about
Molecular architecture of human polycomb repressive complex 2Multivalent Microtubule Recognition by Tubulin Tyrosine Ligase-like Family Glutamylases.The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits.Cryo-electron microscopy structure of the TRPV2 ion channelCrystal Structure of Group II Chaperonin in the Open StateHigh-Resolution Microtubule Structures Reveal the Structural Transitions in αβ-Tubulin upon GTP HydrolysisA novel cereblon modulator recruits GSPT1 to the CRL4(CRBN) ubiquitin ligaseStructural organization of the dynein-dynactin complex bound to microtubulesConformational switching of the 26S proteasome enables substrate degradationFunctional annotation of the Arabidopsis genome using controlled vocabulariesAppion: an integrated, database-driven pipeline to facilitate EM image processingIsolation of yeast complex IV in native lipid nanodiscs.Subunits fold at position-dependent rates during maturation of a eukaryotic RNA virus.Structures of the RNA-guided surveillance complex from a bacterial immune system.Automated cryoEM data acquisition and analysis of 284742 particles of GroEL.A test-bed for optimizing high-resolution single particle reconstructions.Ab initio maximum likelihood reconstruction from cryo electron microscopy images of an infectious virion of the tailed bacteriophage P22 and maximum likelihood versions of Fourier Shell Correlation appropriate for measuring resolution of spherical oA toolbox for ab initio 3-D reconstructions in single-particle electron microscopy.Solid-to-fluid-like DNA transition in viruses facilitates infection.Molecular architecture and connectivity of the budding yeast Mtw1 kinetochore complexThe proteasome under the microscope: the regulatory particle in focusPeering down the barrel of a bacteriophage portal: the genome packaging and release valve in p22Genomic and functional analysis of Vibrio phage SIO-2 reveals novel insights into ecology and evolution of marine siphovirusesUbp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome.Architecture of the Complex Formed by Large and Small Terminase Subunits from Bacteriophage P22.Thermodynamic Interrogation of the Assembly of a Viral Genome Packaging Motor Complex.Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition.DNA bending-induced phase transition of encapsidated genome in phage λ.Bacteriophage lambda stabilization by auxiliary protein gpD: timing, location, and mechanism of attachment determined by cryo-EM.VIPERdb2: an enhanced and web API enabled relational database for structural virologyThe P22 tail machine at subnanometer resolution reveals the architecture of an infection conduit.Drosophila A virus is an unusual RNA virus with a T=3 icosahedral core and permuted RNA-dependent RNA polymerase.Structure Reveals Mechanisms of Viral Suppressors that Intercept a CRISPR RNA-Guided Surveillance Complex.Capsid conformational sampling in HK97 maturation visualized by X-ray crystallography and cryo-EM.Site-specific labeling of proteins for electron microscopy.Achieving better-than-3-Å resolution by single-particle cryo-EM at 200 keV.Structure of the cold- and menthol-sensing ion channel TRPM8.The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading.Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing.Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility.
P50
Q21128799-E39D9AE3-5BBC-4850-95D6-52E476F82DFEQ24337446-FAA765ED-4EBC-46B0-A53E-1DBBB5AED179Q27309735-61836BB4-38E4-4EBE-B415-FC0CB925E4DBQ27310168-3D43143B-57F1-42FC-A20F-011A689E9A8CQ27665033-8CFC27B9-005D-4405-8F82-1FA88B43DB54Q27683920-22C1513D-D7BD-4CDF-A804-0D9856EE845CQ27713259-794F7DEB-F1D6-4B6D-BC9B-EFBFDC588820Q28258499-6D99CEA2-4FC4-4C3D-A67B-645D2C5EC2D4Q28292908-E7D14DBF-1A9E-409E-805A-AAD89BCCACFAQ28770139-76B61A97-280E-4BFA-95EE-DF94CB84214FQ29614288-A0852BF6-915B-4866-9F49-FB53AD095C95Q30268455-D1B7D412-29B1-4871-83A7-417121F3FE17Q30496113-C61D309E-0C50-4EFA-A99A-ED7D594F8C35Q30587075-3264A2FE-DED6-421A-BD30-95E0F6C9FC5CQ31043729-F9519751-E053-4814-870F-8DF7BA1A3256Q33340907-40DB4642-B6E3-4FCE-9402-9B3233575B14Q33578290-5CE6387E-69AF-4D7C-A264-2B3F5A99FE58Q33679077-3B7D6537-8D3A-424C-A6B3-C37752910B1AQ34383696-28F1A708-C96A-47B5-92DC-E785074F75D1Q34474300-DE6C1B62-DC7F-46FB-8D9E-4CEFE4F8B587Q34623947-6CC7DB68-89F7-4516-92C3-B3C8FFD51EE3Q34785823-65B6FB24-A587-4393-9907-6572BE5322A0Q35918719-8198DC1E-4CFC-41A1-AD5B-85598A4EA021Q36029605-58301D50-1B14-4A54-B26C-7689D32D1830Q36103946-EC6DB943-B8C7-4861-9ABD-A16AD993E3A4Q36219330-AB848320-3D56-49CB-B908-A06DBB10AE16Q36568548-5129322D-3A0F-42BB-9826-E0B41D09611EQ36783615-6C3A0CF5-6702-4953-AB50-C07D2498D80DQ37037993-B0540072-391A-4B4A-9D54-B236ABCCDA57Q37202425-68606649-52BB-4D2D-8CF3-409DBE312FC8Q37272297-E88592B8-8DC9-4F53-AAEA-11D2DCB545B6Q37342983-90B19E2E-F27D-4850-9E49-25759948E5A8Q38878360-E0FD303A-A4A5-4F80-A256-DF2594F9527DQ41625342-96FA54DC-F2E3-478B-B0AB-6274C69D9C2CQ42611137-EC51E052-1290-49BB-B3D0-229F8CA314E5Q46569001-A8583331-A9F3-4C36-8687-BDC374488F4CQ48156868-779EBA93-AF14-4534-B985-C6718EDF8102Q48267632-4E804594-C6C2-4FB2-BE1B-0DE7B0AFB67CQ48373223-152FF741-10AC-4C2C-B515-DA0174748890Q50129794-DAF46FF6-4CCF-44A9-89BF-6B3A29F8AFAA
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Gabriel C. Lander
@ast
Gabriel C. Lander
@en
Gabriel C. Lander
@es
Gabriel C. Lander
@nl
Gabriel C. Lander
@sl
type
label
Gabriel C. Lander
@ast
Gabriel C. Lander
@en
Gabriel C. Lander
@es
Gabriel C. Lander
@nl
Gabriel C. Lander
@sl
prefLabel
Gabriel C. Lander
@ast
Gabriel C. Lander
@en
Gabriel C. Lander
@es
Gabriel C. Lander
@nl
Gabriel C. Lander
@sl
P106
P108
P1153
8877122600
P21
P31
P496
0000-0003-4921-1135