Results 141 to 150 of about 1,263,948 (304)

Links National Assembly, 30

open access: yes, 1996
This book contains reports from the national officers and program directors of The Links, Inc., about the activities of the national level of the organization from 1994-1996. It was presented to the 30th National Assembly.
Links, Inc. National Assembly.
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Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

open access: yesFEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai   +4 more
wiley   +1 more source

Links Regional Papers

open access: yes, 1977
Announcement of two scholarship awards sponsored by The Links, Inc. won by high school students in the western United States. Kyra Papillon won sponsorship from the Oakland Bay Area Links to attend a forum for non-governmental organizations in Nairobi ...
Links, Inc. Western Area.
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Rab14 regulates the transport of human papillomavirus to the trans‐Golgi network for infectious cell entry

open access: yesFEBS Letters, EarlyView.
This study reveals that the small GTPase Rab14 is necessary for human papillomavirus (HPV) infection and plays an essential role in the transport of virions to the trans‐Golgi network (TGN). HPV in the early endosome (EE), which harbors GTP‐bound Rab14, is transported to the TGN through the switch of Rab14 from its GTP‐bound to GDP‐bound form.
Yoshiyuki Ishii, Iwao Kukimoto
wiley   +1 more source

Links National Assembly, 25

open access: yes, 1986
This book contains reports from the national officers and program directors of The Links, Inc., about the activities of the national level of the organization from 1984-1986. It was presented to the 25th National Assembly.
Links, Inc. National Assembly.
core  

Degradation mechanism of the von Willebrand factor A2 domain by nattokinase

open access: yesFEBS Letters, EarlyView.
Nattokinase, a natto‐derived protease, exhibits potent antithrombotic effects. This study demonstrates that nattokinase directly cleaves the von Willebrand factor (vWF) A2 domain in vitro. Unlike the native regulator ADAMTS13, nattokinase degrades folded vWF independently of shear stress.
Ryuichi Hyakumoto   +3 more
wiley   +1 more source

Modulation of Homer1 EVH1 domain internal dynamics by putative autism‐associated mutations

open access: yesFEBS Letters, EarlyView.
The putative autism‐associated M65I and S97L variants of the EVH1 domain of the postsynaptic scaffold protein Homer1 do not exhibit substantial changes in their overall structure or partner binding. Both of them, but especially the M65I variant, show altered internal dynamics relative to the wild‐type domain on the μs‐ms timescale, indicated by the ...
Fanni Farkas   +6 more
wiley   +1 more source

Photocross-linking activity-based probes to capture the dynamics of ubiquitin RING E3 ligase interactions. [PDF]

open access: yesBiochem J
Chandler SF   +6 more
europepmc   +1 more source

The ubiquitin‐proteasome system and autophagy as guardians of the cellular proteome

open access: yesFEBS Letters, EarlyView.
This Perspective covers the three principles governing the crosstalk between the ubiquitin‐proteasome system and autophagy in cellular proteostasis: (1) a shared ubiquitin code routing substrates via shuttle factors or autophagy receptors; (2) spatial compartmentalization into phase‐separated degradation hubs and organelle‐specific modules (exemplified
Ivan Dikic
wiley   +1 more source

Links Western Area Conference, 15

open access: yes, 1968
Conference minutes include an account of the proceedings, reports, financial statements, committee membership lists, and other information relevant to the meeting of the Western Area division of The Links, Inc.
Links, Inc. Western Area.
core  

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