The amino acid sequence of cytochrome <i>c</i> from <i>Eisenia foetida</i> (Savigny) (Common brandling worm)

Lyddiatt, Andrew; Boulter, D.

doi:10.1016/0014-5793(76)80022-1

Search citation statements

Order By: Relevance

Paper Sections

Select...

Discussion1

Citation Types

Supporting

Mentioning

Contrasting

Year Published

1976

1982

Publication Types

Select...

Article5

Relationship

Self Cite1

Independent4

Authors

Journals

Cited by 7 publications

(1 citation statement)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is the first echinoderm sequence to be determined and like the Helix sequence [16] possesses a non-acetylated, N-terminal glycine in position-1 of the alignment. Of the remaining invertebrates, the insect sequences [1,5,17] and the annelid sequence [18] all have a non-acetylated tail of 4 or 5 residues at the N-terminus, whilst the crustacean has no such tail and carries a blocked N-terminus [19].…”

Section: Discussionmentioning

confidence: 99%

The amino acid sequence of cytochrome c from Asterias Rubens L. (Common starfish)

Lyddiatt

Boulter

1976

FEBS Letters

Self Cite

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

The amino acid sequence of cytochrome c from Asterias Rubens L. (Common starfish)

Lyddiatt

Boulter

1976

FEBS Letters

Self Cite

View full text Add to dashboard Cite

Evolutionary changes in protein composition — evidence for an optimal strategy

1979

View full text Add to dashboard Cite

The information contained in the composition of different proteins of the same family is analyzed. It is found that within each family the gain in information per amino acid replacement is constant. This finding is interpreted to imply that evolutionary changes in proteins follow an "optimal" path in the sense that they maximize the number of potentially functional sequences that can be generated by T accepted point mutations from a given protein, subject to restrictions due to biological function.

show abstract

Evolutionary change in invertebrate cytochromec

1978

View full text Add to dashboard Cite

Recently published amino acid sequences are compared to those of other cytochromes c. Molecular phylogenies constructed by using an ancestral sequence method are compared to the classical biological view of invertebrate evolution. Problems associated with the analysis of sequences of different chain lengths and of high variability are discussed, and the logistics of increasing the representation of key invertebrate phyla is assessed.

show abstract

The amino acid sequence of cytochrome c from Eisenia foetida (Savigny) (Common brandling worm)

Cited by 7 publications

References 15 publications

The amino acid sequence of cytochrome c from Asterias Rubens L. (Common starfish)

The amino acid sequence of cytochrome c from Asterias Rubens L. (Common starfish)

Evolutionary changes in protein composition — evidence for an optimal strategy

Evolutionary change in invertebrate cytochromec

Contact Info

Product

Resources

About