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.
human | Q5 |
P2671 | Google Knowledge Graph ID | /g/11f0zbnzlg |
P496 | ORCID iD | 0000-0002-0021-889X |
P184 | doctoral advisor | Venkatraman Ramakrishnan | Q60061 |
P69 | educated at | University of Utah | Q168515 |
Virginia Tech | Q65379 | ||
P108 | employer | Harvard Medical School | Q49121 |
California Institute of Technology | Q161562 | ||
P734 | family name | Clemons | Q16865624 |
Clemons | Q16865624 | ||
Clemons | Q16865624 | ||
P8017 | generational suffix | L252247-F2 | |
P735 | given name | William | Q12344159 |
William | Q12344159 | ||
Bil | Q16420918 | ||
Bil | Q16420918 | ||
P106 | occupation | researcher | Q1650915 |
P21 | sex or gender | male | Q6581097 |
Q27671664 | A Structural Model of the Sgt2 Protein and Its Interactions with Chaperones and the Get4/Get5 Complex |
Q35671370 | A cationic cysteine-hydrazide as an enrichment tool for the mass spectrometric characterization of bacterial free oligosaccharides |
Q30776655 | A large conformational change of the translocation ATPase SecA |
Q27627164 | Another piece of the ribosome: solution structure of S16 and its location in the 30S subunit |
Q24311324 | Bag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domain |
Q41176486 | Capturing the signal |
Q35860419 | Chemoenzymatic syntheses of water-soluble lipid I fluorescent probes |
Q42466858 | Comprehensive proteomic profiling of outer membrane vesicles from Campylobacter jejuni |
Q27683285 | Crystal structure of ATP-bound Get3–Get4–Get5 complex reveals regulation of Get3 by Get4 |
Q27630228 | Crystal structure of an initiation factor bound to the 30S ribosomal subunit |
Q49203495 | Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: purification, crystallization and structure determination. |
Q56396627 | Crystal structure of the 30 s ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 s RNA |
Q27619724 | Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 A resolution: evidence for the mechanism of signal peptide binding |
Q30164044 | Crystal structure of the long-chain fatty acid transporter FadL. |
Q57820386 | Decoding sequence-level information to predict membrane protein expression |
Q36321596 | Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY. |
Q36281546 | Expression, purification, and crystallography of the conserved methionine-rich domain of human signal recognition particle 54 kDa protein. |
Q27627265 | Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics |
Q27676804 | Get5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 Complex |
Q46586317 | Improving membrane protein expression by optimizing integration efficiency. |
Q36444249 | Mechanism of Assembly of a Substrate Transfer Complex during Tail-anchored Protein Targeting |
Q42072783 | Minimal requirements for inhibition of MraY by lysis protein E from bacteriophage ΦX174. |
Q27657172 | Model for eukaryotic tail-anchored protein binding based on the structure of Get3 |
Q34048338 | Modeling the effects of prl mutations on the Escherichia coli SecY complex |
Q112585997 | Molecular basis of tail-anchored integral membrane protein recognition by the cochaperone Sgt2 |
Q35566027 | Phasing the 30S ribosomal subunit structure. |
Q36835510 | Precise timing of ATPase activation drives targeting of tail-anchored proteins |
Q27649425 | Ribosome binding of a single copy of the SecY complex: implications for protein translocation |
Q125343630 | Sequence‐based features that are determinant for tail‐anchored membrane protein sorting in eukaryotes |
Q27662391 | Structural characterization of the Get4/Get5 complex and its interaction with Get3 |
Q35863872 | Structural insight into the protein translocation channel |
Q27619576 | Structure of a bacterial 30S ribosomal subunit at 5.5 A resolution |
Q27656871 | Structure of the twin-arginine signal-binding protein DmsD fromEscherichia coli |
Q27675050 | Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface |
Q91458924 | Substrate Tolerance of Bacterial Glycosyltransferase MurG: Novel Fluorescence-Based Assays |
Q27675864 | Tail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologue |
Q27677349 | The Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine Translocation |
Q112586452 | The STI1-domain is a flexible alpha-helical fold with a hydrophobic groove |
Q35986793 | The complex process of GETting tail-anchored membrane proteins to the ER. |
Q125900270 | The mechanism of the phage-encoded protein antibiotic from ΦX174 |
Q57820381 | The structural basis for regulation of the nucleo-cytoplasmic distribution of Bag6 by TRC35 |
Q24320201 | USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation |
Q41607871 | Ultrastructure and complex polar architecture of the human pathogen Campylobacter jejuni. |
Q27642744 | X-ray structure of a protein-conducting channel |
Q60061 | Venkatraman Ramakrishnan | doctoral student | P185 |
Bil Clemons | wikipedia |
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