Gabriel C. Lander
www.lander-lab.com
0000-0003-4921-1135
The Scripps Research Institute
10 papers found
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The N1 domain of the peroxisomal AAA-ATPase Pex6 is required for Pex15 binding and proper assembly with Pex1
Structural basis for a degenerate tRNA identity code and the evolution of bimodal specificity in human mitochondrial tRNA recognition
Structure of the hepatitis C virus E1E2 glycoprotein complex
Structural basis for shape-selective recognition and aminoacylation of a D-armless human mitochondrial tRNA
Dynamics at the serine loop underlie differential affinity of cryptochromes for CLOCK:BMAL1 to control circadian timing
Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation
Author Correction: Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility
The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading
Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility
Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex
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