Y. Noda

发表

Fatigue crack growth behaviour of A5083 series aluminium alloys and their welded joints

K. Murakami, K. Gotoh, Y. Noda, 2011 .

Potential wave-form measurements of an electrochromic device, WO3/Sb2O5/C, at coloration-bleaching processes using a new quasi-reference electrode

Y. Noda, K. Kuwabara, 1993 .

Ionic conductivity and coulometric titration of copper selenide

Takehiko Takahashi, Y. Noda, O. Yamamoto, 1976 .

Atomic force microscope study of thin‐plate martensites in an Fe–Ni–C alloy

Masahiko Yamamoto, Y. Noda, T. Saburi, 1994 .

Local structures in unfolded lysozyme and correlation with secondary structures in the native conformation: Helix‐forming or ‐breaking propensity of peptide segments

Y. Noda, S. Segawa, Takuji Fukuno, 1991, Biopolymers.

Thermodynamics of the reconstitution of tuna cytochrome c from two peptide fragments

Y. Noda, S. Segawa, Atsushi Yokota, 1998, Protein science : a publication of the Protein Society.

Electrophoretic preparation of antimonic acid film

Y. Noda, K. Kuwabara, 1993, Journal of Materials Science.

The thermal conductivity of U3O8−z from 200 to 750 K

Y. Noda, K. Naito, 1979 .

NMR and CD analysis of an intermediate state in the thermal unfolding process of mouse lipocalin-type prostaglandin D synthase.

T. Inui, Y. Noda, S. Nishimura, 2012, Journal of biochemistry.

Glycerol‐enhanced detection of a preferential structure latent in unstructured 1SS‐variants of lysozyme

K. Kasai, H. Tachibana, Y. Noda, 2012, Biopolymers.

NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins.

A. Yokota, H. Tachibana, Satoshi Iimura, 2004, Biochemistry.

NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure.

A. Yokota, H. Tachibana, Y. Noda, 2002, Biochemistry.

The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge.

Y. Kubo, A. Yokota, H. Tachibana, 2000, Journal of molecular biology.

Specificity of trypsin digestion and conformational flexibility at different sites of unfolded lysozyme

Y. Noda, S. Segawa, Takuji Fukuno, 1994, Biopolymers.

NMR analysis of a kinetically trapped intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase.

Y. Noda, S. Segawa, H. Sugimoto, 2011, Journal of molecular biology.

The confirmation of the denatured structure of pyrrolidone carboxyl peptidase under nondenaturing conditions: Difference in helix propensity of two synthetic peptides with single amino acid substitution

K. Yutani, Satoshi Iimura, Y. Noda, 2008, Proteins.

Unusually slow denaturation and refolding processes of pyrrolidone carboxyl peptidase from a hyperthermophile are highly cooperative: real-time NMR studies.

K. Yutani, K. Ogasahara, Satoshi Iimura, 2004, Biochemistry.

Glycerol‐induced folding of unstructured disulfide‐deficient lysozyme into a native‐like conformation

H. Tachibana, K. Sakamoto, Y. Noda, 2009, Biopolymers.