Cloned mouse ribonucleotide reductase subunit M1 cDNA reveals amino acid sequence homology with Escherichia coli and herpesvirus ribonucleotide reductases.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)88881-0 ◽

1985 ◽

Vol 260 (11) ◽

pp. 7015-7022 ◽

Author(s):

I W Caras ◽

B B Levinson ◽

M Fabry ◽

S R Williams ◽

D W Martin

Keyword(s):

Escherichia Coli ◽

Amino Acid Sequence ◽

Ribonucleotide Reductase ◽

Sequence Homology ◽

Amino Acid Sequence Homology ◽

Ribonucleotide Reductases

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Amino acid sequence homology in 30 S ribosomal protein S19 from Bacillus stearothermophilus and Escherichia coli

Biochimica et Biophysica Acta (BBA) - Protein Structure ◽

10.1016/0005-2795(76)90313-5 ◽

1976 ◽

Vol 427 (1) ◽

pp. 371-374 ◽

Author(s):

Artemios Vassos ◽

Ken-Ichi Higo ◽

Leon Marcus

Keyword(s):

Escherichia Coli ◽

Amino Acid Sequence ◽

Ribosomal Protein ◽

Sequence Homology ◽

Bacillus Stearothermophilus ◽

Amino Acid Sequence Homology ◽

Ribosomal Protein S19

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The periplasmic endonuclease I of escherichia coli has amino-acid sequence homology to the extracellular DNases of Vibrio cholerae and Aeromonas hydrophila

Gene ◽

10.1016/0378-1119(94)00835-g ◽

1995 ◽

Vol 154 (1) ◽

pp. 55-59 ◽

Author(s):

Manfred Jekel ◽

Wilfried Wackernagel

Keyword(s):

Escherichia Coli ◽

Amino Acid Sequence ◽

Vibrio Cholerae ◽

Sequence Homology ◽

Aeromonas Hydrophila ◽

Amino Acid Sequence Homology

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An acidic, alanine-rich 50 S ribosomal protein from Halobacterium cutirubrum : Amino acid sequence homology with Escherichia coli proteins L7 and L12

FEBS Letters ◽

10.1016/0014-5793(74)80983-x ◽

1974 ◽

Vol 43 (2) ◽

pp. 127-130 ◽

Author(s):

G. Oda ◽

A.R. Strøm ◽

L.P. Visentin ◽

M. Yaguchi

Keyword(s):

Escherichia Coli ◽

Amino Acid Sequence ◽

Ribosomal Protein ◽

Sequence Homology ◽

Amino Acid Sequence Homology

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Amino acid sequence homology between cholera toxin and Escherichia coli heat-labile toxin

Nature ◽

10.1038/288499a0 ◽

1980 ◽

Vol 288 (5790) ◽

pp. 499-501 ◽

Author(s):

Walter S. Dallas ◽

Stanley Falkow

Keyword(s):

Escherichia Coli ◽

Amino Acid Sequence ◽

Cholera Toxin ◽

Sequence Homology ◽

Amino Acid Sequence Homology ◽

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Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase.

Journal of Bacteriology ◽

10.1128/jb.178.15.4508-4514.1996 ◽

1996 ◽

Vol 178 (15) ◽

pp. 4508-4514 ◽

Author(s):

S Zenno ◽

H Koike ◽

A N Kumar ◽

R Jayaraman ◽

M Tanokura ◽

...

Keyword(s):

Escherichia Coli ◽

Amino Acid Sequence ◽

Sequence Homology ◽

Biochemical Characterization ◽

Vibrio Harveyi ◽

Amino Acid Sequence Homology ◽

High Amino Acid ◽

Flavin Oxidoreductase

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Amino acid sequence homology among the major outer membrane proteins of Escherichia coli.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.81.4.1048 ◽

1984 ◽

Vol 81 (4) ◽

pp. 1048-1052 ◽

Author(s):

H. Nikaido ◽

H. C. Wu

Keyword(s):

Escherichia Coli ◽

Membrane Proteins ◽

Amino Acid Sequence ◽

Outer Membrane ◽

Sequence Homology ◽

Outer Membrane Proteins ◽

Amino Acid Sequence Homology

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Amino acid sequence homology applied to the prediction of protein secondary structures, and joint prediction with existing methods

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(86)90131-7 ◽

1986 ◽

Vol 871 (1) ◽

pp. 45-54 ◽

Author(s):

Ken Nishikawa ◽

Tatsuo Ooi

Keyword(s):

Amino Acid Sequence ◽

Sequence Homology ◽

Secondary Structures ◽

Amino Acid Sequence Homology ◽

Protein Secondary Structures ◽

Joint Prediction

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Amino acid sequence homology between rat prostatic steroid binding protein and rabbit uteroglobin

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(83)91631-5 ◽

1983 ◽

Vol 114 (1) ◽

pp. 325-330 ◽

Author(s):

Michael E. Baker

Keyword(s):

Amino Acid Sequence ◽

Sequence Homology ◽

Binding Protein ◽

Amino Acid Sequence Homology ◽

Steroid Binding ◽

Rabbit Uteroglobin ◽

Steroid Binding Protein

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Transforming growth factors produced by retrovirus-transformed rodent fibroblasts and human melanoma cells: amino acid sequence homology with epidermal growth factor.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.80.15.4684 ◽

1983 ◽

Vol 80 (15) ◽

pp. 4684-4688 ◽

Author(s):

H. Marquardt ◽

M. W. Hunkapiller ◽

L. E. Hood ◽

D. R. Twardzik ◽

J. E. De Larco ◽

...

Keyword(s):

Growth Factors ◽

Growth Factor ◽

Epidermal Growth Factor ◽

Amino Acid Sequence ◽

Sequence Homology ◽

Human Melanoma ◽

Transforming Growth Factors ◽

Amino Acid Sequence Homology ◽

Epidermal Growth

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Amino acid sequence homology between muscle and liver aldolases

FEBS Letters ◽

10.1016/0014-5793(71)80406-4 ◽

1971 ◽

Vol 18 (1) ◽

pp. 59-63 ◽

Author(s):

B.G. Forcina ◽

R.N. Perham

Keyword(s):

Amino Acid Sequence ◽

Sequence Homology ◽

Amino Acid Sequence Homology

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