens. This finding substantiates the notion that the N-propeptide coding domains of the fibrillar collagen genes evolved under less stringent selection than those encoding the C-propeptide and triple helical regions.

UR - https://www.scopus.com/pages/publications/0024652728

U2 - 10.1016/0888-7543(89)90353-4

DO - 10.1016/0888-7543(89)90353-4

M3 - Article

C2 - 2714801

AN - SCOPUS:0024652728

SN - 0888-7543

VL - 4

SP - 438

EP - 441

JO - Genomics

JF - Genomics

IS - 3

ER -

Organization of the exons coding for pro α1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes

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