about
Bag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domainUSP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradationStructure of a bacterial 30S ribosomal subunit at 5.5 A resolutionCrystal structure of the conserved subdomain of human protein SRP54M at 2.1 A resolution: evidence for the mechanism of signal peptide bindingAnother piece of the ribosome: solution structure of S16 and its location in the 30S subunitFunctional insights from the structure of the 30S ribosomal subunit and its interactions with antibioticsCrystal structure of an initiation factor bound to the 30S ribosomal subunitX-ray structure of a protein-conducting channelRibosome binding of a single copy of the SecY complex: implications for protein translocationStructure of the twin-arginine signal-binding protein DmsD fromEscherichia coliModel for eukaryotic tail-anchored protein binding based on the structure of Get3Structural characterization of the Get4/Get5 complex and its interaction with Get3A Structural Model of the Sgt2 Protein and Its Interactions with Chaperones and the Get4/Get5 ComplexStructures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic InterfaceTail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologueGet5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 ComplexThe Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine TranslocationCrystal structure of ATP-bound Get3–Get4–Get5 complex reveals regulation of Get3 by Get4Crystal structure of the long-chain fatty acid transporter FadL.A large conformational change of the translocation ATPase SecAModeling the effects of prl mutations on the Escherichia coli SecY complex.Phasing the 30S ribosomal subunit structure.A cationic cysteine-hydrazide as an enrichment tool for the mass spectrometric characterization of bacterial free oligosaccharidesChemoenzymatic syntheses of water-soluble lipid I fluorescent probes.Structural insight into the protein translocation channel.The complex process of GETting tail-anchored membrane proteins to the ER.Expression, purification, and crystallography of the conserved methionine-rich domain of human signal recognition particle 54 kDa protein.Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY.Mechanism of Assembly of a Substrate Transfer Complex during Tail-anchored Protein Targeting.Precise timing of ATPase activation drives targeting of tail-anchored proteins.Capturing the signalUltrastructure and complex polar architecture of the human pathogen Campylobacter jejuni.Minimal requirements for inhibition of MraY by lysis protein E from bacteriophage ΦX174.Comprehensive proteomic profiling of outer membrane vesicles from Campylobacter jejuni.Improving membrane protein expression by optimizing integration efficiency.Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: purification, crystallization and structure determination.Crystal structure of the 30 s ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 s RNAThe structural basis for regulation of the nucleo-cytoplasmic distribution of Bag6 by TRC35Decoding sequence-level information to predict membrane protein expressionSubstrate Tolerance of Bacterial Glycosyltransferase MurG: Novel Fluorescence-Based Assays
P50
Q24311324-1B59582F-F6EB-4C94-BF0A-9FE0FACB7E2DQ24320201-969E1D0E-7C95-4699-A26F-8FC67E579C96Q27619576-0B938C04-9478-4CDF-8F5D-3454FDD32826Q27619724-9A56865B-81A9-4468-8714-A2860E1A8DC2Q27627164-82FA42C5-4ED2-4E26-BA46-31ED482BD0FBQ27627265-0B13EACA-5D5F-4B1E-B330-F7B543BA36C1Q27630228-32C22FFB-3E50-4291-8873-BFD6D2C430A8Q27642744-330C2058-6329-4F98-A235-B218A3F3A9C5Q27649425-B035EBEB-8863-42B1-B250-9B138DF706A1Q27656871-4336843C-A63E-4651-A7CC-FC31DE86670BQ27657172-94097241-8793-4892-8A97-0682B2B5BE7FQ27662391-8198071B-1F4E-4A5B-8528-14F9541BC8D8Q27671664-EB14ECC3-BE1E-4B9E-AB2C-03DCCAF0AA69Q27675050-56BAF024-1D66-42DA-9343-B6EACE99D2EBQ27675864-9D837481-A295-4712-854A-F9B6B77DFF7CQ27676804-ED763AF1-4DAD-4381-847D-B7CB5792FBB5Q27677349-5BDA753E-0A4A-4A91-8446-D052039771FFQ27683285-BDB834D4-A7AE-4A18-960B-84707A4B0812Q30164044-98CAE048-28A4-4610-93F5-D0A7B6B1B5DCQ30776655-FDE99A28-4A2F-430A-A938-4F8216F48B80Q34048338-B3073789-AD16-4AE4-AC36-DB4EEC22AF3DQ35566027-F73F2B6A-955A-47A4-AC67-353745D674E9Q35671370-BE7087B5-29FB-4A9A-B340-D9EC8F99DDB7Q35860419-A14D4962-1189-4029-9C01-316CD6DF3224Q35863872-DCA88FD5-7B79-4974-8764-F6914B98F0A2Q35986793-475E7AA7-C5B8-487C-80F5-4A4E07F91899Q36281546-C0693F4C-4F49-4ABE-82D1-0114481FCC4CQ36321596-EA6534BA-87AD-4FDD-8586-5FCFD158704BQ36444249-E9BD21D0-8B93-4BE8-B900-9E844868680BQ36835510-E2F2761F-2D85-4AEB-BAD1-C9AE717201EAQ41176486-31586DA8-50C6-4C5D-84DA-AC8C2E4B4196Q41607871-0E416A39-1C1B-4B60-B0DD-10AE9DBF25C7Q42072783-F8EEA633-ECE9-44A4-9DFF-16E4FF83A392Q42466858-3FBA6EB1-60BE-4F0C-9761-468D050374D0Q46586317-C9D61A7F-02D0-4411-88FC-C18F3661EB94Q49203495-2D2908FA-9A14-4095-ACD6-5DA70BBEA66FQ56396627-1BD0BE67-95F7-4581-AFE0-6573E98AA691Q57820381-F82B3322-94CA-4283-A561-F42BC9A4290BQ57820386-219CF209-6EAA-4FF1-8882-E4222BD8B9C1Q91458924-918B2F3B-4BD7-4D7E-9FDF-5387D0A884D2
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
William M Clemons
@ast
William M Clemons
@en
William M Clemons
@es
William M Clemons
@nl
William M Clemons
@sl
type
label
William M Clemons
@ast
William M Clemons
@en
William M Clemons
@es
William M Clemons
@nl
William M Clemons
@sl
altLabel
Jr. William Clemons
@en
prefLabel
William M Clemons
@ast
William M Clemons
@en
William M Clemons
@es
William M Clemons
@nl
William M Clemons
@sl
P106
P21
P31
P496
0000-0002-0021-889X