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Dynamic polymerization of TDP-43 in health and disease
Published on Jul 21, 2017938 Views
TDP-43 is a primarily nuclear RNA-binding protein (RBP), whose abnormal phosphorylation and cytoplasmic aggregation characterizes affected neurons in patients with amyotrophic lateral sclerosis (A
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Dynamic polymerization of TDP-43 in health and disease00:00
TDP-43 is mislocalized and forms inclusions in ALS/FTD 00:18
Structural determinants of TDP-43 function and pathology - 100:50
Structural determinants of TDP-43 function and pathology - 201:03
Structural determinants of TDP-43 function and pathology - 301:23
What is the physiological state of functional TDP-43 and how does it form? - 102:28
What is the physiological state of functional TDP-43 and how does it form? - 203:23
What is the physiological state of functional TDP-43 and how does it form? - 304:00
Biophysical characterization of TDP-43 N-terminal domain (NTD) - 104:48
Biophysical characterization of TDP-43 N-terminal domain (NTD) - 205:28
2.1-Å resolution crystal structure of TDP-43 NTD 05:45
Head-to-tail arrangement of TDP-43 NTD monomers06:23
Electrostatic interactions drive the head-to-tail polymerization of TDP-43 NTD 06:53
Validation of inter-molecular interface in solution by nuclear magnetic resonance (NMR) spectroscopy 07:33
Dynamic oligomerization of TDP-43 NTD monitored by NMR - 1 07:56
Dynamic oligomerization of TDP-43 NTD monitored by NMR - 208:16
Dynamic oligomerization of TDP-43 NTD monitored by NMR - 308:19
Dynamic oligomerization of TDP-43 NTD monitored by NMR - 408:27
Dynamic oligomerization of TDP-43 NTD monitored by NMR - 508:30
Dynamic oligomerization of TDP-43 NTD monitored by NMR - 608:55
Mutagenesis of residues at oligomerization interface based on crystal structure09:40
Point mutations abrogate TDP-43 NTD oligomerization in vitro - 110:06
Point mutations abrogate TDP-43 NTD oligomerization in vitro - 210:15
Point mutations abrogate TDP-43 NTD oligomerization in vitro - 310:17
Point mutations abrogate TDP-43 NTD oligomerization in vitro - 410:19
Point mutations abrogate TDP-43 NTD oligomerization in vitro - 510:41
Point mutations in the N-terminal domain do NOT affect TDP-43 subcellular localization11:02
Functional role of TDP-43 oligomerization in RNA metabolism - 112:28
Functional role of TDP-43 oligomerization in RNA metabolism - 313:06
Functional role of TDP-43 oligomerization in RNA metabolism - 413:50
Visualization of TDP-43 physiological oligomers in cells14:16
Tripartite GFP complementation (Split GFP) - 114:40
Tripartite GFP complementation (Split GFP) - 214:54
Tripartite GFP complementation (Split GFP) - 314:57
Tripartite GFP complementation (Split GFP) - 414:59
Tripartite GFP complementation (Split GFP) - 515:03
Tripartite GFP complementation (Split GFP) - 715:04
Tripartite GFP complementation (Split GFP) - 815:06
Tripartite GFP complementation - 115:12
Tripartite GFP complementation - 215:35
Does TDP-43 oligomerization antagonize its pathologic aggregation? 16:30
Increased phosphorylation in TDP-43 oligomerization mutants16:49
Functional and dynamic TDP-43 oligomerization antagonizes pathologic aggregation - 117:43
Functional and dynamic TDP-43 oligomerization antagonizes pathologic aggregation - 217:54
Functional and dynamic TDP-43 oligomerization antagonizes pathologic aggregation - 318:01
Functional and dynamic TDP-43 oligomerization antagonizes pathologic aggregation - 418:11
Functional and dynamic TDP-43 oligomerization antagonizes pathologic aggregation - 518:23
Functional and dynamic TDP-43 oligomerization antagonizes pathologic aggregation - 618:35
Acknowledgments19:01