1. Volume 122, Issue 7, Pages 1878-1885 (June 2002)
Molecular misreading of the ubiquitin B gene and hepatic mallory body formation 
Laron W. McPhaul, Jun Wang, Elly M. Hol, Marc A.F. Sonnemans, Nora Riley, Victoria Nguyen, Qi Xiao Yuan, Yan–He Lue, Fred W. van Leeuwen, Samuel W. French 
Gastroenterology 
Volume 122, Issue 7, Pages (June 2002)
DOI: /gast
Copyright © 2002 American Gastroenterological Association Terms and Conditions

2. Fig. 1
(A) Wild-type Ub and (B) UBB+1 immunoreactivity in a MB-containing autopsied liver (subject 7) probed with wild-type Ub antibody 3-39 and UBB+1 antibody, respectively (original magnification 220×). Note that straight arrows indicate the same MB-containing cell and curved arrows indicate the same central vein present in each photomicrograph.
Gastroenterology  , DOI: ( /gast )
Copyright © 2002 American Gastroenterological Association Terms and Conditions

3. Fig. 2
Confocal microscopy of a MB-containing liver (subject 5) double immunostained with wild-type Ub (A, green) or UBB+1 (B, red) or both (C, yellow) (original magnification 2500×).
Gastroenterology  , DOI: ( /gast )
Copyright © 2002 American Gastroenterological Association Terms and Conditions

4. Fig. 3
Positive immunogold staining of isolated MB fraction using UBB+1 antibody (original magnification 100,000×). Note that the arrows indicate immunogold-labeled MB filaments (type II MB).
Gastroenterology  , DOI: ( /gast )
Copyright © 2002 American Gastroenterological Association Terms and Conditions

5. Fig. 4
Western blot analysis showing UBB+1 expression in liver homogenate. The molecular weight of the protein standard (in kilodaltons) is on the left. UBB+1 present in liver homogenate has the same molecular weight (11 kilodaltons) as recombinant-UBB+1 (rec-UBB+1) produced in E. coli. The higher-molecular-weight bands are background bands.
Gastroenterology  , DOI: ( /gast )
Copyright © 2002 American Gastroenterological Association Terms and Conditions

6. Fig. 5
Sequence gel showing a GT deletion in cloned Ub transcripts in a human liver (right) when compared with cloned wild-type Ub transcript (left), indicating a GU deletion in RNA.
Gastroenterology  , DOI: ( /gast )
Copyright © 2002 American Gastroenterological Association Terms and Conditions

7. Fig. 6
Postulated role of UBB+1 in MB formation. In the normal process of protein degradation (on the left), conformationally altered cytokeratin filaments in hepatocytes are hyperphosphorylated and ubiquitinated before degradation by the 26S proteasome pathway of intracellular proteolysis of aberrant proteins. A chain of 4 Ub proteins is the minimum signal for efficient targeting to the proteasome.16 UBB+1 is a substrate for ubiquitination, ubiquitinated UBB+1 is refractory to deubiquitination, and ubiquitinated UBB+1 can inhibit the proteasome in a dominant-negative fashion.6,21 Consequently, polyubiquitinated cytokeratins are less efficiently degraded, and (on the right) ubiquitinated and phosphorylated cytokeratins accumulate with ubiquitinated UBB+1, forming MBs.
Gastroenterology  , DOI: ( /gast )
Copyright © 2002 American Gastroenterological Association Terms and Conditions