Zobrazeno 1 - 10
of 142
pro vyhledávání: '"Goldberg, Martin W."'
Autor:
Al-Ansari, Mohammad, Fitzsimons, Taylor, Wei, Wenbin, Goldberg, Martin W., Kunieda, Takekazu, Quinlan, Roy A.
Publikováno v:
Cell Stress & Chaperones, 2024 Jan 01. 29(1), 51-65.
Externí odkaz:
https://www.jstor.org/stable/48771900
Autor:
Dixon, Charles R., Malik, Poonam, de las Heras, Jose I., Saiz-Ros, Natalia, de Lima Alves, Flavia, Tingey, Mark, Gaunt, Eleanor, Richardson, A. Christine, Kelly, David A., Goldberg, Martin W., Towers, Greg J., Yang, Weidong, Rappsilber, Juri, Digard, Paul, Schirmer, Eric C.
Publikováno v:
In iScience 24 September 2021 24(9)
Autor:
Young, Natalie, Gui, Zizhao, Mustafa, Suleiman, Papa, Kleopatra, Jessop, Emily, Ruddell, Elizabeth, Bevington, Laura, Quinlan, Roy A., Benham, Adam M., Goldberg, Martin W., Obara, Boguslaw, Karakesisoglou, Iakowos
Publikováno v:
Cells (2073-4409); Jun2024, Vol. 13 Issue 11, p906, 27p
Autor:
Walther, Tobias C., Pickersgill, Helen S., Cordes, Volker C., Goldberg, Martin W., Allen, Terry D., Mattaj, Iain W., Fornerod, Maarten
Publikováno v:
The Journal of Cell Biology, 2002 Jul 01. 158(1), 63-77.
Externí odkaz:
https://www.jstor.org/stable/1621123
Autor:
Dubińska-Magiera, Magda, Chmielewska, Magdalena, Kozioł, Katarzyna, Machowska, Magdalena, Hutchison, Christopher J., Goldberg, Martin W., Rzepecki, Ryszard
Publikováno v:
Protoplasma
Xenopus LAP2β protein is the single isoform expressed in XTC cells. The protein localizes on heterochromatin clusters both at the nuclear envelope and inside a cell nucleus. The majority of XLAP2β fraction neither colocalizes with TPX2 protein duri
Autor:
Grafe, Marianne, Batsios, Petros, Meyer, Irene, Lisin, Daria, Baumann, Otto, Goldberg, Martin W., Gräf, Ralph
Publikováno v:
Cells
Cells, Vol 8, Iss 2, p 162 (2019)
Volume 8
Issue 2
Cells, 2019, Vol.8(2), pp.162 [Peer Reviewed Journal]
Cells, Vol 8, Iss 2, p 162 (2019)
Volume 8
Issue 2
Cells, 2019, Vol.8(2), pp.162 [Peer Reviewed Journal]
Nuclear lamins are nucleus-specific intermediate filaments (IF) found at the inner nuclear membrane (INM) of the nuclear envelope (NE). Together with nuclear envelope transmembrane proteins, they form the nuclear lamina and are crucial for gene regul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77a76ae39666ca45826c655adac4760d
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/42596
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/42596
Autor:
Saiz-Ros, Natalia, Czapiewski, Rafal, Epifano, Ilaria, Stevenson, Andrew, Swanson, Selene K., Dixon, Charles R., Zamora, Dario B., McElwee, Marion, Vijayakrishnan, Swetha, Richardson, Christine A., Dong, Li, Kelly, David A., Pytowski, Lior, Goldberg, Martin W., Florens, Laurence, Graham, Sheila V., Schirmer, Eric C.
Publikováno v:
Cells, 2019, Vol.8(2), pp.120 [Peer Reviewed Journal]
Cells, Vol 8, Iss 2, p 120 (2019)
Saiz-Ros, N, Czapiewski, R, Epifano, I, Stevenson, A, Swanson, S K, Dixon, C R, Zamora, D B, McElwee, M, Vijayakrishnan, S, Richardson, C A, Dong, L, Kelly, D A, Pytowski, L, Goldberg, M W, Florens, L, Graham, S V & Schirmer, E C 2019, ' Host Vesicle Fusion Protein VAPB Contributes to the Nuclear Egress Stage of Herpes Simplex Virus Type-1 (HSV-1) Replication ', Cells, vol. 8, no. 2 . https://doi.org/10.3390/cells8020120
Cells
Volume 8
Issue 2
Cells, Vol 8, Iss 2, p 120 (2019)
Saiz-Ros, N, Czapiewski, R, Epifano, I, Stevenson, A, Swanson, S K, Dixon, C R, Zamora, D B, McElwee, M, Vijayakrishnan, S, Richardson, C A, Dong, L, Kelly, D A, Pytowski, L, Goldberg, M W, Florens, L, Graham, S V & Schirmer, E C 2019, ' Host Vesicle Fusion Protein VAPB Contributes to the Nuclear Egress Stage of Herpes Simplex Virus Type-1 (HSV-1) Replication ', Cells, vol. 8, no. 2 . https://doi.org/10.3390/cells8020120
Cells
Volume 8
Issue 2
The primary envelopment/de-envelopment of Herpes viruses during nuclear exit is poorly understood. In Herpes simplex virus type-1 (HSV-1), proteins pUL31 and pUL34 are critical, while pUS3 and some others contribute
however, efficient membrane f
however, efficient membrane f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::40ff430cdf5778a64867bf8dec2aaa46
https://doi.org/10.3390/cells8020120
https://doi.org/10.3390/cells8020120
Autor:
Reipert, Siegfried, Goldammer, Helmuth, Richardson, Christine, Goldberg, Martin W., Hawkins, Timothy J., Hollergschwandtner, Elena, Kaufmann, Walter A., Antreich, Sebastian, York-Dieter Stierhof
Supplemental material, DS_10.1369_0022155418786698 for Agitation Modules: Flexible Means to Accelerate Automated Freeze Substitution by Siegfried Reipert, Helmuth Goldammer, Christine Richardson, Martin W. Goldberg, Timothy J. Hawkins, Elena Hollergs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba65ff9a0ff1a74c76de95300398a5e2
Autor:
de Castro, Inês J., Budzak, James, Di Giacinto, Maria L., Ligammari, Lorena, Gokhan, Ezgi, Spanos, Christos, Moralli, Daniela, Richardson, Christine, de las Heras, Jose I., Salatino, Silvia, Schirmer, Eric C., Ullman, Katharine S., Bickmore, Wendy A., Green, Catherine, Rappsilber, Juri, Lamble, Sarah, Goldberg, Martin W., Vinciotti, Veronica, Vagnarelli, Paola
Publikováno v:
de Castro, I J, Budzak, J, Giacinto, M L, Ligammari, L, Gokhan, E, Spanos, C, Moralli, D, Richardson, C, de las Heras, J, Salatino, S, Schirmer, E, Ullman, K, Bickmore, W, Green, C, Rappsilber, J, Lamble, S, Goldberg, M W, Vinciotti, V & Vagnarelli, P 2017, ' Repo-Man/PP1 regulates heterochromatin formation in interphase ', Nature Communications, vol. 8, 14048 . https://doi.org/10.1038/ncomms14048
Nature communications, 2017, Vol.8, pp.14048 [Peer Reviewed Journal]
Nature Communications, Vol 8, Iss 1, Pp 1-16 (2017)
Nature Communications
Nature communications, 2017, Vol.8, pp.14048 [Peer Reviewed Journal]
Nature Communications, Vol 8, Iss 1, Pp 1-16 (2017)
Nature Communications
Repo-Man is a protein phosphatase 1 (PP1) targeting subunit that regulates mitotic progression and chromatin remodelling. After mitosis, Repo-Man/PP1 remains associated with chromatin but its function in interphase is not known. Here we show that Rep
Autor:
Tapodi, Antal, Clemens, Daniel M., Uwineza, Alice, Jarrin, Miguel, Goldberg, Martin W., Thinon, Emmanuelle, Heal, William P., Tate, Edward W., Nemeth-Cahalan, Karinne, Vorontsova, Irene, Hall, James E., Quinlan, Roy A.
Publikováno v:
Experimental eye research
BFSP1 (beaded filament structural protein 1, filensin) is a cytoskeletal protein expressed in the eye lens. It binds AQP0 in vitro and its C-terminal sequences have been suggested to regulate the water channel activity of AQP0. A myristoylated fragme