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P-Type Lectins

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P-Type Lectins. / Dahms, Nancy; Braulke, Thomas; Varki, Ajit.

Essentials of Glycobiology. ed. / Ajit Varki. 4. ed. Cold Spring Harbor, New York : Cold Spring Harbor Laboratory Press, 2022. p. 443 - 454.

Research output: SCORING: Contribution to book/anthology › SCORING: Contribution to collected editions/anthologies › Research › peer-review

Harvard

Dahms, N, Braulke, T & Varki, A 2022, P-Type Lectins. in A Varki (ed.), Essentials of Glycobiology. 4 edn, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, pp. 443 - 454. https://doi.org/10.1101/glycobiology.4e.33

APA

Dahms, N., Braulke, T., & Varki, A. (2022). P-Type Lectins. In A. Varki (Ed.), Essentials of Glycobiology (4 ed., pp. 443 - 454). Cold Spring Harbor Laboratory Press. https://doi.org/10.1101/glycobiology.4e.33

Vancouver

Dahms N, Braulke T, Varki A. P-Type Lectins. In Varki A, editor, Essentials of Glycobiology. 4 ed. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press. 2022. p. 443 - 454 https://doi.org/10.1101/glycobiology.4e.33

Bibtex

@inbook{50dd03d087ee443b9477e2a5acd5e324,
title = "P-Type Lectins",
abstract = "Lysosomes are intracellular membrane-bound organelles that turn over and degrade many types of macromolecules, via the action of lysosomal enzymes (also called acid hydrolases because of the low-pH characteristic of lysosomes). These enzymes are synthesized in the endoplasmic reticulum (ER) on membrane-bound ribosomes and traverse the ER–Golgi pathway along with other newly synthesized proteins. At the terminal Golgi compartment, they are segregated from other glycoproteins and selectively delivered to lysosomes. In most “higher” animal cells, this specialized trafficking is achieved primarily through the recognition of N-glycans containing mannose 6-phosphate (M6P) by “P-type” lectins. As the first clear-cut example of a biological role for glycans on mammalian glycoproteins and the first shown link between glycoprotein biosynthesis and human disease, the interesting history of its discovery is described in some detail. More recent data on other proteins with “P-type” lectin domains are also mentioned.",
author = "Nancy Dahms and Thomas Braulke and Ajit Varki",
year = "2022",
doi = "10.1101/glycobiology.4e.33",
language = "English",
isbn = "978-1-62182-421-3",
pages = "443 -- 454",
editor = "Ajit Varki",
booktitle = "Essentials of Glycobiology",
publisher = "Cold Spring Harbor Laboratory Press",
address = "United States",
edition = "4",

}

RIS

TY - CHAP

T1 - P-Type Lectins

AU - Dahms, Nancy

AU - Braulke, Thomas

AU - Varki, Ajit

PY - 2022

Y1 - 2022

N2 - Lysosomes are intracellular membrane-bound organelles that turn over and degrade many types of macromolecules, via the action of lysosomal enzymes (also called acid hydrolases because of the low-pH characteristic of lysosomes). These enzymes are synthesized in the endoplasmic reticulum (ER) on membrane-bound ribosomes and traverse the ER–Golgi pathway along with other newly synthesized proteins. At the terminal Golgi compartment, they are segregated from other glycoproteins and selectively delivered to lysosomes. In most “higher” animal cells, this specialized trafficking is achieved primarily through the recognition of N-glycans containing mannose 6-phosphate (M6P) by “P-type” lectins. As the first clear-cut example of a biological role for glycans on mammalian glycoproteins and the first shown link between glycoprotein biosynthesis and human disease, the interesting history of its discovery is described in some detail. More recent data on other proteins with “P-type” lectin domains are also mentioned.

AB - Lysosomes are intracellular membrane-bound organelles that turn over and degrade many types of macromolecules, via the action of lysosomal enzymes (also called acid hydrolases because of the low-pH characteristic of lysosomes). These enzymes are synthesized in the endoplasmic reticulum (ER) on membrane-bound ribosomes and traverse the ER–Golgi pathway along with other newly synthesized proteins. At the terminal Golgi compartment, they are segregated from other glycoproteins and selectively delivered to lysosomes. In most “higher” animal cells, this specialized trafficking is achieved primarily through the recognition of N-glycans containing mannose 6-phosphate (M6P) by “P-type” lectins. As the first clear-cut example of a biological role for glycans on mammalian glycoproteins and the first shown link between glycoprotein biosynthesis and human disease, the interesting history of its discovery is described in some detail. More recent data on other proteins with “P-type” lectin domains are also mentioned.

UR - https://www.ncbi.nlm.nih.gov/books/NBK579952/

U2 - 10.1101/glycobiology.4e.33

DO - 10.1101/glycobiology.4e.33

M3 - SCORING: Contribution to collected editions/anthologies

C2 - 35536959

SN - 978-1-62182-421-3

SP - 443

EP - 454

BT - Essentials of Glycobiology

A2 - Varki, Ajit

PB - Cold Spring Harbor Laboratory Press

CY - Cold Spring Harbor, New York

ER -