Výsledky vyhledávání - "B M, Alberts"

Are our universities producing too many PhDs?

Autor: B M, Alberts

Publikováno v: Trends in cell biology. 9(12)

As we enter the 21st century, we face a world that will be increasingly dominated by science and technology. More and more jobs will require many of the analytical and thinking skills of a scientist. Citizens everywhere must also become better able t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9d96cc62ec922ab7c0a047bbba611e3c
https://pubmed.ncbi.nlm.nih.gov/10611688

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Proposed changes for NIH's Center for Scientific Review. Panel on Scientific Boundaries for Review. Center for Scientific Review Advisory Committee, National Institutes of Health

Autor: B M, Alberts, F J, Ayala, D, Botstein, E, Frank, E W, Holmes, R D, Lee, E R, Macagno, P, Marrack, S, Oparil, S H, Orkin, A H, Rubenstein, C W, Slayman, P F, Sparling, L R, Squire, P H, von Hippel, K R, Yamamoto

Publikováno v: Science (New York, N.Y.). 285(5428)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f7a07845e3390f46a452f864875b2041
https://pubmed.ncbi.nlm.nih.gov/10515787

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Isolation of centrosomes from Drosophila embryos

Autor: M, Moritz, B M, Alberts

Publikováno v: Methods in cell biology. 61

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::845cc00e07f2978b4acd72251262ad8c
https://pubmed.ncbi.nlm.nih.gov/9891306

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The rapid dissociation of the T4 DNA polymerase holoenzyme when stopped by a DNA hairpin helix. A model for polymerase release following the termination of each Okazaki fragment

Autor: K J, Hacker, B M, Alberts

Publikováno v: The Journal of biological chemistry. 269(39)

We have examined the molecular mechanism that enables the T4 bacteriophage DNA polymerase holoenzyme to synthesize DNA processively on the leading strand of the replication fork for many minutes, while allowing an identical holoenzyme on the lagging

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9323e08c62fbd9aca150a048ffeba4f0
https://pubmed.ncbi.nlm.nih.gov/7929078

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The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme

Autor: K J, Hacker, B M, Alberts

Publikováno v: The Journal of biological chemistry. 269(39)

We have developed an experimental assay to monitor the rate of dissociation of the T4 DNA polymerase holoenzyme (polymerase plus gene 44/62 and 45 proteins) once it has been stalled by nucleotide omission. Using this assay, we determined that the dis

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https://pubmed.ncbi.nlm.nih.gov/7929077

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Overexpression, purification, sequence analysis, and characterization of the T4 bacteriophage dda DNA helicase

Autor: K J, Hacker, B M, Alberts

Publikováno v: The Journal of biological chemistry. 267(29)

The bacteriophage T4 dda protein is a 5'-3' DNA helicase that stimulates DNA replication and recombination reactions in vitro and seems to play a role in the initiation of T4 DNA replication in vivo. Oligonucleotide probes based on NH2-terminal amino

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https://pubmed.ncbi.nlm.nih.gov/1328208

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The T4 DNA polymerase accessory proteins form an ATP-dependent complex on a primer-template junction

Autor: M M, Munn, B M, Alberts

Publikováno v: The Journal of biological chemistry. 266(30)

The DNA polymerase holoenzyme of bacteriophage T4 contains, besides the DNA polymerase itself (the gene 43 protein), a complex of the protein products of T4 genes 44 and 62 (a DNA-dependent ATPase) and of gene 45. Together, the 44/62 and 45 proteins

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https://pubmed.ncbi.nlm.nih.gov/1939066

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DNA footprinting studies of the complex formed by the T4 DNA polymerase holoenzyme at a primer-template junction

Autor: M M, Munn, B M, Alberts

Publikováno v: The Journal of biological chemistry. 266(30)

We have used DNA footprinting techniques to analyze the interactions of five DNA replication proteins at a primer-template junction: the bacteriophage T4 DNA polymerase (the gene 43 protein), its three accessory proteins (the gene 44/62 and 45 protei

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https://pubmed.ncbi.nlm.nih.gov/1939067

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Amplification of snap-back DNA synthesis reactions by the uvsX recombinase of bacteriophage T4

Autor: S W, Morrical, M L, Wong, B M, Alberts

Publikováno v: The Journal of biological chemistry. 266(21)

The uvsX protein of bacteriophage T4 is a recA-type recombinase. This protein has previously been shown to help initiate DNA replication on a double-stranded DNA template by catalyzing synapsis between the template and a homologous DNA single strand

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https://pubmed.ncbi.nlm.nih.gov/1649833

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