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1.

Geometry of phage head construction.

Moody, M F.

J Mol Biol ; 293(2): 401-33, 1999 Oct 22.

Artículo en Inglés | MEDLINE | ID: mdl-10529353

2.

X-ray scattering titration of the quaternary structure transition of aspartate transcarbamylase with a bisubstrate analogue: influence of nucleotide effectors.

Fetler, L; Tauc, P; Hervé, G; Moody, M F; Vachette, P.

J Mol Biol ; 251(2): 243-55, 1995 Aug 11.

Artículo en Inglés | MEDLINE | ID: mdl-7643401

3.

Kinetics of the allosteric transition of aspartate transcarbamylase. Chemical quench studies.

Kihara, H; Barman, T E; Jones, P T; Moody, M F.

J Mol Biol ; 176(4): 523-34, 1984 Jul 15.

Artículo en Inglés | MEDLINE | ID: mdl-6379193

4.

1H nuclear magnetic resonance studies of an integral membrane protein: subunit c of the F1F0 ATP synthase.

Moody, M F; Jones, P T; Carver, J A; Boyd, J; Campbell, I D.

J Mol Biol ; 193(4): 759-74, 1987 Feb 20.

Artículo en Inglés | MEDLINE | ID: mdl-2886671

5.

Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding.

Hervé, G; Moody, M F; Tauc, P; Vachette, P; Jones, P T.

J Mol Biol ; 185(1): 189-99, 1985 Sep 05.

Artículo en Inglés | MEDLINE | ID: mdl-3900420

6.

Kinetics of structure and activity changes during the allosteric transition of aspartate transcarbamylase.

Kihara, H; Takahashi-Ushijima, E; Amemiya, Y; Honda, Y; Vachette, P; Tauc, P; Barman, T E; Jones, P T; Moody, M F.

J Mol Biol ; 198(4): 745-8, 1987 Dec 20.

Artículo en Inglés | MEDLINE | ID: mdl-3430629

7.

Structural kinetics of the allosteric transition of aspartate transcarbamylase produced by physiological substrates.

Tsuruta, H; Sano, T; Vachette, P; Tauc, P; Moody, M F; Wakabayashi, K; Amemiya, Y; Kimura, K; Kihara, H.

FEBS Lett ; 263(1): 66-8, 1990 Apr 09.

Artículo en Inglés | MEDLINE | ID: mdl-2185037

8.

Stopped-flow solution scattering using synchrotron radiation: apparatus, data collection and data analysis.

Fowler, A G; Foote, A M; Moody, M F; Vachette, P; Provencher, S W; Gabriel, A; Bordas, J; Koch, M H.

J Biochem Biophys Methods ; 7(4): 317-29, 1983 Jul.

Artículo en Inglés | MEDLINE | ID: mdl-6619508

9.

Optical diffraction of electron micrographs of argininosuccinase tubules.

Moody, M F.

Biochim Biophys Acta ; 229(3): 779-84, 1971 Mar 23.

Artículo en Inglés | MEDLINE | ID: mdl-5555224

10.

Structure of the sheath of bacteriophage T4. II. Rearrangement of the sheath subunits during contraction.

Moody, M F.

J Mol Biol ; 25(2): 201-8, 1967 Apr 28.

Artículo en Inglés | MEDLINE | ID: mdl-6034099

11.

Structure of the sheath of bacteriophage T4. I. Structure of the contracted sheath and polysheath.

Moody, M F.

J Mol Biol ; 25(2): 167-200, 1967 Apr 28.

Artículo en Inglés | MEDLINE | ID: mdl-6034098

12.

Sheath of bacteriophage T4. 3. Contraction mechanism deduced from partially contracted sheaths.

Moody, M F.

J Mol Biol ; 80(4): 613-35, 1973 Nov 15.

Artículo en Inglés | MEDLINE | ID: mdl-4589647

13.

X-ray diffraction study of tail-tubes from bacteriophage T2L.

Moody, M F; Makowski, L.

J Mol Biol ; 150(2): 217-44, 1981 Aug 05.

Artículo en Inglés | MEDLINE | ID: mdl-7321045

14.

Changes in the x-ray solution scattering of aspartate transcarbamylase following the allosteric transition.

Moody, M F; Vachette, P; Foote, A M.

J Mol Biol ; 133(4): 517-32, 1979 Oct 09.

Artículo en Inglés | MEDLINE | ID: mdl-395314

15.

Crystallization and preliminary x-ray study of the catalytic subunit of aspartate transcarbamylase.

Foote, A M; Winkler, F K; Moody, M F.

J Mol Biol ; 146(3): 389-91, 1981 Mar 05.

Artículo en Inglés | MEDLINE | ID: mdl-7265236

16.

Zinc-sulfur bonds of aspartate transcarbamylase studied by x-ray absorption spectroscopy.

Phillips, J C; Bordas, J; Foote, A M; Koch, M H; Moody, M F.

Biochemistry ; 21(5): 830-4, 1982 Mar 02.

Artículo en Inglés | MEDLINE | ID: mdl-7041968

17.

Kinetics of the quaternary structure change of aspartate transcarbamylase triggered by succinate, a competitive inhibitor.

Tsuruta, H; Vachette, P; Sano, T; Moody, M F; Amemiya, Y; Wakabayashi, K; Kihara, H.

Biochemistry ; 33(33): 10007-12, 1994 Aug 23.

Artículo en Inglés | MEDLINE | ID: mdl-8060968

18.

Stopped-flow x-ray scattering: the dissociation of aspartate transcarbamylase.

Moody, M F; Vachette, P; Foote, A M; Tardieu, A; Koch, M H; Bordas, J.

Proc Natl Acad Sci U S A ; 77(7): 4040-3, 1980 Jul.

Artículo en Inglés | MEDLINE | ID: mdl-6933451

19.

Letter: Structure determination of membranes in swollen lamellar systems.

Moody, M F.

Biophys J ; 14(9): 697-702, 1974 Sep.

Artículo en Inglés | MEDLINE | ID: mdl-4414410

20.

Application of optical diffraction to helical structures in the bacteriophage tail.

Moody, M F.

Philos Trans R Soc Lond B Biol Sci ; 261(837): 181-95, 1971 May 27.

Artículo en Inglés | MEDLINE | ID: mdl-4399204

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Geometry of phage head construction.

X-ray scattering titration of the quaternary structure transition of aspartate transcarbamylase with a bisubstrate analogue: influence of nucleotide effectors.

Kinetics of the allosteric transition of aspartate transcarbamylase. Chemical quench studies.

1H nuclear magnetic resonance studies of an integral membrane protein: subunit c of the F1F0 ATP synthase.

Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding.

Kinetics of structure and activity changes during the allosteric transition of aspartate transcarbamylase.

Structural kinetics of the allosteric transition of aspartate transcarbamylase produced by physiological substrates.

Stopped-flow solution scattering using synchrotron radiation: apparatus, data collection and data analysis.

Optical diffraction of electron micrographs of argininosuccinase tubules.

Structure of the sheath of bacteriophage T4. II. Rearrangement of the sheath subunits during contraction.

Structure of the sheath of bacteriophage T4. I. Structure of the contracted sheath and polysheath.

Sheath of bacteriophage T4. 3. Contraction mechanism deduced from partially contracted sheaths.

X-ray diffraction study of tail-tubes from bacteriophage T2L.

Changes in the x-ray solution scattering of aspartate transcarbamylase following the allosteric transition.

Crystallization and preliminary x-ray study of the catalytic subunit of aspartate transcarbamylase.

Zinc-sulfur bonds of aspartate transcarbamylase studied by x-ray absorption spectroscopy.

Kinetics of the quaternary structure change of aspartate transcarbamylase triggered by succinate, a competitive inhibitor.

Stopped-flow x-ray scattering: the dissociation of aspartate transcarbamylase.

Letter: Structure determination of membranes in swollen lamellar systems.

Application of optical diffraction to helical structures in the bacteriophage tail.