Günter Blobel - Still passionate after all these years

Trends in Cell Biology

Volumn 11, Issue 8, 2001, Pages 349-350

  Shields, D ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; POLYPEPTIDE; SECRETORY PROTEIN;

CONFERENCE PAPER; ENDOPLASMIC RETICULUM; HUMAN; POLYSOME; PRIORITY JOURNAL; PROTEIN TRANSPORT; RIBOSOME; SECRETORY CELL;

CELL NUCLEUS; ENDOPLASMIC RETICULUM; GERMANY; HISTORY, 20TH CENTURY; NUCLEAR PORE; PORTRAITS; PROTEINS;

EID: 0035423803     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(01)02065-7     Document Type: Conference Paper

References (11)

1. Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of the polypeptides within ribosomes
2. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
3. Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components
4. A protein-conducting channel in the endoplasmic reticulum
5. Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein
6. Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein
7. Cell-free synthesis of fish preproinsulin, and processing by heterologous mammalian microsomal membranes
8. Homology in amino-terminal sequence of precursors to pancreatic secretory proteins
9. Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction. Interphase and mitotic distribution
10. A signal sequence for the insertion of a transmembrane glycoprotein. Similarities to the signals of secretory proteins in primary structure and function