(Q36818763)

English

A 35-kDa protein is the basic unit of the core from the 2 x 10(4)-kDa aggregation factor responsible for species-specific cell adhesion in the marine sponge Microciona prolifera

scientific article published on September 1996

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

A 35-kDa protein is the basic unit of the core from the 2 x 10(4)-kDa aggregation factor responsible for species-specific cell adhesion in the marine sponge Microciona prolifera (English)

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

1 reference

based on heuristic

inferred from title

author name string

Fernàndez-Busquets X

1

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

Kammerer RA

2

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

Burger MM

3

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

language of work or name

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publication date

1 September 1996

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Europe PubMed Central

PubMed publication ID

16 August 2017

number of pages

8

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inferred from page(s)

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

16 August 2017

271

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

38

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

23558-23565

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins

1 reference

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Physical properties of sponge aggregation factor. A unique proteoglycan complex.

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Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction

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The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis

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Identification and further characterization of the specific cell binding fragment from sponge aggregation factor

1 reference

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Cartilage proteoglycans. Structure and heterogeneity of the protein core and the effects of specific protein modifications on the binding to hyaluronate

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Characterization of sponge aggregation factor. A unique proteoglycan complex

1 reference

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Organization and polysaccharides of sponge aggregation factor

1 reference

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Proteoglycans: structures and interactions

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Liquid chromatographic determination of amino acids after gas-phase hydrolysis and derivatization with (dimethylamino)azobenzenesulfonyl chloride

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Adherence to the first-AUG rule when a second AUG codon follows closely upon the first

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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15 Cleavage at aspartylprolyl bonds

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Specific chemical modifications of link protein and their effect on binding to hyaluronate and cartilage proteoglycan.

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Anhydrous hydrogen fluoride deglycosylates glycoproteins

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Molecular cloning and functional expression of the cardiac sarcolemmal Na(+)-Ca2+ exchanger

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S-type lectins occur also in invertebrates: high conservation of the carbohydrate recognition domain in the lectin genes from the marine sponge Geodia cydonium

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cDNA structure and expression of calpactin, a peptide involved in Ca2(+)-dependent cell aggregation in sponges

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Non-proteoglycan forms of biglycan increase with age in human articular cartilage

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Molecular cloning of syndecan, an integral membrane proteoglycan

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Interaction of small dermatan sulfate proteoglycan from fibroblasts with fibronectin

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Proteoglycans in cell regulation

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Studies on yeast metabolism. I. Fractionation and microdetermination of cell carbohydrates

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The signal peptide

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Negative regulation of transforming growth factor-beta by the proteoglycan decorin

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Partial characterization of the sexual agglutination factor from Hansenula wingei Y-2340 type 5 cells

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Binding strength between cell adhesion proteoglycans measured by atomic force microscopy

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Deglycosylation of glycoproteins by trifluoromethanesulfonic acid

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Use of rhodamine B isothiocyanate to detect proteoglycan core proteins in polyacrylamide gels

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Sponge aggregation factor: identification of the specific collagen-binding site by means of a monoclonal antibody

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Control of the aggregation factor-aggregation receptor interaction in sponges by protein kinase C

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Quantitation of type I to type III collagen ratios in small samples of human tendon, blood vessels, and atherosclerotic plaque

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21 January 2018

Identifiers

10.1074/JBC.271.38.23558

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

16 August 2017

ResearchGate publication ID

0 references

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