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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
6  on kidney cancer tumor suppressors, such as von Hippel-Lindau protein and folliculin.
7 pha, and reducing HIF2alpha affinity for the von Hippel-Lindau protein and its degradation.
8 us (KSHV) targets the HIF-1alpha suppressors von Hippel-Lindau protein and p53 for degradation via it
9                   The tumor suppressors VHL (von Hippel-Lindau protein) and p53 target HIF-1alpha for
10 he identification of loss of function of the von Hippel-Lindau protein as the basis for clear cell RC
11                                Because pVHL (von Hippel-Lindau protein) directs the proteolysis of Hi
12  of HIF-alpha increases its affinity for the von Hippel Lindau protein elongin B/C (VCB) ubiquitin li
13                               In additional, von Hippel-Lindau protein expression was significantly i
14 pha is constitutively ubiquitinated by pVHL (von Hippel-Lindau protein) followed by proteasomal degra
15 ed, providing clues as to how disruptions in von Hippel-Lindau protein function may result in eye dis
16 y, KLF2 promoted HIF-1alpha degradation in a von Hippel-Lindau protein-independent but proteasome-dep
17 man-brain library with D2 as bait identified von Hippel-Lindau protein-interacting deubiquitinating e
18                    The tumor suppressor VHL (von Hippel-Lindau) protein is a substrate receptor for U
19  current understanding of the biology of the von Hippel-Lindau protein, its role in the pathophysiolo
20 conditions via the prolyl hydroxylase domain/von Hippel-Lindau protein pathway.
21                                              Von Hippel Lindau protein (pVHL) and hypoxia inducible f
22     We find that GCs limit the expression of Von Hippel Lindau protein (pVHL), a negative regulator o
23 F1alpha expression through downregulation of von Hippel Lindau protein (pVHL).
24                                          The von Hippel-Lindau protein (pVHL) bound directly to hydro
25 ronectin coimmunoprecipitated with wild-type von Hippel-Lindau protein (pVHL) but not tumor-derived p
26 so preferentially interacted with PHD1-3 and von Hippel-Lindau protein (pVHL) during normoxia but not
27                          Inactivation of the von Hippel-Lindau protein (pVHL) has been implicated in
28 f previous observations that deletion of the von Hippel-Lindau protein (pVHL) in juxtaglomerular (JG)
29 a-inducible factor (HIF)-alpha proteins, and von Hippel-Lindau protein (pVHL) in mouse folic acid nep
30  role for prolyl hydroxylation and resultant von Hippel-Lindau protein (pVHL) interactions in the ubi
31                         The tumor suppressor von Hippel-Lindau protein (pVHL) is critical for cellula
32                                          The von Hippel-Lindau protein (pVHL) is the substrate recogn
33                                          The von Hippel-Lindau protein (pVHL) mediates the ubiquitina
34 e, HIF-1 hydroxylation, and interaction with von Hippel-Lindau protein (pVHL), resulting in HIF-1alph
35             A key regulator of HIF-1alpha is von Hippel-Lindau protein (pVHL), which mediates the oxy
36         Fusion of the seven amino acids to a Von Hippel-Lindau protein (pVHL)-binding ligand (which s
37 nhances the ubiquitylation of HIF1alpha by a von Hippel-Lindau protein (pVHL)-dependent mechanism.
38 onectin and collagen network is regulated by von Hippel-Lindau protein (pVHL).
39 lyubiquitination by a complex containing the von Hippel-Lindau protein (pVHL).
40 e HIF, resulting in high-affinity binding to Von Hippel-Lindau protein (pVHL).
41 associated with the germline mutation of the von Hippel-Lindau protein (pVHL).
42                    The tumor suppressor VHL (von Hippel-Lindau protein) serves as a negative regulato
43 elaboration of the neurobiologic role of the von Hippel-Lindau protein, the mainstay of management re
44                     Nanobody A5 was fused to Von Hippel-Lindau protein to generate a PROTAC that degr
45           We used mice lacking cardiac pVHL (von Hippel-Lindau protein) to investigate how chronic HI
46                Mgr interacts with Drosophila von Hippel Lindau protein (Vhl).
47                                              Von Hippel-Lindau protein (VHL) is the E3 ubiquitin liga
48 mplex formation and degradation by employing von Hippel-Lindau protein (VHL) recruiting PROTACs for t
49 F-1 alpha regulates its interaction with the von Hippel-Lindau protein (VHL) that targets HIF-1 alpha
50                  The Vhlh gene codes for the von Hippel-Lindau protein (VHL), a tumor suppressor that
51 ith cardiac myocyte-specific deletion of the von Hippel-Lindau protein (VHL), an essential component
52 roxylase PHD2 is required for binding of the von Hippel-Lindau protein (VHL), leading to ubiquitinati
53 lation, which is required for binding of the von Hippel-Lindau protein (VHL), the recognition compone
54 rated the first small molecule targeting the von Hippel-Lindau protein (VHL), the substrate recogniti
55 xylation promotes binding of HIFalpha to the von Hippel-Lindau protein (VHL)-elongin B/C complex, thu
56 e chaperone requirements for assembly of the von Hippel-Lindau protein (VHL)-elongin BC (VBC) tumor s
57 droxylation leading to ubiquitination by the von Hippel-Lindau protein (VHL)-Elongin C ubiquitin-liga
58 a subunit is mediated by prolyl hydroxylase, von Hippel-Lindau protein (VHL)/Elongin-C E3 ubiquitin l
59 hrough Pax8-rtTA-based inducible knockout of von Hippel-Lindau protein (VHL-KO), protects from rhabdo
60 g an additional TRiC-binding domain from the von Hippel-Lindau protein (vTBD), at the N-terminus of S
61 reduced and the pattern of expression of the von Hippel-Lindau protein was aberrant.