Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity - Test2 - elhamkhani - TriplyDB

Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity

Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity

http://www.wikidata.org/entity/Q27681114

about

An in cellulo-derived structure of PAK4 in complex with its inhibitor Inka1 Signaling, Regulation, and Specificity of the Type II p21-activated Kinases Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases Innate immunity kinase TAK1 phosphorylates Rab1 on a hotspot for posttranslational modifications by host and pathogen The Tribbles 2 (TRB2) pseudokinase binds to ATP and autophosphorylates in a metal-independent manner Rational Redesign of a Functional Protein Kinase-Substrate Interaction.MOB1 Mediated Phospho-recognition in the Core Mammalian Hippo Pathway.Global analysis of human nonreceptor tyrosine kinase specificity using high-density peptide microarrays.Architecture and mechanism of the central gear in an ancient molecular timer.The C2 Domain and Altered ATP-Binding Loop Phosphorylation at Ser³⁵⁹ Mediate the Redox-Dependent Increase in Protein Kinase C-δ Activity Identification and classification of small molecule kinases: insights into substrate recognition and specificity.Characterization of the Catalytic and Nucleotide Binding Properties of the α-Kinase Domain of Dictyostelium Myosin-II Heavy Chain Kinase A Kinome-wide decoding of network-attacking mutations rewiring cancer signaling.Gain-of-function mutations in protein kinase Cα (PKCα) may promote synaptic defects in Alzheimer's disease Revisiting protein kinase-substrate interactions: Toward therapeutic development.Unmasking determinants of specificity in the human kinome.Ancestral resurrection reveals evolutionary mechanisms of kinase plasticity.Identification of non-Ser/Thr-Pro consensus motifs for Cdk1 and their roles in mitotic regulation of C2H2 zinc finger proteins and Ect2.Discovery of new substrates of the elongation factor-2 kinase suggests a broader role in the cellular nutrient response.Distinct kinetics of serine and threonine dephosphorylation are essential for mitosis.PAK4 crystal structures suggest unusual kinase conformational movements.Identification of PNG kinase substrates uncovers interactions with the translational repressor TRAL in the oocyte-to-embryo transition.Water-mediated conformational preselection mechanism in substrate binding cooperativity to protein kinase A.Homing in: Mechanisms of Substrate Targeting by Protein Kinases.Dynamics of human protein kinase Aurora A linked to drug selectivity

P2860

Q27320133-0F441EF9-ECD7-407A-9E8C-16FC6FFCFA12 Q28083745-6C5B6C73-6EB7-420E-9F3E-8D813A538D26 Q28270556-1CEB9BA6-BF6C-4D76-A165-4344EE02C1EA Q28829229-6646B618-D1FE-403E-BA6C-BB128221054C Q28834261-8F16A7B9-C754-4C79-B26F-C0FF62F0C41F Q33721699-A86FFF07-3E81-4BF3-B720-45C5005A166C Q33771033-A4AFD74C-0BB4-496B-85B3-B788EA1C4272 Q34286045-00184021-84BA-4B9C-A936-7D540640CABC Q34553873-9438E89A-0149-4CD1-B950-27273A362BE0 Q35516520-70FF06D6-92D0-4AA7-AAB5-525E4AD301F2 Q35887323-5A1F2485-E068-4F85-AEEA-EE1B5999ADDF Q36092952-56F2ACC3-B561-4516-9366-C576E04DBA30 Q36278233-8A949D08-9EB0-4C60-A384-488618BF85AE Q37499816-BC114B89-C122-438D-8D7D-3945F7A98DFA Q38789563-8EE40B9F-B31F-4EAF-AEDB-DEBA83913485 Q41950534-6144973C-8817-48A5-9956-D7A4AC555544 Q42100110-83CFAF85-F9E2-415E-BF01-59D255A8DBCE Q42112278-74A099E2-4947-4FAF-9FC1-7A100FF19954 Q47142189-D2FB4FB5-739C-4421-80CE-974672FC1923 Q47588118-19AAC17A-2C68-4464-A9E9-7DA16B01F0FB Q47675076-4D074A7A-33EA-478F-8F0E-9DEF659284C9 Q50421891-EFD5D7C4-6FD6-4D9F-B3BB-CF22F9CE2497 Q52629614-D24F903B-EC82-4FC3-8309-C0C1D36F9D70 Q52653566-1DF61633-5968-4E13-9061-3745F1F7BFC0 Q56889888-49994C1E-CE6C-49E2-A3AE-07C171873170

P2860

Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity

http://www.wikidata.org/entity/Q27681114

description

2014 nî lūn-bûn

@nan

2014 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Identification of a Major Dete ...... se Phosphoacceptor Specificity

@en

Identification of a Major Dete ...... se Phosphoacceptor Specificity

@nl

type

label

Identification of a Major Dete ...... se Phosphoacceptor Specificity

@en

Identification of a Major Dete ...... se Phosphoacceptor Specificity

@nl

prefLabel

Identification of a Major Dete ...... se Phosphoacceptor Specificity

@en

Identification of a Major Dete ...... se Phosphoacceptor Specificity

@nl

P1433

Q27681114-CDE8B10A-2BFE-4740-8F2A-2835BACD7138

P1476

Q27681114-8812C946-7B5B-438F-909C-17097DB4C7A1

P2093

Q27681114-04407E1D-8602-4423-B305-B5DB5B7D2719

Q27681114-29085243-EC57-4BE6-BB4D-09D7ABC6BCBA

Q27681114-35FBF3EF-7F34-4E34-83AF-5F471482C5BF

Q27681114-52E9D6CD-7C24-4472-91B5-B43A90F9D49E

Q27681114-60CCA4F3-A559-48F1-BC85-1DC773BC7E55

Q27681114-772B3969-494A-4C27-A1C8-827FA2F6A0CA

Q27681114-9BEA7AFC-F892-42B1-B15B-AF3C55DF510F

Q27681114-A7485C31-581F-4BF6-88F2-E3416B7A6501

Q27681114-B173D17E-649C-45D7-917C-1C824E806F62

Q27681114-E7657C2E-7F9F-4286-A516-81BC68DF3101

P2860

Q27681114-09CD78C3-55D4-4908-B556-78FB9A6479DC

Q27681114-0F5B4D5E-8545-4156-949C-1008FD402F84

Q27681114-110E7529-6896-4017-AB13-00CB04656BF4

Q27681114-125C5EC5-5D6B-479A-8C42-8355DF3FE350

Q27681114-1BC3FEC1-62BE-4ECE-B882-E712B8BF436F

Q27681114-1F3F0853-4D89-4F94-B906-8B69BD611217

Q27681114-27E8ACE5-9928-4B95-B2FC-D4B16F5862B2

Q27681114-3767F2DC-E766-4FE0-8BB3-56C056D4855A

Q27681114-4448D805-C38E-4F92-BD97-C2E7B772F278

Q27681114-4F8ED67B-2243-4A5C-987E-60FB4F1B568F

P304

Q27681114-89E4BB1B-2E90-4306-8604-6E47F9EA1B24

P31

Q27681114-F21F84CF-3FD2-4AD2-8E4C-0DB6F998CD0B

P356

Q27681114-C740EF40-F639-452F-8360-BF0FB8A56197

P433

Q27681114-1FED0EE1-266F-49A1-BFAC-E763986CA70A

P478

Q27681114-F6F1F2AA-906A-43CA-892D-C00CCE72F15C

P50

Q27681114-05CF132F-D799-44AD-A197-37A827C1CAD6

Q27681114-30E92E0A-CA90-42FE-A39F-2728A04E8D5E

Q27681114-639CAED0-9C8B-41D5-9073-32358F2A68AB

P577

Q27681114-09F415C0-D0DC-4C0D-B40A-AF9B33D5CD38

P5875

Q27681114-53A890E9-2D97-48B5-AD7F-75F33D1B8A7A

P698

Q27681114-53635416-D0BA-4C14-A068-879681DB2520

P921

Q27681114-75F7D792-0CC4-40AD-9154-C6D47AB7F458

P932

Q27681114-8E93F5DC-A639-410F-B7AB-F0B06EA89760

P356

J.MOLCEL.2013.11.013

P1433

P1476

Identification of a Major Dete ...... se Phosphoacceptor Specificity

@en

P2093

Anastasia F Thévenin

http://www.w3.org/2001/XMLSchema#string

Benjamin E Turk

http://www.w3.org/2001/XMLSchema#string

Byung Hak Ha

http://www.w3.org/2001/XMLSchema#string

Catherine Chen

http://www.w3.org/2001/XMLSchema#string

Hua Jane Lou

http://www.w3.org/2001/XMLSchema#string

Jeffrey R Peterson

http://www.w3.org/2001/XMLSchema#string

Kevin Y Yip

http://www.w3.org/2001/XMLSchema#string

Philip M Kim

http://www.w3.org/2001/XMLSchema#string

Rong Zhang

http://www.w3.org/2001/XMLSchema#string

Titus J Boggon

http://www.w3.org/2001/XMLSchema#string

P2860

PDK1, the master regulator of AGC kinase signal transduction

LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1

Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP

The protein kinase complement of the human genome

PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse

The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases

The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms

Structure and autoregulation of the insulin-like growth factor 1 receptor kinase

Crystal Structures of the p21-Activated Kinases PAK4, PAK5, and PAK6 Reveal Catalytic Domain Plasticity of Active Group II PAKs

Type II p21-activated kinases (PAKs) are regulated by an autoinhibitory pseudosubstrate

P304

140-7

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.MOLCEL.2013.11.013

http://www.w3.org/2001/XMLSchema#string

P433

1

http://www.w3.org/2001/XMLSchema#string

P478

53

http://www.w3.org/2001/XMLSchema#string

P50

Panagis Filippakopoulos

Mark Bender Gerstein

P577

2014-01-09T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

259490514

http://www.w3.org/2001/XMLSchema#string

P698

24374310

http://www.w3.org/2001/XMLSchema#string

P921

P932

3898841

http://www.w3.org/2001/XMLSchema#string