Structure of neurolysin reveals a deep channel that limits substrate access (Q27630616)

2

K

Madauss

1 reference

20 October 2023

W Lian

3

W

Lian

1 reference

20 October 2023

M R Beck

4

M R

Beck

1 reference

20 October 2023

W D Tolbert

5

W D

Tolbert

1 reference

20 October 2023

D W Rodgers

6

D W

Proceedings of the National Academy of Sciences of the United States of America

Rodgers

1 reference

20 October 2023

language of work or name

English

0 references

publication date

13 March 2001

0 references

published in

0 references

volume

98

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issue

6

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page(s)

3127-32

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cites work

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Confocal microscopy reveals thimet oligopeptidase (EC 3.4.24.15) and neurolysin (EC 3.4.24.16) in the classical secretory pathway.

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Two mitochondrial matrix proteases act sequentially in the processing of mammalian matrix enzymes

29 September 2017

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Subsite Specificity of Porcine Pepsin

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Purification of the main somatostatin-degrading proteases from rat and pig brains, their action on other neuropeptides, and their identification as endopeptidases 24.15 and 24.16

2 June 2018

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Targeting of endopeptidase 24.16 to different subcellular compartments by alternative promoter usage.

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Processing of X-ray diffraction data collected in oscillation mode

21 January 2018

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Prolyl Oligopeptidase

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CHARMM: A program for macromolecular energy, minimization, and dynamics calculations

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Relationship between enzyme specificity and the backbone dynamics of free and inhibited alpha-lytic protease

21 January 2018

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Crystallization and preliminary analysis of neurolysin

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Polypeptide halomethyl ketones bind to serine proteases as analogs of the tetrahedral intermediate. X-ray crystallographic comparison of lysine- and phenylalanine-polypeptide chloromethyl ketone-inhibited subtilisin

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[36] Neurolysin: Purification and assays

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12 December 2020