Evidence map›Paper›PMID 25665168›Full record

ReviewBiology2015

PDZ Domain Recognition: Insight from Human Tax-Interacting Protein 1 (TIP-1) Interaction with Target Proteins.

Smita Mohanty, Mohiuddin Ovee, Monimoy Banerjee

Open access · goldAbstract readReview
In one paragraph

Review in Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 36% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Development of a [89Zr]Zr-labeled Human Antibody using a Novel Phage-displayed Human scFv Library.Clinical cancer research : an official journal of the American Association for Cancer Research · 2024
    Article
  4. Review
  5. Blocking the functional domain of TIP1 by antibodies sensitizes cancer to radiation therapy.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023
    Article
  6. Review
  7. Targeting a Radiosensitizing Antibody-Drug Conjugate to a Radiation-Inducible Antigen.Clinical cancer research : an official journal of the American Association for Cancer Research · 2021
    Article
  8. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Smita MohantyDepartment of Chemistry, Oklahoma State University, Stillwater, OK 74078, USA. smita.mohanty@okstate.edu.
Mohiuddin OveeDepartment of Chemistry, Oklahoma State University, Stillwater, OK 74078, USA. mohiuddin.ovee@okstate.edu.
Monimoy BanerjeeDepartment of Chemistry, Oklahoma State University, Stillwater, OK 74078, USA. monimoy.banerjee@stjude.org.
Oklahoma State University · US

Funding

Molecular basis of congenital disorders of glycosylation: mechanisms of oligosachR21DK082397 · NIDDK · AUBURN UNIVERSITY AT AUBURN · PI MOHANTY, SMITA · 2009 to 2010
$528k
NIDDK NIH HHS R21 DK082397
6 · The paper itself

Abstract

Cellular signaling is primarily directed via protein-protein interactions. PDZ (PSD-95/Discs large/ZO-1 homologous) domains are well known protein-protein interaction modules involved in various key signaling pathways. Human Tax-interacting protein 1 (TIP-1), also known as glutaminase interaction protein (GIP), is a Class I PDZ domain protein that recognizes the consensus binding motif X-S/T-X-V/I/L-COOH of the C-terminus of its target proteins. We recently reported that TIP-1 not only interacts via the C-terminus of its target partner proteins but also recognizes an internal motif defined by the consensus sequence S/T-X-V/L-D in the target protein. Identification of new target partners containing either a C-terminal or internal recognition motif has rapidly expanded the TIP-1 protein interaction network. TIP-1 being composed solely of a single PDZ domain is unique among PDZ containing proteins. Since it is involved in many important signaling pathways, it is a possible target for drug design. In this mini review, we have discussed human TIP-1, its structure, mechanism of function, its interactions with target proteins containing different recognition motifs, and its involvement in human diseases. Understanding the molecular mechanisms of TIP-1 interactions with distinct target partners and their role in human diseases will be useful for designing novel therapeutics.

Identifiers

PMID25665168
PMCPMC4381219
OpenAlexW2101151590

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.