What is he best known for?
The fields of study he is best known for:
Walid A. Houry mainly investigates Biochemistry, Chaperone, Protein folding, Cell biology and Genetics.
As part of one scientific family, Walid A. Houry deals mainly with the area of Chaperone, narrowing it down to issues related to the Hsp90, and often Helicase, Protein subunit and Protein complex assembly.
His Protein folding research incorporates themes from GroEL, Foldase and HSP60.
His research in Cell biology intersects with topics in Serine protease and AAA proteins.
His Genetics research incorporates elements of Structural motif and Computational biology.
His research integrates issues of Lineage and Gene regulatory network in his study of Computational biology.
His most cited work include:
- The genetic landscape of a cell. (1828 citations)
- Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone (670 citations)
- Identification of in vivo substrates of the chaperonin GroEL. (464 citations)
What are the main themes of his work throughout his whole career to date?
His main research concerns Biochemistry, Cell biology, Chaperone, Protease and Protein folding.
His work on Escherichia coli, ATPase, AAA proteins and Plasma protein binding as part of general Biochemistry study is frequently linked to Lysine decarboxylase, bridging the gap between disciplines.
His studies deal with areas such as Heat shock protein, RUVBL2, Chromatin remodeling and R2TP complex as well as Cell biology.
His study with Chaperone involves better knowledge in Genetics.
His Gene study in the realm of Genetics connects with subjects such as Synthetic genetic array.
The study incorporates disciplines such as GroEL and Co-chaperone in addition to Protein folding.
He most often published in these fields:
- Biochemistry (36.50%)
- Cell biology (32.85%)
- Chaperone (31.39%)
What were the highlights of his more recent work (between 2018-2021)?
- Cell biology (32.85%)
- Protease (15.33%)
- Chaperone (31.39%)
In recent papers he was focusing on the following fields of study:
His primary areas of investigation include Cell biology, Protease, Chaperone, Cooperativity and Biophysics.
His Protein folding and Plasma protein binding investigations are all subjects of Cell biology research.
His Protease research is multidisciplinary, incorporating elements of Proteases, Crystal structure, Function, Microbiology and Small molecule.
His study looks at the intersection of Small molecule and topics like Anticancer drug with Biochemistry.
His biological study spans a wide range of topics, including Proteostasis and Protein domain.
His Cooperativity study combines topics from a wide range of disciplines, such as Computational biology and Trigger factor.
Between 2018 and 2021, his most popular works were:
- Mitochondrial ClpP-Mediated Proteolysis Induces Selective Cancer Cell Lethality (59 citations)
- A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery. (38 citations)
- ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores. (9 citations)
In his most recent research, the most cited papers focused on:
The scientist’s investigation covers issues in Protease, Proteostasis, Biophysics, Hydrolase and Serine protease.
He studied Protease and Proteolysis that intersect with Cancer, Respiratory chain complex, Oxidative phosphorylation, Protein folding and Function.
His work carried out in the field of Proteostasis brings together such families of science as Proteomics, Chaperone, Protein–protein interaction, Computational biology and Protein Homeostasis.
His Biophysics study integrates concerns from other disciplines, such as Protein degradation, ATP hydrolysis, Escherichia coli, Molecular machine and Structural biology.
In his study, Cell biology is strongly linked to Proteases, which falls under the umbrella field of Escherichia coli.
Walid A. Houry has researched Hydrolase in several fields, including Activator and Small molecule.
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