Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide

par Krukenberg, Kristin A, Böttcher, Ulrike M K, Southworth, Daniel R, Agard, David A
Publié 2009

TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes

par Siegers, Katja, Bölter, Bettina, Schwarz, Juliane P., Böttcher, Ulrike M.K., Guha, Suranjana, Hartl, F.Ulrich
Publié 2003

L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle

par Grallath, Silke, Schwarz, Juliane P, Böttcher, Ulrike M K, Bracher, Andreas, Hartl, F Ulrich, Siegers, Katja
Publié 2006

TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes

par Siegers, Katja, Bölter, Bettina, Schwarz, Juliane P, Böttcher, Ulrike M K, Guha, Suranjana, Hartl, F Ulrich
Publié 2008

L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle

par Grallath, Silke, Schwarz, Juliane P., Böttcher, Ulrike M.K., Bracher, Andreas, Hartl, F. Ulrich, Siegers, Katja
Publié 2007