Molecular Cloning and Tissue Distribution of Keratocan BOVINE CORNEAL KERATAN SULFATE PROTEOGLYCAN 37A
Lolita M. Corpuz,James L. Funderburgh,Martha L. Funderburgh,George S. Bottomley,Sujatha Prakash,Gary W. Conrad +5 more
TLDR
Funderburgh et al. as mentioned in this paper showed that the keratan sulfate-containing proteoglycans of bovine corneal stroma contain three unique core proteins designated 37A, 37B, and 25.About:
This article is published in Journal of Biological Chemistry.The article was published on 1996-04-19 and is currently open access. It has received 213 citations till now. The article focuses on the topics: Keratocan & Keratan sulfate.read more
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Matrix Proteoglycans: From Molecular Design to Cellular Function
TL;DR: The proteoglycan superfamily now contains more than 30 full-time molecules that fulfill a variety of biological functions and additional roles, derived from studies of mutant animals, indicate that certain proteoglycans are essential to life whereas others might be redundant.
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Proteoglycan form and function: A comprehensive nomenclature of proteoglycans
Renato V. Iozzo,Liliana Schaefer +1 more
TL;DR: The proposed nomenclature encompasses forty-three distinct proteoglycan-encoding genes and many alternatively-spliced variants and is based on three criteria: Cellular and subcellular location, overall gene/protein homology, and the utilization of specific protein modules within their respective protein cores.
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Lumican Regulates Collagen Fibril Assembly: Skin Fragility and Corneal Opacity in the Absence of Lumican
Shukti Chakravarti,Terry Magnuson,Jonathan H. Lass,Karl J. Jepsen,Christian LaMantia,Heidi Carroll +5 more
TL;DR: A crucial role is established for lumican in the regulation of collagen assembly into fibrils in various connective tissues and the development of a highly organized collagenous matrix and corneal transparency.
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The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins.
TL;DR: The focus is on the “functional network” created by these molecules in tissues, on genetic evidence for their functional roles during ontogeny, and on their activities as modulators of complex pathological processes such as fibrosis and cancer growth.
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The family of the small leucine-rich proteoglycans: key regulators of matrix assembly and cellular growth.
TL;DR: These proteoglycans are tissue organizers, orienting and ordering collagen fibrils during ontogeny and in pathological processes such as wound healing, tissue repair, and tumor stroma formation, and three-dimensional modeling of their prototype protein core proposes a flexible, arch-shaped binding surface suitable for strong and distinctive interactions with ligand proteins.
References
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Book
Molecular Cloning: A Laboratory Manual
TL;DR: Molecular Cloning has served as the foundation of technical expertise in labs worldwide for 30 years as mentioned in this paper and has been so popular, or so influential, that no other manual has been more widely used and influential.
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Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
TL;DR: A new method of total RNA isolation by a single extraction with an acid guanidinium thiocyanate-phenol-chloroform mixture is described, providing a pure preparation of undegraded RNA in high yield and can be completed within 4 h.
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Identification of common molecular subsequences.
TL;DR: This letter extends the heuristic homology algorithm of Needleman & Wunsch (1970) to find a pair of segments, one from each of two long sequences, such that there is no other Pair of segments with greater similarity (homology).
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A new method for predicting signal sequence cleavage sites.
TL;DR: A new method for identifying secretory signal sequences and for predicting the site of cleavage between a signal sequence and the mature exported protein is described.
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Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
Bostjan Kobe,Johann Deisenhofer +1 more
TL;DR: This work has determined the crystal structure of the porcine inhibitor, which is the first three-dimensional structure of a protein containing leucine-rich repeats and represents a new class of α/β protein fold.