S. Tuzi

A. Naito, I. Kawamura, S. Tuzi, 2015, Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology.

Participation of the BC Loop in the Correct Folding of Bacteriorhodopsin as Revealed by Solid‐state NMR †

A. Naito, I. Kawamura, S. Tuzi, 2009, Photochemistry and photobiology.

Dynamic aspects of extracellular loop region as a proton release pathway of bacteriorhodopsin studied by relaxation time measurements by solid state NMR.

A. Naito, H. Saitǒ, I. Kawamura, 2007, Biochimica et biophysica acta.

Pressure‐induced Isomerization of Retinal on Bacteriorhodopsin as Disclosed by Fast Magic Angle Spinning NMR †

A. Naito, H. Saitǒ, K. Nishimura, 2007, Photochemistry and photobiology.

Local protein structure and dynamics at kinked transmembrane α-helices of [1-13C]Pro-labeled bacteriorhodopsin as revealed by site-directed solid-state 13C NMR

A. Naito, H. Saitǒ, S. Tuzi, 2003 .

Dynamic structure of pharaonis phoborhodopsin (sensory rhodopsin II) and complex with a cognate truncated transducer as revealed by site‐directed 13C solid‐state NMR

H. Saitǒ, N. Kamo, S. Tuzi, 2003, FEBS letters.

Tolerance to freezing stress in cyanobacteria, Nostoc commune and some cyanobacteria with various tolerances to drying stress

Y. Kashino, S. Tuzi, M. Hirai, 2004 .

Structure and orientation of dynorphin bound to lipid bilayers by 13C solid-state NMR

A. Naito, H. Saitǒ, K. Nishimura, 2005 .

Change in local dynamics of bacteriorhodopsin with retinal isomerization under pressure as studied by fast magic angle spinning NMR

H. Saito, A. Naito, I. Kawamura, 2012 .

Determination of the N–H Bond Lengths for Simple Peptides in the Solid State by Natural Abundance 15N Two-Dimensional Separated Local Dipolar Field (2D-SLDF) NMR Spectroscopy

A. Naito, S. Tuzi, H. Saitô, 1993 .

Chapter 2 Dipolar interactions and interatomic distances

A. Naito, S. Tuzi, H. Saitô, 1998 .

Evidence of local conformational fluctuations and changes in bacteriorhodopsin, dependent on lipids, detergents and trimeric structure, as studied by 13C NMR.

J. Lanyi, A. Naito, M. Tanio, 1998, Biochimica et biophysica acta.

Dynamics Change of Phoborhodopsin and Transducer by Activation: Study Using D75N Mutant of the Receptor by Site‐directed Solid‐state 13C NMR †

A. Naito, N. Kamo, I. Kawamura, 2008, Photochemistry and photobiology.

Conformation and dynamics of the [3-(13)C]Ala, [1-(13)C]Val-labeled truncated pharaonis transducer, pHtrII(1-159), as revealed by site-directed (13)C solid-state NMR: changes due to association with phoborhodopsin (sensory rhodopsin II).

A. Naito, N. Kamo, S. Tuzi, 2004, Biophysical journal.

with Phoborhodopsin (Sensory Rhodopsin II)

A. Naito, N. Kamo, S. Tuzi, 2004 .

Morphological behavior of lipid bilayers induced by melittin near the phase transition temperature.

A. Naito, S. Izumi, S. Tuzi, 2005, Biophysical journal.

Dynorphin induced magnetic ordering in lipid bilayers as studied by (31)P NMR spectroscopy.

A. Naito, S. Tuzi, T. Nagao, 2002, Biochimica et biophysica acta.

Dynamic aspects of membrane proteins and membrane-associated peptides as revealed by 13C NMR: Lessons from bacteriorhodopsin as an intact protein

A. Naito, M. Tanio, S. Tuzi, 2002 .

Conformation and dynamics of melittin bound to magnetically oriented lipid bilayers by solid-state (31)P and (13)C NMR spectroscopy.

H. Saito, A. Naito, S. Tuzi, 2000, Biophysical journal.

Conformation and Dynamics of Melittin Bound to Magnetically Oriented Lipid Bilayers by Solid-State

A. Naito, S. Tuzi, T. Nagao, 2000 .

Participation of the Surface Structure of Pharaonis Phoborhodopsin, ppR and its A149S and A149V mutants, Consisting of the C‐terminal α‐helix and E–F Loop, in the Complex‐formation with the Cognate Transducer pHtrII, as Revealed by Site‐directed 13C Solid‐state NMR †

A. Naito, N. Kamo, I. Kawamura, 2007, Photochemistry and photobiology.

Chapter 24 - Polysaccharides and biological systems

A. Naito, S. Tuzi, H. Saitô, 1998 .

Membrane-induced alteration of the secondary structure in the SWAP-70 pleckstrin homology domain.

T. Ikegami, H. Yagisawa, S. Tuzi, 2012, Journal of biochemistry.

Strain of a Cellulose-Producing Bacterium Carboxymethylcellulase Gene-Disrupted Formation of Highly Twisted Ribbons in a

T. Nakai, T. Imai, K. Oiwa, 2014 .

Surface and Dynamic Structures of Bacteriorhodopsin in a 2D Crystal, a Distorted or Disrupted Lattice, as Revealed by Site‐directed Solid‐state 13C NMR †

A. Naito, M. Tanio, S. Tuzi, 2007, Photochemistry and photobiology.

Cytoplasmic surface structures of bacteriorhodopsin modified by site-directed mutations and cation binding as revealed by 13C NMR

S. Tuzi, S. Yamaguchi, H. Saitô, 2003, European Biophysics Journal.

A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c oxidase and lysozyme. Dynamic behavior of protein and detergent in the complex.

K. Shinzawa-Itoh, A. Naito, S. Tuzi, 1992, European journal of biochemistry.

Determination of the three-dimensional structure of a new crystalline form of N-acetyl-Pro-Gly-Phe as revealed by 13 C REDOR, X-ray diffraction, and molecular dynamics calculation

M. Aida, N. Yasuoka, A. Naito, 1996 .

The structure and mobility of l-alanine residues of tropomyosin in the solid state as studied by high resolution solid state 13C NMR spectroscopy

I. Ando, S. Tuzi, Satoshi Sakamaki, 1990 .

The 13C-NMR chemical shift and the higher order structure of l-alanine residues in tropomyosin in the solid state and in solution

I. Ando, S. Tuzi, 1989 .

13C‐nmr chemical shift and conformation of L‐alanine residues incorporated into poly(β‐benzyl L‐aspartate) in the solid state

I. Ando, T. Ozaki, A. Shoji, 1987 .

Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.

A. Naito, M. Tanio, S. Tuzi, 2000, Biochimica et biophysica acta.

Role of aromatic residues in amyloid fibril formation of human calcitonin by solid-state 13C NMR and molecular dynamics simulation.

A. Naito, S. Tuzi, K. Ueda, 2013, Physical chemistry chemical physics : PCCP.

Structure and Dynamics of the Phospholipase C-δ1 Pleckstrin Homology Domain Located at the Lipid Bilayer Surface*

M. Okada, H. Yagisawa, S. Tuzi, 2003, Journal of Biological Chemistry.

Phosphatidylserine induces functional and structural alterations of the membrane‐associated pleckstrin homology domain of phospholipase C‐δ1

M. Okada, H. Yagisawa, S. Tuzi, 2007, The FEBS journal.

Effect of Electrostatic Interaction on Fibril Formation of Human Calcitonin as Studied by High Resolution Solid State 13C NMR*

A. Naito, S. Tuzi, A. Nosaka, 2003, The Journal of Biological Chemistry.

Empirical Versus N On Empirical Evaluation Of Secondary Structure Of Fibrous And Membrane Proteins By Solid-State Nmr: A Practical Approach

A. Naito, S. Tuzi, H. Saitô, 1998 .

Determination of principal components and their directions of 15N chemical shift tensor and N–H bond lengths in simple peptides as parameters for characterization of N–H⋯OC hydrogen bonds

A. Naito, S. Tuzi, Akira Fukutani, 2002 .

A high-resolution 15N solid-state NMR study of collagen and related polypeptides. The effect of hydration on formation of interchain hydrogen bonds as the primary source of stability of the collagen-type triple helix.

A. Naito, S. Tuzi, H. Saitô, 1994, European journal of biochemistry.

Solid-state NMR studies of two backbone conformations at Tyr185 as a function of retinal configurations in the dark, light, and pressure adapted bacteriorhodopsins.

A. Naito, K. Nishimura, I. Kawamura, 2007, Journal of the American Chemical Society.

Suppressed or recovered intensities analysis in site-directed (13)C NMR: assessment of low-frequency fluctuations in bacteriorhodopsin and D85N mutants revisited.

A. Naito, M. Tanio, S. Tuzi, 2010, Biochimica et biophysica acta.

Conformational changes of bacteriorhodopsin along the proton-conduction chain as studied with (13)C NMR of [3-(13)C]Ala-labeled protein: arg(82) may function as an information mediator.

J. Lanyi, A. Naito, M. Tanio, 1999, Biophysical Journal.

Dynamic aspect of bacteriorhodopsin as viewed from 13C NMR: Conformational elucidation, surface dynamics and information transfer from the surface to inner residues

M. Tanio, S. Tuzi, S. Yamaguchi, 2002 .

Inter- and intra-molecular contributions of neighboring dipolar pairs to the precise determination of interatomic distances in a simple [13C, 15N]-peptide by 13C, 15N-REDOR NMR spectroscopy

K. Nishimura, S. Tuzi, H. Saitô, 1994 .

Conformation and dynamics of membrane proteins and biologically active peptides as studied by high-resolution solid-state 13C NMR

A. Naito, M. Tanio, K. Nishimura, 1998 .

A high-resolution solid-state 13C-NMR study on [1-13C]Ala and [3-13C]Ala and [1-13C]Leu and Val-labelled bacteriorhodopsin. Conformation and dynamics of transmembrane helices, loops and termini, and hydration-induced conformational change.

A. Naito, S. Tuzi, H. Saitô, 1993, European journal of biochemistry.

Dynamics and orientation of transmembrane peptide from bacteriorhodopsin incorporated into lipid bilayer as revealed by solid state (31)P and (13)C NMR spectroscopy.

A. Naito, S. Tuzi, S. Kimura, 2002, Biopolymers.

Structure and Dynamics of Membrane-Bound Proteins

M. Tanio, K. Nishimura, S. Tuzi, 2016 .

Temperature-dependent conformational change of bacteriorhodopsin as studied by solid-state 13C NMR.

A. Naito, S. Tuzi, H. Saitô, 1996, European journal of biochemistry.

Stability of the C-terminal alpha-helical domain of bacteriorhodopsin that protrudes from the membrane surface, as studied by high-resolution solid-state 13C NMR.

J. Lanyi, A. Naito, M. Tanio, 1998, Journal of biochemistry.

Long-distance effects of site-directed mutations on backbone conformation in bacteriorhodopsin from solid state NMR of [1-13C]Val-labeled proteins.

J. Lanyi, A. Naito, M. Tanio, 1999, Biophysical journal.

A (13)C NMR study on [3-(13)C]-, [1-(13)C]Ala-, or [1-(13)C]Val-labeled transmembrane peptides of bacteriorhodopsin in lipid bilayers: insertion, rigid-body motions, and local conformational fluctuations at ambient temperature.

A. Naito, S. Tuzi, S. Kimura, 2001, Biopolymers.

13C NMR study on conformation and dynamics of the transmembrane alpha-helices, loops, and C-terminus of [3-13C]Ala-labeled bacteriorhodopsin.

A. Naito, S. Tuzi, H. Saitô, 1994, Biochemistry.

Irreversible conformational change of bacterio-opsin induced by binding of retinal during its reconstitution to bacteriorhodopsin, as studied by (13)C NMR.

J. Lanyi, A. Naito, M. Tanio, 2000, Journal of biochemistry.

A. Naito, N. Kamo, I. Kawamura, 2007, Photochemistry and photobiology.

Site‐directed 13C solid‐state NMR studies on membrane proteins: strategy and goals toward revealing conformation and dynamics as illustrated for bacteriorhodopsin labeled with [1‐13C]amino acid residues

M. Tanio, S. Tuzi, S. Yamaguchi, 2004, Magnetic resonance in chemistry : MRC.

Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimensional array formation as revealed by site-directed solid-state 13C NMR studies on [3-13C]Ala- and [1-13C]Val-labeled bacteriorhodopsin.

S. Tuzi, S. Yamaguchi, H. Saitô, 2003, Biochimica et biophysica acta.

Regio-selective detection of dynamic structure of transmembrane alpha-helices as revealed from (13)C NMR spectra of [3-13C]Ala-labeled bacteriorhodopsin in the presence of Mn2+ ion.

A. Naito, J. Hasegawa, S. Tuzi, 2001, Biophysical journal.

Dynamic aspect of bacteriorhodopsin as a typical membrane protein as revealed by site-directed solid-state 13C NMR.

S. Tuzi, S. Yamaguchi, H. Saitô, 2004, Solid state nuclear magnetic resonance.

Conformation and dynamics of [3-13C]Ala- labeled bacteriorhodopsin and bacterioopsin, induced by interaction with retinal and its analogs, as studied by 13C nuclear magnetic resonance.

J. Lanyi, A. Naito, S. Tuzi, 1996, Biochemistry.