Zobrazeno 1 - 10
of 157
pro vyhledávání: '"K. E. Van Holde"'
Publikováno v:
The Biological bulletin. 173(1)
The hemocyanin-like molecule found in the blood of the most primitive bivalves (protobranchs) reversibly binds O2. Its respiratory properties and its sedimentation behavior are both distinctive. Although its electron-dense image looks like that of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fcbf9a999ef36312d90142c1b12bead
https://pubmed.ncbi.nlm.nih.gov/29314995
https://pubmed.ncbi.nlm.nih.gov/29314995
Autor:
Thomas P. Ellen, K. E. Van Holde
Publikováno v:
Biochemistry. 43:7867-7872
The interaction of linker histone H1 with both linear and superhelical double-stranded DNA has been investigated at low ionic strengths. Gel mobility retardation experiments demonstrate strikingly different behavior for the two forms of DNA. First, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8157be056eae06dd4bee48a455886299
https://doi.org/10.1021/bi0497704
https://doi.org/10.1021/bi0497704
Autor:
K. E. Van Holde, Thomas D. Yager
Publikováno v:
Biochemistry and Cell Biology. 81:169-172
Nucleosome remodeling has been shown, in many cases, to involve cis displacement of nucleosomes on the DNA. This process seems similar to the long-recognized random diffusion of nucleosomes along DNA, but the remodeling process is unidirectional and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9abb7aa984005766b8bbb2c96e5c9d03
https://doi.org/10.1139/o03-038
https://doi.org/10.1139/o03-038
Autor:
K. E. Van Holde
Publikováno v:
Biophysical Chemistry. 100:71-79
The development of protein structural chemistry during the twentieth century is briefly reviewed. Emphasis is placed on certain major problems that have defined the field, and how they have been resolved, often as a consequence of technological advan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7e1011d44b58cd920c090b6c6a89fed
https://doi.org/10.1016/s0301-4622(02)00263-6
https://doi.org/10.1016/s0301-4622(02)00263-6
Publikováno v:
Biophysical Chemistry. 86:165-172
In contrast to small allosteric systems (like hemoglobin) those containing very large numbers ( n ) of binding sites never exhibit cooperativity (as measured by the Hill coefficient, n H ) even approaching the potential limit, n . The reason for this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2796de5506dd8092f161031bc548e258
https://doi.org/10.1016/s0301-4622(00)00154-x
https://doi.org/10.1016/s0301-4622(00)00154-x
Autor:
G. J. Carter, K. E. Van Holde
Publikováno v:
Biochemistry. 37:12477-12488
The ability of avian-specific linker histone H5, and the globular domains of H5 (GH5) and H1(0) (GH1(0), to self-associate either free in solution or when bound to DNA was investigated. All three proteins underwent a salt-dependent increase in turbid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e1d2580df2a9f9b72e635f7440f906b
https://doi.org/10.1021/bi980716v
https://doi.org/10.1021/bi980716v
Publikováno v:
Biophysical Journal. 72(3):1388-1395
In chromatin, the physiological amount of H1 is one molecule per nucleosome or, roughly, one molecule per 200 bp of DNA. We observed that at such a stoichiometry, H1 selectively binds to supercoiled DNA with magnitude of sigma > or = 0.012 (both nega
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3df5005131f80a73cde9d6a8dffeae1f
Autor:
Bruno Samorì, K. E. Van Holde, Jordanka Zlatanova, Guoliang Yang, Charles H. Robert, Sanford H. Leuba, Carlos Bustamante
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 1994, 91 (24), pp.11621-11625. ⟨10.1073/pnas.91.24.11621⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 1994, 91 (24), pp.11621-11625. ⟨10.1073/pnas.91.24.11621⟩
Unfixed chicken erythrocyte chromatin fibers in very low salt have been imaged with a scanning force microscope operating in the tapping mode in air at ambient humidity. These images reveal a three-dimensional organization of the fibers. The planar "
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57a83306782309981a4431ce0379b1cf
https://doi.org/10.1073/pnas.91.24.11621
https://doi.org/10.1073/pnas.91.24.11621
Publikováno v:
Proceedings of the National Academy of Sciences. 91:11567-11570
To elucidate the function of lysine-rich histone, yeast cells, which are believed to lack this histone, were transformed with an expression vector carrying the sea urchin histone H1 gene under control of an inducible promoter. Expression of full-leng
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c6740cc2f490074583f3c7a10e97c21
https://doi.org/10.1073/pnas.91.24.11567
https://doi.org/10.1073/pnas.91.24.11567
Publikováno v:
Proceedings of the National Academy of Sciences. 91:3525-3529
We have compared chicken erythrocyte linker histones H1 and H5 binding to a synthetic four-way DNA junction. Each histone binds to form a single complex, with an affinity which permits competition against a large excess of linear duplex DNA. The affi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e490d2b0f32f1a161901d43fd305c5b6
https://doi.org/10.1073/pnas.91.9.3525
https://doi.org/10.1073/pnas.91.9.3525