(Q48209588)

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Hsp104 is a highly conserved protein with two essential nucleotide-binding sites

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Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

Hsp104 is a highly conserved protein with two essential nucleotide-binding sites (English)

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

author name string

Parsell DA

1

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Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

Sanchez Y

2

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Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

Stitzel JD

3

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Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

Lindquist S

4

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9 February 2018

http://europepmc.org/abstract/MED/1896074

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1 September 1991

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Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

353

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Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

6341

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Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

270-273

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Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

The heat-shock proteins

1 reference

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HSP104 required for induced thermotolerance

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Association between the mammalian 110,000-dalton heat-shock protein and nucleoli

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Morphological study of the mammalian stress response: characterization of changes in cytoplasmic organelles, cytoskeleton, and nucleoli, and appearance of intranuclear actin filaments in rat fibroblasts after heat-shock treatment

1 reference

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7 January 2021

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Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes

1 reference

https://api.crossref.org/works/10.1038/353270A0

7 January 2021

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The molecular evolution of genes and proteins: a tale of two serines

1 reference

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Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

1 reference

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Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La.

1 reference

https://api.crossref.org/works/10.1038/353270A0

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ClpB is the Escherichia coli heat shock protein F84.1.

1 reference

https://api.crossref.org/works/10.1038/353270A0

7 January 2021

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Expression of ClpB, an analog of the ATP-dependent protease regulatory subunit in Escherichia coli, is controlled by a heat shock sigma factor (sigma 32).

1 reference

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ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins

1 reference

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Site-directed mutagenesis of a nucleotide-binding domain in HSV-1 thymidine kinase: effects on catalytic activity

1 reference

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Separation of yeast proteasome subunits. Immunoreactivity with antibodies against ATP-dependent protease Ti from Escherichia coli

1 reference

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7 January 2021

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ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin

1 reference

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Molecular cloning and functional analysis of three subunits of yeast proteasome

1 reference

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The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses

1 reference

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Speculations on the functions of the major heat shock and glucose-regulated proteins

1 reference

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Conserved protein domains in a myosin heavy chain gene from Dictyostelium discoideum

1 reference

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7 January 2021

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Identifiers

10.1038/353270A0

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

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0 references

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

9 February 2018

http://europepmc.org/abstract/MED/1896074

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