Richard Zimmermann

A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes.

Tail-anchored and signal-anchored proteins utilize overlapping pathways during membrane insertion.

Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity.

Polypeptide-binding proteins mediate completion of co-translational protein translocation into the mammalian endoplasmic reticulum.

Transport of the intracisternal A-type particle Gag polyprotein to the endoplasmic reticulum is mediated by the signal recognition particle.

The Sec61p complex is a dynamic precursor activated channel.

Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p.

Protein transport into canine pancreatic microsomes: a quantitative approach.

Specific detection and semi-quantitative analysis of TRPC4 protein expression by antibodies.

Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions.

ERj1p uses a universal ribosomal adaptor site to coordinate the 80S ribosome at the membrane.

ERj1p has a basic role in protein biogenesis at the endoplasmic reticulum.

Genomic and expression analysis of the 3q25-q26 amplification unit reveals TLOC1/SEC62 as a probable target gene in prostate cancer.

The nucleotide exchange factor activity of Grp170 may explain the non-lethal phenotype of loss of Sil1 function in man and mouse.

Protein transport into the endoplasmic reticulum: mechanisms and pathologies.

The heat shock protein 70 molecular chaperone network in the pancreatic endoplasmic reticulum - a quantitative approach.

A novel twist to protein secretion in eukaryotes.

Lanthanum ions inhibit the mammalian Sec61 complex in its channel dynamics and protein transport activity.

Analysis of the membrane proteome of canine pancreatic rough microsomes identifies a novel Hsp40, termed ERj7.

The ER-membrane-resident Hsp40 ERj1 is a novel substrate for protein kinase CK2.

Evolutionary gain of function for the ER membrane protein Sec62 from yeast to humans.

The mammalian and yeast translocon complexes comprise a characteristic Sec61 channel.

Protein translocation across the ER membrane.

Silencing of the SEC62 gene inhibits migratory and invasive potential of various tumor cells.

BiP modulates the affinity of its co-chaperone ERj1 for ribosomes.

Interaction of calmodulin with Sec61α limits Ca2+ leakage from the endoplasmic reticulum.

Sec62 protein level is crucial for the ER stress tolerance of prostate cancer.

An interaction between human Sec63 and nucleoredoxin may provide the missing link between the SEC63 gene and polycystic liver disease.

Sec61 complexes form ubiquitous ER Ca2+ leak channels.

Sec62 protein level is crucial for the ER stress tolerance of prostate cancer.

Calmodulin regulation of the calcium-leak channel Sec61 is unique to vertebrates.

Functional characterization of the essential tail anchor of the herpes simplex virus type 1 nuclear egress protein pUL34.

Introduction of an implant surgical selective into a predoctoral dental curriculum.

Ca2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane.

Sec62 bridges the gap from 3q amplification to molecular cell biology in non-small cell lung cancer.