Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Sang-Hyun Rah"'
Publikováno v:
Journal of Visualized Experiments.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::08d18f200e0ce6684825e2710a043a1a
https://doi.org/10.3791/65137
https://doi.org/10.3791/65137
Autor:
Jacob W. J. Kerssemakers, Sang-Hyun Rah, Richard Janissen, Je-Kyung Ryu, Davide Michieletto, Cees Dekker, Andrea Bonato
Publikováno v:
Ryu, J-K, Rah, S-H, Janissen, R, Kerssemakers, J W J, Bonato, A, Michieletto, D & Dekker, C 2022, ' Condensin extrudes DNA loops in steps up to hundreds of base pairs that are generated by ATP binding events ', Nucleic Acids Research, vol. 50, no. 2, pp. 820-832 . https://doi.org/10.1093/nar/gkab1268
Nucleic acids research, 50(2)
Nucleic Acids Research
bioRxiv
Nucl. Acid Res. 50
Nucleic acids research, 50(2)
Nucleic Acids Research
bioRxiv
Nucl. Acid Res. 50
The condensin SMC protein complex organizes chromosomal structure by extruding loops of DNA. Its ATP-dependent motor mechanism remains unclear but likely involves steps associated with large conformational changes within the ∼50 nm protein complex.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b589d734e704ed6b5292c013bcddcc0e
https://www.pure.ed.ac.uk/ws/files/261761699/gkab1268.pdf
https://www.pure.ed.ac.uk/ws/files/261761699/gkab1268.pdf
Publikováno v:
Molecules and cells. 45(1)
Mechanical forces play pivotal roles in regulating cell shape, function, and fate. Key players that govern the mechanobiological interplay are the mechanosensitive proteins found on cell membranes and in cytoskeleton. Their unique nanomechanics can b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::899225a1f6cb37fc530f528edc4fc32d
https://pubmed.ncbi.nlm.nih.gov/35114644
https://pubmed.ncbi.nlm.nih.gov/35114644
Publikováno v:
SSRN Electronic Journal.
The condensin SMC protein complex organizes chromosomal structure by extruding loops of DNA. Its ATP-dependent motor mechanism remains unclear but likely involves steps associated with large conformational changes within the ~50 nm protein complex. H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9ede9e15ab43fafcd370b82311f4d1cd
https://doi.org/10.2139/ssrn.3728949
https://doi.org/10.2139/ssrn.3728949
Autor:
Ho Min Kim, Je-Kyung Ryu, Hi Eun Jung, Beom Seok Park, Heung Kyu Lee, Soo Jin Kim, Sang Hyun Rah, Ji In Kang, Jie-Oh Lee, Tae-Young Yoon, Dong Sun Lee
Publikováno v:
Immunity. 46:38-50
Lipopolysaccharide (LPS), the major component of the outer membrane of Gram-negative bacteria, binds Toll-like receptor 4 (TLR4)-MD2 complex and activates innate immune responses. LPS transfer to TLR4-MD2 is catalyzed by both LPS binding protein (LBP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06e4de8cbc3724a364e41425b4fe6d11
https://doi.org/10.1016/j.immuni.2016.11.007
https://doi.org/10.1016/j.immuni.2016.11.007
Publikováno v:
Science Advances
A multifaceted improvement of molecular tweezers finds that GC-rich DNAs appear stiffer, while methylation softens them.
Submicrometer elasticity of double-stranded DNA (dsDNA) governs nanoscale bending of DNA segments and their interactions wit
Submicrometer elasticity of double-stranded DNA (dsDNA) governs nanoscale bending of DNA segments and their interactions wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1e6eb2b8ad891a952e34f1946e6e4a7
https://doi.org/10.1126/sciadv.aav1697
https://doi.org/10.1126/sciadv.aav1697
Autor:
Tae-Young Yoon, Sang-Hyun Rah, Hyunook Kang, Duyoung Min, James U. Bowie, Hee Jung Choi, Hyun-Kyu Choi, Hak Chan Kim, Min Ju Shon, Hawoong Jeong
Publikováno v:
Science
A pathway for helical membrane proteins Membrane proteins are inserted into cell membranes while they are being translated and may fold concurrently into their secondary and tertiary structures. Choi et al. describe a single-molecule force microscopy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf17462e02720b4236cc323e782d0cd0
https://pubmed.ncbi.nlm.nih.gov/31780561
https://pubmed.ncbi.nlm.nih.gov/31780561
Publikováno v:
Physics and High Technology. 25:24-30
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::57bac837596611e273ae2ac9f69ea399
https://doi.org/10.3938/phit.25.053
https://doi.org/10.3938/phit.25.053
Publikováno v:
2015 11th Conference on Lasers and Electro-Optics Pacific Rim (CLEO-PR).
N-ethylmaleimide-sensitive factor (NSF) and alpha soluble NSF attachment protein (α-SNAP) disassemble the SNAP receptor (SNARE) complex for recycling of the SNARE proteins. Using single-molecule fluorescence and force spectroscopy, we found that NSF
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c1ba2b86ec433289605c8706263d4ad3
https://doi.org/10.1109/cleopr.2015.7376355
https://doi.org/10.1109/cleopr.2015.7376355
Autor:
Yongsoo Park, Tae-Young Yoon, Ho Min Kim, Reinhard Jahn, Soo Jin Kim, Duyoung Min, Je-Kyung Ryu, Changbong Hyeon, Sang Hyun Rah, Haesoo Kim
Publikováno v:
Science
An explosive way to fuse membranes The molecular machine that promotes membrane fusion during intracellular transport involves a number of so-called SNARE proteins. Ryu et al. describe the molecular mechanism by which two proteins —NSF and α-SNAP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cd5db8ffd63942ecae34404b0300903
https://hdl.handle.net/11858/00-001M-0000-0026-BCA9-611858/00-001M-0000-0026-BCAA-411858/00-001M-0000-0026-BCA7-A
https://hdl.handle.net/11858/00-001M-0000-0026-BCA9-611858/00-001M-0000-0026-BCAA-411858/00-001M-0000-0026-BCA7-A