William M Clemons

American structural biologist

DBpedia resource is: http://dbpedia.org/resource/Bil_Clemons

Abstract is: William "Bil" Clemons, Jr. is an American structural biologist and Professor of Biochemistry at Caltech. He is best known for his work solving the atomic structure of the ribosome with dissertation advisor, Nobel Prize winner in Chemistry, Venki Ramakrishnan. He is also known for his work on the structure and function of proteins involved in membrane translocation and docking of proteins, including the membrane protein translocation channel SecY, chaperones involved in the targeting of tail-anchored membrane proteins in the Get pathway, and signal recognition proteins of the Twin-arginine translocation pathway. He was elected a member of the National Academy of Sciences in 2022.

William M Clemons is …
instance of (P31):
humanQ5

External links are
P2671Google Knowledge Graph ID/g/11f0zbnzlg
P496ORCID iD0000-0002-0021-889X

P184doctoral advisorVenkatraman RamakrishnanQ60061
P69educated atUniversity of UtahQ168515
Virginia TechQ65379
P108employerHarvard Medical SchoolQ49121
California Institute of TechnologyQ161562
P734family nameClemonsQ16865624
ClemonsQ16865624
ClemonsQ16865624
P8017generational suffixL252247-F2
P735given nameWilliamQ12344159
WilliamQ12344159
BilQ16420918
BilQ16420918
P106occupationresearcherQ1650915
P21sex or gendermaleQ6581097

Reverse relations

author (P50)
Q27671664A Structural Model of the Sgt2 Protein and Its Interactions with Chaperones and the Get4/Get5 Complex
Q35671370A cationic cysteine-hydrazide as an enrichment tool for the mass spectrometric characterization of bacterial free oligosaccharides
Q30776655A large conformational change of the translocation ATPase SecA
Q27627164Another piece of the ribosome: solution structure of S16 and its location in the 30S subunit
Q24311324Bag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domain
Q41176486Capturing the signal
Q35860419Chemoenzymatic syntheses of water-soluble lipid I fluorescent probes
Q42466858Comprehensive proteomic profiling of outer membrane vesicles from Campylobacter jejuni
Q27683285Crystal structure of ATP-bound Get3–Get4–Get5 complex reveals regulation of Get3 by Get4
Q27630228Crystal structure of an initiation factor bound to the 30S ribosomal subunit
Q49203495Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: purification, crystallization and structure determination.
Q56396627Crystal structure of the 30 s ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 s RNA
Q27619724Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 A resolution: evidence for the mechanism of signal peptide binding
Q30164044Crystal structure of the long-chain fatty acid transporter FadL.
Q57820386Decoding sequence-level information to predict membrane protein expression
Q36321596Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY.
Q36281546Expression, purification, and crystallography of the conserved methionine-rich domain of human signal recognition particle 54 kDa protein.
Q27627265Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
Q27676804Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex
Q46586317Improving membrane protein expression by optimizing integration efficiency.
Q36444249Mechanism of Assembly of a Substrate Transfer Complex during Tail-anchored Protein Targeting
Q42072783Minimal requirements for inhibition of MraY by lysis protein E from bacteriophage ΦX174.
Q27657172Model for eukaryotic tail-anchored protein binding based on the structure of Get3
Q34048338Modeling the effects of prl mutations on the Escherichia coli SecY complex
Q112585997Molecular basis of tail-anchored integral membrane protein recognition by the cochaperone Sgt2
Q35566027Phasing the 30S ribosomal subunit structure.
Q36835510Precise timing of ATPase activation drives targeting of tail-anchored proteins
Q27649425Ribosome binding of a single copy of the SecY complex: implications for protein translocation
Q125343630Sequence‐based features that are determinant for tail‐anchored membrane protein sorting in eukaryotes
Q27662391Structural characterization of the Get4/Get5 complex and its interaction with Get3
Q35863872Structural insight into the protein translocation channel
Q27619576Structure of a bacterial 30S ribosomal subunit at 5.5 A resolution
Q27656871Structure of the twin-arginine signal-binding protein DmsD fromEscherichia coli
Q27675050Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface
Q91458924Substrate Tolerance of Bacterial Glycosyltransferase MurG: Novel Fluorescence-Based Assays
Q27675864Tail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologue
Q27677349The Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine Translocation
Q112586452The STI1-domain is a flexible alpha-helical fold with a hydrophobic groove
Q35986793The complex process of GETting tail-anchored membrane proteins to the ER.
Q125900270The mechanism of the phage-encoded protein antibiotic from ΦX174
Q57820381The structural basis for regulation of the nucleo-cytoplasmic distribution of Bag6 by TRC35
Q24320201USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation
Q41607871Ultrastructure and complex polar architecture of the human pathogen Campylobacter jejuni.
Q27642744X-ray structure of a protein-conducting channel

Q60061Venkatraman Ramakrishnandoctoral studentP185

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