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The Networking of Chaperones by Co-chaperones

Overview of attention for book
Cover of 'The Networking of Chaperones by Co-chaperones'

Table of Contents

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    Book Overview
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    Chapter 1 GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG Domain Proteins: Nucleotide Exchange Factors for Hsp70 Molecular Chaperones
  3. Altmetric Badge
    Chapter 2 Functions of the Hsp90-Binding FKBP Immunophilins
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    Chapter 3 Hsp70/Hsp90 Organising Protein (Hop): Beyond Interactions with Chaperones and Prion Proteins
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    Chapter 4 Specification of Hsp70 Function by Type I and Type II Hsp40
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    Chapter 5 Cdc37 as a Co-chaperone to Hsp90.
  7. Altmetric Badge
    Chapter 6 p23 and Aha1.
  8. Altmetric Badge
    Chapter 7 UCS Proteins: Chaperones for Myosin and Co-Chaperones for Hsp90.
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    Chapter 8 Chaperonin—Co-chaperonin Interactions
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    Chapter 9 Co-chaperones of the Mammalian Endoplasmic Reticulum
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    Chapter 10 The Evolution and Function of Co-Chaperones in Mitochondria
  12. Altmetric Badge
    Chapter 11 CHIP: A Co-chaperone for Degradation by the Proteasome
  13. Altmetric Badge
    Chapter 12 The Role of HSP70 and Its Co-chaperones in Protein Misfolding, Aggregation and Disease.
Attention for Chapter 6: p23 and Aha1.
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Chapter title
p23 and Aha1.
Chapter number 6
Book title
The Networking of Chaperones by Co-chaperones
Published in
Sub cellular biochemistry, January 2015
DOI 10.1007/978-3-319-11731-7_6
Pubmed ID
25487019
Book ISBNs
978-3-31-911730-0, 978-3-31-911731-7
Authors

Alexandra Beatrice Rehn, Johannes Buchner

Abstract

Hsp90 is a conserved molecular chaperone and is responsible for the folding and activation of several hundred client proteins, involved in various cellular processes. The large number and the diversity of these client proteins demand a high adaptiveness of Hsp90 towards the need of the individual client. This adaptiveness is amongst others mediated by more than 20 so-called cochaperones that differ in their actions towards Hsp90. Some of these cochaperones are able to modulate the ATPase activity of Hsp90 and/or its client protein binding, folding and activation. p23 and Aha1 are two prominent examples with opposing effects on the ATPase activity of Hsp90. p23 is able to inhibit the ATP turnover while Aha1 is the strongest known activator of the ATPase activity of Hsp90. Even though both cochaperones are conserved from yeast to man and have been studied for years, some Hsp90-related as well as Hsp90-independent functions are still enigmatic and under current investigation. In this chapter, we first introduce the ATPase cycle of Hsp90 and then focus on the two cochaperones integrating them in the Hsp90 cycle.

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X Demographics

The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
 Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 14 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 14 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 3 21%
Student > Postgraduate 2 14%
Other 1 7%
Lecturer 1 7%
Professor 1 7%
Other 3 21%
Unknown 3 21%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 4 29%
Agricultural and Biological Sciences 2 14%
Unspecified 1 7%
Earth and Planetary Sciences 1 7%
Engineering 1 7%
Other 0 0%
Unknown 5 36%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 10 December 2014.
All research outputs
#15,272,611
of 22,711,242 outputs
Outputs from Sub cellular biochemistry
#183
of 353 outputs
Outputs of similar age
#208,623
of 352,754 outputs
Outputs of similar age from Sub cellular biochemistry
#8
of 26 outputs
Altmetric has tracked 22,711,242 research outputs across all sources so far. This one is in the 22nd percentile – i.e., 22% of other outputs scored the same or lower than it.
So far Altmetric has tracked 353 research outputs from this source. They receive a mean Attention Score of 4.7. This one is in the 37th percentile – i.e., 37% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 352,754 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 31st percentile – i.e., 31% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 26 others from the same source and published within six weeks on either side of this one. This one is in the 42nd percentile – i.e., 42% of its contemporaries scored the same or lower than it.

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