Fate of Pup inside the Mycobacterium Proteasome Studied by in-Cell NMR

Order of the Proteasomal ATPases and Eukaryotic Proteasome Assembly

(2011) Robert J. Tomko et al.   CELL BIOCHEMISTRY AND BIOPHYSICS

Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli

(2011) Francisca A Cerda-Maira et al.   EMBO REPORTS

Activity of the Mycobacterial Proteasomal ATPase Mpa Is Reversibly Regulated by Pupylation

(2011) Cyrille L. Delley et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

(2011) Tim Bartels et al.   NATURE

A soluble  -synuclein construct forms a dynamic tetramer

(2011) W. Wang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structural basis for the assembly and gate closure mechanisms of the Mycobacterium tuberculosis 20S proteasome

(2010) Dongyang Li et al.   EMBO JOURNAL

The mycobacterial Mpa–proteasome unfolds and degrades pupylated substrates by engaging Pup's N-terminus

(2010) Frank Striebel et al.   EMBO JOURNAL

Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway

(2010) Frank Imkamp et al.   EMBO REPORTS

Prokaryotic Ubiquitin-Like Protein Provides a Two-Part Degron to Mycobacterium Proteasome Substrates

(2010) K. E. Burns et al.   JOURNAL OF BACTERIOLOGY

Prokaryotic Ubiquitin-like Protein (Pup) Is Coupled to Substrates via the Side Chain of Its C-Terminal Glutamate

(2010) Markus Sutter et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

“Depupylation” of Prokaryotic Ubiquitin-like Protein from Mycobacterial Proteasome Substrates

(2010) Kristin E. Burns et al.   MOLECULAR CELL

Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis

(2010) Francisca A. Cerda-Maira et al.   MOLECULAR MICROBIOLOGY

Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation

(2010) Tao Wang et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

In-cell NMR spectroscopy

(2010) Andres Y. Maldonado et al.   PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein

(2009) Shanhui Liao et al.   BIOCHEMICAL JOURNAL

A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa

(2009) Markus Sutter et al.   FEBS LETTERS

Prokaryotic Ubiquitin-Like Protein Pup Is Intrinsically Disordered

(2009) Xiang Chen et al.   JOURNAL OF MOLECULAR BIOLOGY

Deletion ofdopinMycobacterium smegmatisabolishes pupylation of protein substratesin vivo

(2009) Frank Imkamp et al.   MOLECULAR MICROBIOLOGY

Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes

(2009) Frank Striebel et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Structural Insights on the Mycobacterium tuberculosis Proteasomal ATPase Mpa

(2009) Tao Wang et al.   STRUCTURE

Proteasomal Protein Degradation in Mycobacteria Is Dependent upon a Prokaryotic Ubiquitin-like Protein

(2008) Kristin E. Burns et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Differential Dynamical Effects of Macromolecular Crowding on an Intrinsically Disordered Protein and a Globular Protein: Implications for In-Cell NMR Spectroscopy

(2008) Conggang Li et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

In-Cell Biochemistry Using NMR Spectroscopy

(2008) David S. Burz et al.   PLoS One

Ubiquitin-Like Protein Involved in the Proteasome Pathway of Mycobacterium tuberculosis

(2008) M. J. Pearce et al.   SCIENCE