Zobrazeno 1 - 10
of 323
pro vyhledávání: '"Reinstein J"'
Autor:
Reinstein, J., Pyenson, B.
Publikováno v:
In Journal of Thoracic Oncology October 2024 19(10) Supplement:S474-S474
Publikováno v:
In The Journal of Minimally Invasive Gynecology November 2023 30(11) Supplement:S131-S132
Autor:
GRüNBEIN, M.L., STRICKER, M., KOVACS, G.N., Kloos, M., DOAK, R.B., SHOEMAN, R.L, REINSTEIN, J., Lecler, Sylvain, Haacke, Stefan, Schlichting, I.
Publikováno v:
Nature Methods
Nature Methods, Nature Publishing Group, 2020, 17, ⟨10.1038/s41592-020-0847-3⟩
Nature Methods, 2020, 17, ⟨10.1038/s41592-020-0847-3⟩
Nature Methods, Nature Publishing Group, 2020, 17, ⟨10.1038/s41592-020-0847-3⟩
Nature Methods, 2020, 17, ⟨10.1038/s41592-020-0847-3⟩
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::d152d3f753743d9790be33427ef189da
https://hal.archives-ouvertes.fr/hal-03511503
https://hal.archives-ouvertes.fr/hal-03511503
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 6, p e99504 (2014)
PLoS One
PLoS ONE, Vol 9, Iss 6, p e99504 (2014)
PLoS One
Human immunodeficiency virus particles undergo a step of proteolytic maturation, in which the main structural polyprotein Gag is cleaved into its mature subunits matrix (MA), capsid (CA), nucleocapsid (NC) and p6. Gag proteolytic processing is accomp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::ebcc3985b30d47cb8c00b080520829a3
http://europepmc.org/articles/PMC4051761
http://europepmc.org/articles/PMC4051761
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 10, p e78384 (2013)
PLoS One
PLoS ONE, Vol 8, Iss 10, p e78384 (2013)
PLoS One
The globular 25 kDa protein cytosine monophosphate kinase (CMPK, EC ID: 2.7.4.14) from E. coli belongs to the family of nucleoside monophosphate (NMP) kinases (NMPK). Many proteins of this family share medium to high sequence and high structure simil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::d7d72e8200b46a5d8141411dec0b307c
https://pubmed.ncbi.nlm.nih.gov/24205218
https://pubmed.ncbi.nlm.nih.gov/24205218
Publikováno v:
PLoS ONE, Vol 8, Iss 6, p e67362 (2013)
PLoS ONE
PLoS One
PLoS ONE
PLoS One
Type-6-secretion systems of Gram-negative bacteria are widely distributed needle-like multi-protein complexes that are involved in microbial defense mechanisms. During bacterial competition these injection needles dispense effector proteins into the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::e3a3b459f242e14ad3dcb970e2ea40fe
http://europepmc.org/articles/PMC3695027?pdf=render
http://europepmc.org/articles/PMC3695027?pdf=render
Autor:
Schweizer, R., Reinstein, J.
Publikováno v:
Biospektrum
The molecular chaperone DnaK was optimized by directed evolution for better refolding activity toward two substrates and the identified DnaK variants were analyzed for characteristic changes in their mechanism. Remarkably, none of the variants was mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______1874::e0482eb96759c170d181a25ea67d84e2
http://link.springer.com/content/pdf/10.1007/s12268-012-0194-8
http://link.springer.com/content/pdf/10.1007/s12268-012-0194-8
Publikováno v:
The Journal of Biological Chemistry
ClpB cooperates with the DnaK chaperone system in the reactivation of protein from aggregates and is a member of the ATPases associated with a variety of cellular activities (AAA+) protein family. The underlying disaggregation reaction is dependent o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______1874::bfbbc68c963e44dd8dd8dde831dc1259
http://www.jbc.org/content/280/45/37965
http://www.jbc.org/content/280/45/37965
Publikováno v:
The Journal of Biological Chemistry
The molecular chaperone Hsp90 is known to be involved in the activation of key regulatory proteins such as kinases, steroid hormone receptors, and transcription factors in an ATP-dependent manner. During the chaperone cycle, Hsp90 has been found asso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::5242788ec0a06e98bbe6ef44d2150828
https://hdl.handle.net/11858/00-001M-0000-002C-205A-B11858/00-001M-0000-002C-2058-F
https://hdl.handle.net/11858/00-001M-0000-002C-205A-B11858/00-001M-0000-002C-2058-F
Autor:
Brehmer, D., Rüdiger, S., Gässler, C., Klostermeier, D., Packschies, L., Reinstein, J., Mayer, M., Bukau, B.
Publikováno v:
Nature Structural and Molecular Biology
The Hsp70 chaperone activity in protein folding is regulated by ATP-controlled cycles of substrate binding and release. Nucleotide exchange plays a key role in these cycles by triggering substrate release. Structural searches of Hsp70 homologs reveal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______1874::fccf70699aa7250d5a9f6ff08623c1a6
https://hdl.handle.net/11858/00-001M-0000-002C-2128-411858/00-001M-0000-002C-212A-F
https://hdl.handle.net/11858/00-001M-0000-002C-2128-411858/00-001M-0000-002C-212A-F