FileTitleManuscript Id
Chapter Introductionlodish8e_ch13_1.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_1_dlap.xml56e9963a757a2e9e52000000
13.1 Targeting Proteins To and Across the ER Membrane lodish8e_ch13_2.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_2_dlap.xml56e9963a757a2e9e52000000
Pulse-Chase Experiments with Purified ER Membranes Demonstrated That Secreted Proteins Cross the ER Membrane lodish8e_ch13_3.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_3_dlap.xml56e9963a757a2e9e52000000
A Hydrophobic N-Terminal Signal Sequence Targets Nascent Secretory Proteins to the ER lodish8e_ch13_4.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_4_dlap.xml56e9963a757a2e9e52000000
Cotranslational Translocation Is Initiated by Two GTP-Hydrolyzing Proteins lodish8e_ch13_5.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_5_dlap.xml56e9963a757a2e9e52000000
Passage of Growing Polypeptides Through the Translocon Is Driven by Translation lodish8e_ch13_6.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_6_dlap.xml56e9963a757a2e9e52000000
ATP Hydrolysis Powers Post-translational Translocation of Some Secretory Proteins in Yeast lodish8e_ch13_7.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_7_dlap.xml56e9963a757a2e9e52000000
Key Concepts of Section 13.1lodish8e_ch13_8.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_8_dlap.xml56e9963a757a2e9e52000000
13.2 Insertion of Membrane Proteins into the ER lodish8e_ch13_9.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_9_dlap.xml56e9963a757a2e9e52000000
Several Topological Classes of Integral Membrane Proteins Are Synthesized on the ER lodish8e_ch13_10.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_10_dlap.xml56e9963a757a2e9e52000000
Internal Stop-Transfer Anchor and Signal-Anchor Sequences Determine Topology of Single-Pass Proteins lodish8e_ch13_11.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_11_dlap.xml56e9963a757a2e9e52000000
Multipass Proteins Have Multiple Internal Topogenic Sequences lodish8e_ch13_12.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_12_dlap.xml56e9963a757a2e9e52000000
A Phospholipid Anchor Tethers Some Cell-Surface Proteins to the Membrane lodish8e_ch13_13.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_13_dlap.xml56e9963a757a2e9e52000000
The Topology of a Membrane Protein Can Often Be Deduced from Its Sequence lodish8e_ch13_14.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_14_dlap.xml56e9963a757a2e9e52000000
Key Concepts of Section 13.2lodish8e_ch13_15.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_15_dlap.xml56e9963a757a2e9e52000000
13.3 Protein Modifications, Folding, and Quality Control in the ER lodish8e_ch13_16.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_16_dlap.xml56e9963a757a2e9e52000000
A Preformed N-Linked Oligosaccharide Is Added to Many Proteins in the Rough ER lodish8e_ch13_17.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_17_dlap.xml56e9963a757a2e9e52000000
Oligosaccharide Side Chains May Promote Folding and Stability of Glycoproteins lodish8e_ch13_18.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_18_dlap.xml56e9963a757a2e9e52000000
Disulfide Bonds Are Formed and Rearranged by Proteins in the ER Lumen lodish8e_ch13_19.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_19_dlap.xml56e9963a757a2e9e52000000
Chaperones and Other ER Proteins Facilitate Folding and Assembly of Proteins lodish8e_ch13_20.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_20_dlap.xml56e9963a757a2e9e52000000
Improperly Folded Proteins in the ER Induce Expression of Protein-Folding Catalysts lodish8e_ch13_21.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_21_dlap.xml56e9963a757a2e9e52000000
Unassembled or Misfolded Proteins in the ER Are Often Transported to the Cytosol for Degradation lodish8e_ch13_22.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_22_dlap.xml56e9963a757a2e9e52000000
Key Concepts of Section 13.3lodish8e_ch13_23.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_23_dlap.xml56e9963a757a2e9e52000000
13.4 Targeting of Proteins to Mitochondria and Chloroplasts lodish8e_ch13_24.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_24_dlap.xml56e9963a757a2e9e52000000
Amphipathic N-Terminal Targeting Sequences Direct Proteins to the Mitochondrial Matrix lodish8e_ch13_25.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_25_dlap.xml56e9963a757a2e9e52000000
Mitochondrial Protein Import Requires Outer-Membrane Receptors and Translocons in Both Membranes lodish8e_ch13_26.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_26_dlap.xml56e9963a757a2e9e52000000
Studies with Chimeric Proteins Demonstrate Important Features of Mitochondrial Protein Import lodish8e_ch13_27.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_27_dlap.xml56e9963a757a2e9e52000000
Three Energy Inputs Are Needed to Import Proteins into Mitochondria lodish8e_ch13_28.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_28_dlap.xml56e9963a757a2e9e52000000
Multiple Signals and Pathways Target Proteins to Submitochondrial Compartments lodish8e_ch13_29.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_29_dlap.xml56e9963a757a2e9e52000000
Import of Chloroplast Stromal Proteins Is Similar to Import of Mitochondrial Matrix Proteins lodish8e_ch13_30.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_30_dlap.xml56e9963a757a2e9e52000000
Proteins Are Targeted to Thylakoids by Mechanisms Related to Bacterial Protein Translocation lodish8e_ch13_31.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_31_dlap.xml56e9963a757a2e9e52000000
Key Concepts of Section 13.4lodish8e_ch13_32.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_32_dlap.xml56e9963a757a2e9e52000000
13.5 Targeting of Peroxisomal Proteins lodish8e_ch13_33.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_33_dlap.xml56e9963a757a2e9e52000000
A Cytosolic Receptor Targets Proteins with an SKL Sequence at the C-Terminus to the Peroxisomal Matrix lodish8e_ch13_34.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_34_dlap.xml56e9963a757a2e9e52000000
Peroxisomal Membrane and Matrix Proteins Are Incorporated by Different Pathways lodish8e_ch13_35.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_35_dlap.xml56e9963a757a2e9e52000000
Key Concepts of Section 13.5lodish8e_ch13_36.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_36_dlap.xml56e9963a757a2e9e52000000
13.6 Transport Into and Out of the Nucleus lodish8e_ch13_37.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_37_dlap.xml56e9963a757a2e9e52000000
Large and Small Molecules Enter and Leave the Nucleus via Nuclear Pore Complexes lodish8e_ch13_38.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_38_dlap.xml56e9963a757a2e9e52000000
Nuclear Transport Receptors Escort Proteins Containing Nuclear-Localization Signals into the Nucleus lodish8e_ch13_39.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_39_dlap.xml56e9963a757a2e9e52000000
A Second Type of Nuclear Transport Receptor Escorts Proteins Containing Nuclear-Export Signals Out of the Nucleus lodish8e_ch13_40.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_40_dlap.xml56e9963a757a2e9e52000000
Most mRNAs Are Exported from the Nucleus by a Ran-Independent Mechanism lodish8e_ch13_41.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_41_dlap.xml56e9963a757a2e9e52000000
Key Concepts of Section 13.6lodish8e_ch13_42.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_42_dlap.xml56e9963a757a2e9e52000000
Key Terms lodish8e_ch13_43.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_43_dlap.xml56e9963a757a2e9e52000000
Review the Concepts lodish8e_ch13_44.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_44_dlap.xml56e9963a757a2e9e52000000
References lodish8e_ch13_45.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_45_dlap.xml56e9963a757a2e9e52000000
Perspectives for the Future lodish8e_ch13_46.html56e9963a757a2e9e52000000
DLAP questionslodish8e_ch13_46_dlap.xml56e9963a757a2e9e52000000