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

Por Krukenberg, Kristin A, Böttcher, Ulrike M K, Southworth, Daniel R, Agard, David A
Publicado em 2009

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

Por Siegers, Katja, Bölter, Bettina, Schwarz, Juliane P., Böttcher, Ulrike M.K., Guha, Suranjana, Hartl, F.Ulrich
Publicado em 2003

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

Por Grallath, Silke, Schwarz, Juliane P, Böttcher, Ulrike M K, Bracher, Andreas, Hartl, F Ulrich, Siegers, Katja
Publicado em 2006

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

Por Siegers, Katja, Bölter, Bettina, Schwarz, Juliane P, Böttcher, Ulrike M K, Guha, Suranjana, Hartl, F Ulrich
Publicado em 2008

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

Por Grallath, Silke, Schwarz, Juliane P., Böttcher, Ulrike M.K., Bracher, Andreas, Hartl, F. Ulrich, Siegers, Katja
Publicado em 2007