Unappreciated Roles for K + Channels in Bacterial Physiology

Beagle, S.D.. and S.W. Lockless

Trends Microbiol 5:S0966 (2020)

Use of a Fluorescence-Based Assay To Measure Escherichia coli Membrane Potential Changes in High Throughput

Hudson, M.A., Siegele, D.A. and S.W. Lockless

Antimicrob Agents Chemother 64:e00910 (2020)

TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential

Zhang H., Pan Y., Hu L., Hudson M.A., Hofstetter K.S., Xu Z., Rong M., Wang Z., Prasad B.V.V., Lockless S.W.*, Chiu W*, Zhou M*.

Nat Commun 11:547 (2020)

A Novel Actin Binding Drug with In Vivo Efficacy

Ravichandran A, Geng M, Hull K.G., Li J, Romo D, Lu S.E., Albee A, Nutter C, Gordon D.M., Ghannoum M.A., Lockless S.W. and L. Smith

Antimicrob Agents Chemother 63:e01585-18 (2018)

High affinity interactions of Pb2+ with synaptotagmin I

Katti S, Her B, Srivastava A.K., Taylor A.B., Lockless S.W. and T.I. Igumenova

Metallomic 10:1211-1222 (2018)

Ion Binding to Transport Proteins using Isothermal Titration Calorimetry

Liu S. and S.W. Lockless

Methods Mol Biol 1684:289-303 (2018)

A Clostridium difficile alanine racemase affects spore germination and accommodates serine as a substrate

Shrestha R., Lockless S.W. and J.A. Sorg

J Biol Chem 292:10735-10742 (2017)

Preparation To Minimize Buffer Mismatch in Isothermal Titration Calorimetry Experiments

Bian, X. and S. W. Lockless

Anal Chem 88:5549-5553 (2016)

Ion binding properties of a K+ channel selectivity filter in different conformations

Liu, S., Focke,P.J., Matulef, K., Bian, X., Moënne-Loccoz, P., Valiyaveetil, F.I. and S. W. Lockless

Proc Natl Acad Sci  112:15096-15100 (2015)

 

Electrical signalling goes bacterial

Beagle, S.D. and S.W. Lockless

Nature 526:44-45 (2015)

 

Determinants of cation transport selectivity: equilibrium binding and transport kinetics

Lockless, S.W.

J Gen Physiol 146:3-13 (2015)

 

Live Imaging of Inorganic Phosphate in Plants with Cellular and Subcellular Resolution

Mukherjee, P., Banerjee, S., Wheeler, A., Ratliff, L.A., Garcia, L.R., Lockless, S.W. and W.K. Versaw

Plant Physiology 167:628-628 (2015)

 

Structure of a membrane-embedded prenyltransferase homologous to UBIAD1

Huang, H.*, Levin, E.J.*, Liu, S., Bai, Y., Lockless, S.W. and M. Zhou.

PLoS Biology 12:e1001911 (2014)

 

Equilibrium selectivity alone does not create K+-selective ion conduction in K+ channels

Liu, S. and S.W. Lockless

Nat Commun 4:2746 (2013)

 

Preferential binding of K+ ions in the selectivity filter at equilibrium explains high selectivity of K+ channels

Liu, S.*, Bian, X.* and S.W. Lockless

J Gen Physiol 140:671-679 (2012)

 

Traceless protein splicing utilizing evolves split inteins

Lockless, S.W. and T.W. Muir

Proc Natl Acad Sci 106:10999-11004 (2009)

 

Structural Principles and Thermodynamic Properties of Ion Selectivity in a K+ Channel

Lockless, S.W., Zhou, M., MacKinnon, R

PLoS Biology 5:e121 (2007)

 

Evolutionary information for specifying a protein fold

Socolich, M.A.*, Lockless, S.W.*, Russ, W.P., Lee, H., Gardner, K.H. and R. Ranganathan

Nature 437:512-518 (2005)

 

CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains

Vergani P, Lockless, S.W., Nairn A.C. and Gadsby D.C.

Nature 433:876-880 (2005)

 

Allosteric Determinants in Guanine Nucleotide-binding Proteins

Hatley, M.E., Lockless, S.W., Gibson, S.K., Gilman A.G. and R. Ranganathan

Proc Natl Acad Sci 100:14445-14450 (2003)

 

Evolutionarily Conserved Networks of Residues Mediate Allosteric Communication in Proteins

Suel, G.*, Lockless, S.W.*, Wall, M.A. and R. Ranganathan

Nat Struct Biol 10:59-69 (2003)

 

Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families

Lockless, S.W. and R. Ranganathan

Science 286:295-299 (1999)

 

Recognition of Capped RNA Substrates by VP39, the Vaccinia-Encoded mRNA Cap-Specific 2'-O-Methyltransferase

Lockless, S.W., Cheng, H-T., Hodel, A.E., Quiocho, F.A. and P.D. Gershon

Biochemistry 37:8564-5874 (1998)

 

* Authors contributed equally to this work.