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1 a peptide ligand for the E3 ubiquitin ligase von Hippel Lindau protein.
2 ted genes for HIF-1alpha, HIF-2alpha, or the von Hippel-Lindau protein.
3 tional activation was partially inhibited by von Hippel-Lindau protein.
4 T heterodimer), proline hydroxylase, and the von Hippel-Lindau protein.
5 This provides a recognition motif for the von Hippel Lindau protein, a component of an E3 ubiquiti
7 us (KSHV) targets the HIF-1alpha suppressors von Hippel-Lindau protein and p53 for degradation via it
9 he identification of loss of function of the von Hippel-Lindau protein as the basis for clear cell RC
11 of HIF-alpha increases its affinity for the von Hippel Lindau protein elongin B/C (VCB) ubiquitin li
13 pha is constitutively ubiquitinated by pVHL (von Hippel-Lindau protein) followed by proteasomal degra
14 ed, providing clues as to how disruptions in von Hippel-Lindau protein function may result in eye dis
15 y, KLF2 promoted HIF-1alpha degradation in a von Hippel-Lindau protein-independent but proteasome-dep
16 man-brain library with D2 as bait identified von Hippel-Lindau protein-interacting deubiquitinating e
18 current understanding of the biology of the von Hippel-Lindau protein, its role in the pathophysiolo
20 We find that GCs limit the expression of Von Hippel Lindau protein (pVHL), a negative regulator o
22 ronectin coimmunoprecipitated with wild-type von Hippel-Lindau protein (pVHL) but not tumor-derived p
23 so preferentially interacted with PHD1-3 and von Hippel-Lindau protein (pVHL) during normoxia but not
25 f previous observations that deletion of the von Hippel-Lindau protein (pVHL) in juxtaglomerular (JG)
26 a-inducible factor (HIF)-alpha proteins, and von Hippel-Lindau protein (pVHL) in mouse folic acid nep
27 role for prolyl hydroxylation and resultant von Hippel-Lindau protein (pVHL) interactions in the ubi
31 e, HIF-1 hydroxylation, and interaction with von Hippel-Lindau protein (pVHL), resulting in HIF-1alph
33 nhances the ubiquitylation of HIF1alpha by a von Hippel-Lindau protein (pVHL)-dependent mechanism.
38 elaboration of the neurobiologic role of the von Hippel-Lindau protein, the mainstay of management re
41 F-1 alpha regulates its interaction with the von Hippel-Lindau protein (VHL) that targets HIF-1 alpha
43 ith cardiac myocyte-specific deletion of the von Hippel-Lindau protein (VHL), an essential component
44 roxylase PHD2 is required for binding of the von Hippel-Lindau protein (VHL), leading to ubiquitinati
45 lation, which is required for binding of the von Hippel-Lindau protein (VHL), the recognition compone
46 rated the first small molecule targeting the von Hippel-Lindau protein (VHL), the substrate recogniti
47 xylation promotes binding of HIFalpha to the von Hippel-Lindau protein (VHL)-elongin B/C complex, thu
48 e chaperone requirements for assembly of the von Hippel-Lindau protein (VHL)-elongin BC (VBC) tumor s
49 droxylation leading to ubiquitination by the von Hippel-Lindau protein (VHL)-Elongin C ubiquitin-liga
50 a subunit is mediated by prolyl hydroxylase, von Hippel-Lindau protein (VHL)/Elongin-C E3 ubiquitin l
51 hrough Pax8-rtTA-based inducible knockout of von Hippel-Lindau protein (VHL-KO), protects from rhabdo
52 g an additional TRiC-binding domain from the von Hippel-Lindau protein (vTBD), at the N-terminus of S
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