Mycobacterium tuberculosiscopper-regulated protein SocB is an intrinsically disordered protein that folds upon interaction with a synthetic phospholipid bilayer

Mycobacterium tuberculosisand Copper: A Newly Appreciated Defense against an Old Foe?

(2015) K. Heran Darwin   JOURNAL OF BIOLOGICAL CHEMISTRY

Copper homeostasis in Mycobacterium tuberculosis

(2015) Xiaoshan Shi et al.   Metallomics

JPred4: a protein secondary structure prediction server

(2015) Alexey Drozdetskiy et al.   NUCLEIC ACIDS RESEARCH

Small Proteins Can No Longer Be Ignored

(2014) Gisela Storz et al.   Annual Review of Biochemistry

Atomic-level description of ubiquitin folding

(2013) S. Piana et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

A novel copper-responsive regulon in Mycobacterium tuberculosis

(2010) Richard A. Festa 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

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

Identification of a copper-binding metallothionein in pathogenic mycobacteria

(2008) Ben Gold et al.   Nature Chemical Biology

Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases

(2007) Lee Whitmore et al.   BIOPOLYMERS