Catabolism of chondroitin sulfate. - Wikidata - wikimedia - TriplyDB

Catabolism of chondroitin sulfate.

Catabolism of chondroitin sulfate.

http://www.wikidata.org/entity/Q38552797

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Chondroitin sulfate/dermatan sulfate sulfatases from mammals and bacteria.

P2860

Q38928043-FFA19DAD-78AE-406B-AC3F-85866824B6A9

P2860

Catabolism of chondroitin sulfate.

http://www.wikidata.org/entity/Q38552797

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Catabolism of chondroitin sulfate.

@en

type

label

Catabolism of chondroitin sulfate.

@en

prefLabel

Catabolism of chondroitin sulfate.

@en

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Q38552797-E1D0D7BF-AD5E-4549-B53E-03AB081C995A

P356

CMBLE-2015-0011

P1433

Cellular & Molecular Biology Letters

P1476

Catabolism of chondroitin sulfate.

@en

P2093

Shuhei Yamada

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P2860

Expression analysis of six paralogous human hyaluronidase genes clustered on chromosomes 3p21 and 7q31

Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol (GPI)-anchored cell-surface receptor for jaagsiekte sheep retrovirus, the envelope protein of which mediates oncogenic transformation

CD44-dependent intracellular and extracellular catabolism of hyaluronic acid by hyaluronidase-1 and -2

KIAA1199, a deafness gene of unknown function, is a new hyaluronan binding protein involved in hyaluronan depolymerization

Crystal structure of hyaluronidase, a major allergen of bee venom

Structure of human hyaluronidase-1, a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis

The crystal and molecular structures of a cathepsin K:chondroitin sulfate complex

Structure of the DBL3x domain of pregnancy-associated malaria protein VAR2CSA complexed with chondroitin sulfate A

Identification of domains in human beta-hexosaminidase that determine substrate specificity

Mouse sperm lacking cell surface hyaluronidase PH-20 can pass through the layer of cumulus cells and fertilize the egg

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196-212

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scholarly article

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10.1515/CMBLE-2015-0011

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2

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20

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2015-06-01T00:00:00Z

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26204402

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