(Q27640607)

1

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Robert Huber

5

object named as

Robert Huber

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Hans Brandstetter

2

object named as

Hans Brandstetter

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author name string

Hans Bartunik

3

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Gleb Bourenkow

Journal of Molecular Biology

4

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language of work or name

English

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publication date

14 March 2003

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published in

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volume

327

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issue

1

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page(s)

75-83

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1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Structure and functions of the 20S and 26S proteasomes

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Structure of 20S proteasome from yeast at 2.4 A resolution

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

A protein catalytic framework with an N-terminal nucleophile is capable of self-activation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

20 S proteasomes are assembled via distinct precursor complexes. Processing of LMP2 and LMP7 proproteins takes place in 13-16 S preproteasome complexes

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Maturation of mammalian 20 S proteasome: purification and characterization of 13 S and 16 S proteasome precursor complexes

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor beta subunits

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Late events in the assembly of 20S proteasomes

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Dissecting the assembly pathway of the 20S proteasome

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Critical elements in proteasome assembly

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Autocatalytic processing of the 20S proteasome

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Conformational constraints for protein self-cleavage in the proteasome

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Characterisation of the newly identified human Ump1 homologue POMP and analysis of LMP7(beta 5i) incorporation into 20 S proteasomes

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

A gated channel into the proteasome core particle

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Structural basis for the activation of 20S proteasomes by 11S regulators

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Proteasome from Thermoplasma acidophilum: a threonine protease

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Proteasome β-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9

Implementation of molecular replacement in AMoRe

7 January 2021

1 reference

https://api.crossref.org/works/10.1016/S0022-2836(03)50080-9