Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Kathleen Wallis"'
Autor:
Salman Azhar, Sally A. Lewis, Michael B. Rho, Kathleen Wallis, Douglas B. Murphy, Nicholas J. Cowan
Publikováno v:
Journal of Biological Chemistry. 268:15158-15167
The mechanism of binding of microtubule-associated protein 2 (MAP2) to taxol-stabilized microtubules (MTs) was examined through Scatchard analysis of equilibrium binding and by immunoelectron microscopy. We demonstrate the following. 1) Binding is a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bafa1f1cafe43e69c4638afca24f9aa9
https://doi.org/10.1016/s0021-9258(18)82450-4
https://doi.org/10.1016/s0021-9258(18)82450-4
Publikováno v:
The Journal of Cell Biology
Cells contain multiple tubulin isotypes that are the products of different genes and posttranslational modifications. It has been proposed that tubulin isotypes become segregated into different classes of microtubules each adapted to specific activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1058009e15cf4a6f34f6af0ae1684e7
http://europepmc.org/articles/PMC2115985
http://europepmc.org/articles/PMC2115985
Publikováno v:
Journal of Biological Chemistry. 262:14305-14312
We report here the complete sequence of a highly divergent chicken erythrocyte beta-tubulin, c beta 6, which appears to represent a major exception to the observation that the primary sequences and sites of expression of beta-tubulin isotypes are con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::063fb2612cb07c74957cb3b55d593bbf
https://doi.org/10.1016/s0021-9258(18)47938-0
https://doi.org/10.1016/s0021-9258(18)47938-0
Autor:
Allan Fenselau, Kathleen Wallis
Publikováno v:
Biochemistry. 13:3884-3888
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36bf48674ccfd9a6050f9a28f7015fe6
https://doi.org/10.1021/bi00716a010
https://doi.org/10.1021/bi00716a010
Autor:
Allan Fenselau, Kathleen Wallis
Publikováno v:
Biochemical Journal. 142:619-627
1. Tissue activities, intracellular distribution as well as selected kinetic and molecular properties of succinyl-CoA–3-oxo acid CoA transferase (EC 2.8.3.5), which is an initiator of ketone body usage, were examined in rat kidney, heart, brain, sk
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a048ad5974b997ab51b5651f1597d40
https://doi.org/10.1042/bj1420619
https://doi.org/10.1042/bj1420619
Autor:
Allan Fenselau, Kathleen Wallis
Publikováno v:
Life sciences. 15(4)
Succinyl-CoA: acetoacetate CoA transferases from rat kidney, heart, brain, and skeletal muscle display substrate inhibition by acetoacetate that is characterized by an “inversion concentration” of 4–6 mM acetoacetate, i.e., at acetoacetate conc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aac4b7d239360edc2262b4a1fdce30e3
https://pubmed.ncbi.nlm.nih.gov/4549944
https://pubmed.ncbi.nlm.nih.gov/4549944
Autor:
Allan Fenselau, Kathleen Wallis
Publikováno v:
Biochemical and biophysical research communications. 62(2)
Summary Succinyl-CoA:acetoacetate CoA transferase, which forms a covalent intermediate with CoA, can be readily purified from rat kidney, heart, brain, and skeletal muscle using an acetoacetyl-CoA-agarose column. Significant purification (20–180 fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e8f73568237a3629e3ed14da0b1ab66
https://pubmed.ncbi.nlm.nih.gov/1111526
https://pubmed.ncbi.nlm.nih.gov/1111526
Autor:
Kathleen Wallis, Allan Fenselau
Publikováno v:
Life sciences. Pt. 2: Biochemistry, general and molecular biology. 12(4)
Studies on the mouse hepatoma BW7756 reveal that mitochondria from the neoplastic tissue, unlike those from normal liver tissue, are able to utilize ketone bodies as respiratory substrates and contain succinyl-CoA: acetoacetate CoA transferase. This
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57e9927b0abb630be50810c9df2cd21c
https://pubmed.ncbi.nlm.nih.gov/4350669
https://pubmed.ncbi.nlm.nih.gov/4350669