Proteolytic release of the intramolecular chaperone domain confers processivity to endosialidase F. (Q41780441)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19189967%20AND%20SRC:MED&resulttype=core&format=json

20 January 2020

title

Proteolytic release of the intramolecular chaperone domain confers processivity to endosialidase F (English)

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20 January 2020

0 references

1 reference

3

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20 January 2020

author name string

David Schwarzer

1

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20 January 2020

Katharina Stummeyer

2

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20 January 2020

Friedrich Freiberger

4

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20 January 2020

Bastian Rode

5

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20 January 2020

Melanie Grove

6

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20 January 2020

Thomas Scheper

7

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20 January 2020

Mark von Itzstein

8

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20 January 2020

Martina Mühlenhoff

9

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20 January 2020

Rita Gerardy-Schahn

10

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20 January 2020

language of work or name

English

0 references

publication date

3 February 2009

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Journal of Biological Chemistry

20 January 2020

number of pages

10

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based on heuristic

inferred from page(s)

published in

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20 January 2020

volume

284

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20 January 2020

issue

14

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20 January 2020

page(s)

9465-9474

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Crystal structure of Escherichia coli phage HK620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related

20 January 2020

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18 August 2018

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18 August 2018

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18 August 2018

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18 August 2018

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18 August 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/19189967

inferred from PubMed ID database lookup

12 December 2020

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Giant liposomes as model membranes for immunological studies: spontaneous insertion of purified K1-antigen (poly-alpha-2,8-NeuAc) of Escherichia coli

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19189967

inferred from PubMed ID database lookup

12 December 2020

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Identifiers

DOI

10.1074/JBC.M808475200

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20 January 2020

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20 January 2020

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