Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins (Q24312902)

anatomical structure morphogenesis

GOA release 2020-03-11

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GOA release 2020-03-11

A Grubb

5

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author name string

J Ni

1

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M Abrahamson

2

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M Zhang

3

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M A Fernandez

4

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J Su

6

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G L Yu

7

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Y Li

8

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D Parmelee

9

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L Xing

10

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T A Coleman

11

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S Gentz

12

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R Thotakura

13

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N Nguyen

14

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M Hesselberg

15

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R Gentz

Journal of Biological Chemistry

16

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language of work or name

English

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publication date

18 April 1997

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published in

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volume

272

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issue

16

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page(s)

10853-8

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cites work

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The human type 2 cystatin gene family consists of eight to nine members, with at least seven genes clustered at a single locus on human chromosome 20

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Importance of the evolutionarily conserved glycine residue in the N-terminal region of human cystatin C (Gly-11) for cysteine endopeptidase inhibition.

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Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases

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Identification of Full-Sized Forms of Salivary (Type) Cystatins (Cystatin SN, Cystatin SA, Cystatin S, and Two Phosphorylated Forms of Cystatin S) in Human Whole Saliva and Determination of Phosphorylation Sites of Cystatin S

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Signal sequences. The limits of variation

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Cystatin C (CST3), the candidate gene for hereditary cystatin C amyloid angiopathy (HCCAA), and other members of the cystatin gene family are clustered on chromosome 20p11.2.

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