Rockefeller University Press

Last updated
Rockefeller University Press
Parent company Rockefeller University
Founded1910
Founder Simon Flexner
Country of originUnited States
Headquarters locationNew York City
Publication typesAcademic journals
Nonfiction topicsScience
Official website www.rupress.org

The Rockefeller University Press (RUP) is a department of Rockefeller University.

Contents

Journals

Rockefeller University Press publishes three scientific journals: Journal of Experimental Medicine , founded in 1896, Journal of General Physiology , founded in 1918, and Journal of Cell Biology , founded in 1955 under the title The Journal of Biophysical and Biochemical Cytology. All editorial decisions on manuscripts submitted to the three journals are made by active scientists in conjunction with in-house scientific editors, and all peer-review operations and pre-press production functions are carried out at the Rockefeller University Press offices. In 2018, Rockefeller University Press partnered with EMBO Press and Cold Spring Harbor Laboratory Press to launch the "Life Science Alliance" journal.

Focus

Rockefeller University Press places a strong emphasis on preserving the integrity of primary research data, and it is a pioneer in the application of new technologies to achieve that goal. [1] [2] [3]

Open access policy

Rockefeller University Press provides public access to the articles it publishes. [4] [5] All content of Journal of Experimental Medicine, Journal of Cell Biology, and Journal of General Physiology (back to volume 1, issue 1) is hosted on Silverchair and PubMed Central, where it is available to the public for free 6 months after publication under a Creative Commons license. Some content is published Open Access immediately upon publication under a CC-BY license.

See also

Related Research Articles

<span class="mw-page-title-main">Christian de Duve</span> Belgian biochemist and cytologist (1917–2013)

Christian René Marie Joseph, Viscount de Duve was a Nobel Prize-winning Belgian cytologist and biochemist. He made serendipitous discoveries of two cell organelles, peroxisomes and lysosomes, for which he shared the Nobel Prize in Physiology or Medicine in 1974 with Albert Claude and George E. Palade. In addition to peroxisome and lysosome, he invented scientific names such as autophagy, endocytosis, and exocytosis on a single occasion.

<span class="mw-page-title-main">Albert Claude</span> Belgian-American cell biologist (1899–1983)

Albert Claude was a Belgian-American cell biologist and medical doctor who shared the Nobel Prize in Physiology or Medicine in 1974 with Christian de Duve and George Emil Palade. His elementary education started in a comprehensive primary school at Longlier, his birthplace. He served in the British Intelligence Service during the First World War, and got imprisoned in concentration camps twice. In recognition of his service, he was granted enrolment at the University of Liège in Belgium to study medicine without any formal education required for the course. He earned his Doctor of Medicine degree in 1928. Devoted to medical research, he initially joined German institutes in Berlin. In 1929 he found an opportunity to join the Rockefeller Institute in New York. At Rockefeller University he made his most groundbreaking achievements in cell biology. In 1930 he developed the technique of cell fractionation, by which he discovered the agent of the Rous sarcoma, as well as components of cell organelles such as the mitochondrion, chloroplast, endoplasmic reticulum, Golgi apparatus, ribosome, and lysosome. He was the first to employ the electron microscope in the field of biology. In 1945 he published the first detailed structure of cell. His collective works established the complex functional and structural properties of cells.

<span class="mw-page-title-main">Utrophin</span> Mammalian protein found in Homo sapiens

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<span class="mw-page-title-main">Integrin alpha-1</span> Mammalian protein found in Homo sapiens

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<span class="mw-page-title-main">Integrin beta 5</span> Protein-coding gene in the species Homo sapiens

Integrin beta-5 is a protein that in humans is encoded by the ITGB5 gene.

<span class="mw-page-title-main">VAV2</span> Protein-coding gene in the species Homo sapiens

Guanine nucleotide exchange factor VAV2 is a protein that in humans is encoded by the VAV2 gene.

<span class="mw-page-title-main">DYNC1I2</span> Protein-coding gene in the species Homo sapiens

Cytoplasmic dynein 1 intermediate chain 2 is a protein that in humans is encoded by the DYNC1I2 gene.

<span class="mw-page-title-main">CKAP4</span> Protein-coding gene in humans

Cytoskeleton-associated protein 4 is a protein that in humans is encoded by the CKAP4 gene.

<span class="mw-page-title-main">ZW10</span>

Centromere/kinetochore protein zw10 homolog is a protein that in humans is encoded by the ZW10 gene. This gene encodes a protein that is one of many involved in mechanisms to ensure proper chromosome segregation during cell division. The encoded protein binds to centromeres during the prophase, metaphase, and early anaphase cell division stages and to kinetochore microtubules during metaphase.

<span class="mw-page-title-main">PEX10</span> Protein-coding gene in the species Homo sapiens

Peroxisome biogenesis factor 10 is a protein that in humans is encoded by the PEX10 gene. Alternative splicing results in two transcript variants encoding different isoforms.

<span class="mw-page-title-main">Uroplakin-1a</span> Mammalian protein found in Homo sapiens

Uroplakin-1a (UP1a) is a protein that in humans is encoded by the UPK1A gene.

<span class="mw-page-title-main">HES6</span> Protein-coding gene in the species Homo sapiens

Transcription cofactor HES-6 is a protein that in humans is encoded by the HES6 gene.

<span class="mw-page-title-main">PPM1G</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">Ewald Weibel</span> Swiss anatomist and physiologist (1929–2019)

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<i>Journal of Cell Biology</i> Academic journal

The Journal of Cell Biology is a peer-reviewed scientific journal published by Rockefeller University Press.

<span class="mw-page-title-main">CEP164</span> Protein-coding gene in the species Homo sapiens

Centrosomal protein of 164 kDa, also known as CEP164, is a protein that in humans is encoded by the CEP164 gene. Its function appears two be twofold: CEP164 is required for primary cilium formation. Furthermore, it is an important component in the response to DNA damage by UV light.

David Schlaepfer is a California-born scientist known for his studies on cell migration and cancer metastasis. His early research focused on signaling by protein kinases, with a subsequent focus on the proteins that regulate the turnover of cell contacts with the extracellular matrix. In particular, Schlaepfer is well known for his studies on focal adhesion kinase (FAK).

<span class="mw-page-title-main">MIS18BP1</span> Protein-coding gene in the species Homo sapiens

MIS18 binding protein 1 is a protein that in humans is encoded by the MIS18BP1 gene. The gene is also known as LKNL2, M18BP1, C14orf106, and HSA242977.

<span class="mw-page-title-main">SFI1</span> Protein-coding gene in the species Homo sapiens

Sfi1 homolog, spindle assembly associated (yeast) is a protein that in humans is encoded by the SFI1 gene. It localizes to the centriole, and its S. pombe ortholog has been shown to be involved in spindle pole body duplication. SFI1 forms a complex with centrin 2.

References

  1. Wade, Nicholas (2006-01-24). "It May Look Authentic; Here's How To Tell It Isn't". The New York Times . Retrieved 2008-01-25.
  2. Rossner M, Yamada KM (2004). "What's in a picture? The temptation of image manipulation". J. Cell Biol. 166 (1): 11–15. doi:10.1083/jcb.200406019. PMC   2172141 . PMID   15240566. Archived from the original on November 20, 2007.
  3. Rossner M, O'Donnell R (2004). "The JCB will let your data shine in RGB". J. Cell Biol. 164 (1): 11–13. doi:10.1083/jcb.200312069. PMC   2171972 . PMID   18172955. Archived from the original on December 2, 2007.
  4. Hill E (2007). "JCB content automatically deposited in PubMed Central (PMC)". J. Cell Biol. 179 (1): 9. doi:10.1083/jcb.200708190. PMC   2064724 .
  5. Rossner M (2007). "Bending the truth with a PRISM". J. Cell Biol. 179 (2): 177–178. doi:10.1083/jcb.200709001. PMC   2064752 . PMID   17938251.