- Kunth M, Lu GJ, Witte C, Shapiro MG, Schröder L (2018) Protein nanostructures produce self-adjusting hyperpolarized magnetic resonance imaging contrast through physical gas partitioning. ACS Nano in press
- Lu GJ #, Farhadi A#, Mukherjee A, Shapiro MG (2018) Proteins, air and water: reporter genes for ultrasound and magnetic resonance imaging. Current Opinion in Chemical Biology 45, 57-63. (# co-authors)
- Maresca D, Lakshmanan A, Abedi M, Bar-Zion A, Farhadi A, Lu GJ, Szablowski JO, Wu D, Yoo S, Shapiro MG (2018) Biomolecular Ultrasound and Sonogenetics. Annu. Rev. Chem. Biomol. Eng. 9, 229-252.
- Lu GJ, Farhadi A, Szablowski JO, Lee-Gosselin A, Barnes SR, Lakshmanan A, Bourdeau RW, Shapiro MG (2018) Acoustically modulated magnetic resonance imaging of gas-filled protein nanostructures. Nature Materials 17, 456-463. News & Views. Featured on the journal cover. Caltech news. Behind the paper.
Gas vesicles (GVs) can produce robust susceptibility-based MRI contrast that is erasable by ultrasound treatment, and the resulting differential image unambiguously reveals the location of contrast agents irrespective of confounding endogenous tissue signals.
- Farhadi A, Ho G, Kunth M, Ling B, Lakshmanan A, Lu GJ, Bourdeau RW, Schröder L, Shapiro MG (2018) Recombinantly Expressed Gas Vesicles as Nanoscale Contrast Agents for Ultrasound and Hyperpolarized MRI. AIChE Journal 64:2927–2933.
- Lakshmanan A #, Lu GJ #, Farhadi A #, Nety SP #, Kunth M, Lee-Gosselin A, Maresca D, Bourdeau RW, Yin M, Yan J, Witte C, Malounda D, Foster FS, Schröder L, Shapiro MG (2017) Preparation of biogenic gas vesicle nanostructures for use as contrast agents for ultrasound and MRI. Nature Protocols 12(10):2050-2080. (# co-authors)
A detailed protocol on the expression, purification, functionalization, ultrasound imaging and hyperpolarized xenon MRI of gas vesicles (GVs).
- Mukherjee A, Davis HC, Ramesh P, Lu GJ, Shapiro MG (2017) Biomolecular MRI reporters: Evolution of new mechanisms. Prog. Nucl. Magn. Reson. Spectrosc. 102-103:32-42.
- Maley AM, Lu GJ, Shapiro MG, Corn RM (2017) Characterizing Single Polymeric and Protein Nanoparticles with Surface Plasmon Resonance Imaging Measurements. ACS Nano 11(7):7447-7456.
- Barskiy DA, Coffey AM, Nikolaou P, Mikhaylov DM, Goodson BM, Branca RT, Lu GJ, Shapiro MG, Telkki V-V, Zhivonitko VV, Koptyug IV, Salnikov OG, Kovtunov KV, Bukhtiyarov VI, Rosen MS, Barlow MJ, Safavi S, Hall IP, Schröder L, Chekmenev EY (2017) NMR Hyperpolarization Techniques of Gases. Chemistry 23(4):725-751.
- Radoicic J, Lu GJ, Opella SJ (2014) NMR structures of membrane proteins in phospholipid bilayers. Q. Rev. Biophys. 47(3):249-283.
- Tian Y, Lu GJ, Marassi FM, Opella SJ (2014) Structure of the membrane protein MerF, a bacterial mercury transporter, improved by the inclusion of chemical shift anisotropy constraints. J. Biomol. NMR 60(1):67-71.
- Lu GJ, Opella SJ (2014) Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR. J. Biomol. NMR 58(1):69-81.
A summary of the strategy to combine multiple methods for resonance assignment, a key bottleneck of solving membrane protein structures by oriented sample solid-state NMR.
- Lu GJ, Opella SJ (2014) Mechanism of dilute-spin-exchange in solid-state NMR. J. Chem. Phys. 140(12):124201.
An experimental proof that the proton-relay mechanism plays the central role in spin exchange in oriented sample solid-state NMR.
- Lu GJ, Opella SJ (2013) Motion-adapted pulse sequences for oriented sample (OS) solid-state NMR of biopolymers. J. Chem. Phys. 139(8):084203.
Numerical simulations to illustrate that the “motion-adapted” principle is the reason for the superior performance of MSHOT-Pi4/Pi pulse sequence on membrane protein samples.
- Lu GJ, Tian Y, Vora N, Marassi FM, Opella SJ (2013) The structure of the mercury transporter MerF in phospholipid bilayers: a large conformational rearrangement results from N-terminal truncation. J. Am. Chem. Soc. 135(25):9299-9302.
The structure of the full-length mercury transporter protein MerF (PDB: 2M67) reveals ~ 90° conformational rearrangement of an α-helix compared to the structure of a truncated construct. Green arrows highlight the directions of the α-helix involved.
- Das BB, Nothnagel HJ, Lu GJ, Son WS, Tian Y, Marassi FM, Opella SJ (2012) Structure determination of a membrane protein in proteoliposomes. J. Am. Chem. Soc. 134(4):2047-2056.
- Lu GJ, Park SH, Opella SJ (2012) Improved 1H amide resonance line narrowing in oriented sample solid-state NMR of membrane proteins in phospholipid bilayers. J. Magn. Reson. 220:54-61.
The initial discovery that MSHOT-Pi4/Pi pulse sequence improved 1H spectral resolution by more than 2 folds and the improvement pertained specifically to membrane protein samples.
- Son WS, Park SH, Nothnagel HJ, Lu GJ, Wang Y, Zhang H, Cook GA, Howell SC, Opella SJ (2012) ‘q-Titration’ of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy. J. Magn. Reson. 214(0):111-118.
- Lu GJ, Son WS, Opella SJ (2011) A general assignment method for oriented sample (OS) solid-state NMR of proteins based on the correlation of resonances through heteronuclear dipolar couplings in samples aligned parallel and perpendicular to the magnetic field. J. Magn. Reson. 209(2):195-206.
A new method, “dipolar coupling correlated isotropic chemical shift analysis” (DCCICS), for resonance assignment by oriented sample solid-state NMR.
- Marassi FM, Das BB, Lu GJ, Nothnagel HJ, Park SH, Son WS, Tian Y, Opella SJ (2011) Structure determination of membrane proteins in five easy pieces. Methods 55(4):363-369.
- Knox RW, Lu GJ, Opella SJ, Nevzorov AA (2010) A Resonance Assignment Method for Oriented-Sample Solid-State NMR of Proteins. J. Am. Chem. Soc. 132(24):8255-8257.
- Cherney LT, Cherney MM, Garen CR, Lu GJ, James MNG (2008) Crystal Structure of the Arginine Repressor Protein in Complex with the DNA Operator from Mycobacterium tuberculosis. J. Mol. Biol. 384(5):1330-1340.
- Cherney LT, Cherney MM, Garen CR, Lu GJ, James MNG (2008) Structure of the C-terminal domain of the arginine repressor protein from Mycobacterium tuberculosis. Acta Crystallogr D Biol Crystallogr 64(Pt 9):950-956.
- Lu GJ, Garen CR, Cherney MM, Cherney LT, Lee C, James MNG (2007) Expression, purification and preliminary X-ray analysis of the C-terminal domain of an arginine repressor protein from Mycobacterium tuberculosis. Acta Crystallogr Sect F Struct Biol Cryst Commun 63(Pt 11):936-939.
The first batch of crystals formed from arginine repressor protein, ArgR, of M. tuberculosis.