D
David L. Huffman
Researcher at Western Michigan University
Publications - 29
Citations - 3557
David L. Huffman is an academic researcher from Western Michigan University. The author has contributed to research in topics: Copper & Wilson disease protein. The author has an hindex of 23, co-authored 29 publications receiving 3417 citations. Previous affiliations of David L. Huffman include University of Illinois at Urbana–Champaign & Northwestern University.
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The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli.
TL;DR: The cytosolic (CueR) and periplasmic (CusRS) sensor systems differentially regulate copper export systems in response to changes in copper and oxygen availability, underscore the increased toxicity of copper under anaerobic conditions and the complex adaptation of copper export in E. coli.
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Function, structure, and mechanism of intracellular copper trafficking proteins.
TL;DR: Although the intimate mechanism is still open, it appears that a low activation barrier for metal transfer is achieved by a network of coordinate-covalent, electrostatic, and hydrogen bonding interactions in the vicinity of the metal-binding site itself.
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Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins.
TL;DR: The structures of Hah1 provide models for intermediates in metal ion transfer and suggest a detailed molecular mechanism for protein recognition and metal ion exchange between MT/HCXXC containing domains.
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Metallochaperones and metal-transporting ATPases: a comparative analysis of sequences and structures.
Fabio Arnesano,Lucia Banci,Ivano Bertini,Simone Ciofi-Baffoni,Elena Molteni,David L. Huffman,Thomas V. O'Halloran +6 more
TL;DR: It is found that metallochaperones and their physiological partner ATPases from several phylogenetic kingdoms recognize one another, via an interplay of electrostatics, hydrogen bonding, and hydrophobic interactions, in a manner that precisely orients the metal-binding side chains for rapid metal transfer between otherwise tight binding sites.
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Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution.
Amy C. Rosenzweig,David L. Huffman,Melody Y. Hou,Amy K. Wernimont,Robert A. Pufahl,Thomas V. O'Halloran +5 more
TL;DR: The Atx1 structural motif represents a prototypical metal ion trafficking unit that is likely to be employed in a variety of organisms for different metal ions and is one of the largest unknown structures solved by direct methods.