M. Doi

发表

Different effects of 4-hydroxyproline and 4-fluoroproline on the stability of collagen triple helix.

T. Nakazawa, S. Uchiyama, Yuji Kobayashi, 2005, Biochemistry.

Collagen‐like triple helix formation of synthetic (Pro‐Pro‐Gly)10 analogues: (4(S)‐hydroxyprolyl‐4(R)‐hydroxyprolyl‐Gly)10, (4(R)‐hydroxyprolyl‐4(R)‐hydroxyprolyl‐Gly)10 and (4(S)‐fluoroprolyl‐4(R)‐fluoroprolyl‐Gly)10

T. Nakazawa, S. Uchiyama, Yuji Kobayashi, 2005, Journal of peptide science : an official publication of the European Peptide Society.

Crystal structure of the collagen triple helix model [{PRO-HYP(R)-GLY}4-{HYP(S)-Pro-GLY}2-{PRO-HYP(R)-GLY}4]3

Y. Kang, T. Nakazawa, S. Uchiyama, 2012 .

The triple helical structure and stability of collagen model peptide with 4(s)‐hydroxyprolyl‐pro‐gly units

Y. Kang, T. Nakazawa, S. Uchiyama, 2012, Biopolymers.

Characterization of collagen model peptides containing 4-fluoroproline; (4(S)-fluoroproline-pro-gly)10 forms a triple helix, but (4(R)-fluoroproline-pro-gly)10 does not.

T. Nakazawa, S. Uchiyama, Yuji Kobayashi, 2003, Journal of the American Chemical Society.

Simple and efficient syntheses of Boc- and Fmoc-protected 4( R )- and 4( S )-fluoroproline solely from 4( R )-hydroxyproline

T. Nakazawa, S. Uchiyama, Yuji Kobayashi, 2002 .

Synthesis of novel all-cis-functionalized cyclopropane template-assembled collagen models

T. Nakazawa, Yuji Kobayashi, M. Doi, 2001 .

Conformations in the Solid State and Solubility Properties of Protected Homooligopeptides of Glycine and β-Alanine

M. Doi, M. Narita, K. Kudo, 1986 .

The Ability of the Proline Residue to Promote Successive-Intramolecular Hydrogen Bonds in Oligopeptides

M. Doi, M. Narita, R. Wakita, 1986 .

The Ability of an α-Aminoisobutyric Acid Residue to Promote Helical Folding in Oligopeptides

M. Doi, K. Ishikawa, M. Narita, 1985 .

Syntheses and Properties of Oligo-L-leucines Containing α-Aminoisobutyric Acid Residues. The Novel Strategy for Solubility Improvement in Helical Oligopeptides Based on the Restriction of the Values of the Backbone Dihedral Angles φ and ψ of α-Aminoisobutyric Acid Residues

M. Doi, K. Ishikawa, M. Narita, 1985 .

Polymorphism of collagen triple helix revealed by 19F NMR of model peptide [Pro-4(R)-hydroxyprolyl-Gly]3-[Pro-4(R)-fluoroprolyl-Gly]-[Pro-4(R)-hydroxyprolyl-Gly]3.

T. Nakazawa, S. Uchiyama, D. Motooka, 2012, The journal of physical chemistry. B.

Conformational analysis of elcatonin in solution.

Y. Kyōgoku, S. Nishimura, M. Doi, 1994, European journal of biochemistry.

OXIDATION OF AZULENE DERIVATIVES. AUTOXIDATION OF GUAIAZULENE IN A POLAR APROTIC SOLVENT

S. Takekuma, M. Doi, T. Nozoe, 1984 .

Conformational preferences of 4-chloroproline residues.

Byung Jin Byun, Y. Kang, T. Nakazawa, 2012, Biopolymers.

Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductases.

L. Moroder, F. Siedler, H. Musiol, 1993, Biochemistry.

Conformational analysis of human calcitonin in solution

Yuji Kobayashi, T. Ohkubo, S. Nishimura, 2006, Journal of peptide science : an official publication of the European Peptide Society.

Quartz crystal microbalance sensor for the detection of collagen model peptides based on the formation of triple helical structure.

S. Morita, Ko-jyoh Tanaka, M. Doi, 2021, Journal of bioscience and bioengineering.

Solution structure of a human calcitonin analog elucidated by NMR and distance geometry calculations.

Y. Kyōgoku, K. Yamasaki, M. Doi, 2009, International journal of peptide and protein research.

The α-Helical Conformation of the Aib-Containing Oligopeptide, Boc–(Leu3–Aib)2–OBzl

K. Okuyama, M. Doi, M. Narita, 1988 .

Stabilization mechanism of triple helical structure of collagen molecules

T. Nakazawa, Yuji Kobayashi, T. Ohkubo, 2003, Letters in Peptide Science.